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2 starch + H2O
2 malto-oligosaccharides + maltose
2-chloro-4-nitrophenyl alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranoside + H2O
2-chloro-4-nitrophenol + alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranose
-
-
the increase of absorbance of 2-chloro-4-nitrophenol liberated by HSA is measured continuously at 400 nm
-
?
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside + H2O
2-chloro-4-nitrophenol + alpha-D-maltoheptaose
-
-
-
-
?
2-chloro-4-nitrophenyl alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-D-maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl alpha-D-maltotrioside + H2O
?
-
-
-
?
2-chloro-4-nitrophenyl alpha-maltotrioside + H2O
?
-
-
-
?
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside + H2O
2-chloro-4-nitrophenol + ?
pH 6.8, 30°C
-
-
?
2-chloro-4-nitrophenyl beta-D-maltoheptaoside + H2O
2-chloro-4-nitrophenol + beta-D-maltoheptaose
-
-
-
?
2-chloro-4-nitrophenyl beta-D-maltoheptaoside + H2O
?
2-chloro-4-nitrophenyl-4-O-beta-D-galactopyranosyl-maltoside + H2O
?
-
-
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose
-
commercial substrate for a flourescence-based assay, pH 7.0
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + maltotriose
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
3 glycogen
maltotriose + maltotetraose + maltopentaose
-
approx. 10% of activity with starch
-
-
?
3 starch + 2 H2O
3 malto-oligosaccharides + D-glucose + maltose
-
-
-
-
?
4,6-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
4,6-O-benzylidene 4-nitrophenyl-alpha-D-maltoheptaoside + H2O
4,6-O-benzylidene 4-nitrophenyl-alpha-D-maltosides
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
4-nitrophenyl alpha-D-maltohexaoside + H2O
?
-
-
-
?
4-nitrophenyl alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoside + H2O
4-nitrophenol + alpha-D-maltose
4-nitrophenol is bound at the ative site
-
-
?
4-nitrophenyl maltoheptaoside + H2O
4-nitrophenol + maltoheptaoside
-
-
-
?
4-nitrophenyl maltoheptaoside + H2O
maltotriose + maltotetraose + 4-nitrophenyl maltotetraoside + 4-nitrophenyl maltotrioside
-
-
-
?
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaose
-
activity measured in total fly homogenates, substrate concentration of 2.2 mM in HEPES buffer, enzyme activity preferentially required for degrading starch components of plant tissue
-
-
?
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaoside
-
-
-
-
?
4-nitrophenyl-alpha-D-maltoside + H2O
4-nitrophenol + maltose
-
-
-
-
?
acarbose + H2O
?
-
the substrate is a potent inhibitor of alpha-amylases, cyclomaltodextrinase activity
-
-
?
alpha-1,4-glucan + H2O
fragments of alpha-1,4-glucan
-
-
-
-
?
alpha-cyclodextrin + H2O
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
92% of activity with soluble starch
-
-
?
alpha-maltosyl fluoride + H2O
maltose + fluoride
-
-
-
-
?
alpha-maltotriosyl fluoride + H2O
maltotriose + fluoride
ammylopectin + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
amylopectin + H2O
D-glucose + ?
amylopectin + H2O
D-glucose + maltose
71.1% activity compared to amylose
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
fragments of amylopectin
amylopectin + H2O
malto-oligosaccharides
amylopectin + H2O
maltooligosaccharides
amylopectin + H2O
maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + D-glucose
0.5% substrate solution, 12% activity compared to amylose
-
-
?
amylopectin + H2O
maltose + maltotriose
-
-
main products
-
?
amylopektin + H2O
?
-
activity is 41% compared to the activity with soluble starch
-
-
?
amylose + H2O
D-glucose + maltose
best substrate
-
-
?
amylose + H2O
D-glucose + maltose + maltotriose
-
-
-
?
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
amylose + H2O
fragments of amylose
amylose + H2O
malto-oligosaccharides
amylose + H2O
maltooligosaccharides
amylose + H2O
maltose + D-glucose
amylose + H2O
maltose + maltotriose
-
-
main products
-
?
amylose + H2O
maltotriose + maltotetraose + maltopentaose
-
approx. 10% of activity with starch
-
-
?
amylose + H2O
oligosaccharides
amylose DP17, preferred substrate of mutant enzyme T212Y
-
-
?
beta-cyclodextrin + H2O
?
beta-cyclodextrin + H2O
D-glucose + maltose
39.0% activity compared to amylose
-
-
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
27% of activity with potato starch
-
-
?
beta-cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
beta-limit dextrin + H2O
?
beta-limit dextrin + H2O
fragments of beta-limit dextrin
-
-
-
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
cassava raw starch + H2O
?
-
-
-
-
?
corn raw starch + H2O
?
-
-
-
-
?
corn starch + H2O
malto-oligosaccharides
-
100% activity
-
-
?
corn starch + H2O
maltohexaose + maltopentaose + maltotriose
-
64% activity compared to potato starch
major end-products of starch hydrolysis
-
?
corn starch + H2O
maltose + maltotriose
-
103.2% activity compared to soluble starch
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
cycloamylose + H2O
maltooligosaccharides
-
-
-
?
cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
cyclomaltohexaose + H2O
?
dextrin + H2O
fragments of dextrin
dextrin + H2O
malto-oligosaccharides
-
67% activity compared to corn starch
-
-
?
dextrin + H2O
maltooligosaccharides
gamma-cyclodextrin + H2O
?
gamma-cyclodextrin + H2O
maltose + ?
-
-
-
-
?
gelatinized soluble starch + H2O
?
-
best substrate
-
-
?
gelatinized starch + H2O
maltotetraose + maltopentaose + maltohexaose
-
isozyme RBLA prefers gelatinized starch
-
-
?
glycogen + H2O
D-glucose + maltose
40.2% activity compared to amylose
-
-
?
glycogen + H2O
fragments of glycogen
glycogen + H2O
malto-oligosaccharides
glycogen + H2O
maltooligosaccharides
glycogen + H2O
maltose + ?
glycogen + H2O
maltose + maltotriose
glycogen starch + H2O
maltose + maltotriose
-
-
-
-
?
hydrolyzed starch + H2O
maltose
insoluble Blue Starch + H2O
?
pH 5.5, 37°C
-
-
?
isomaltose + H2O
?
-
23% of the activity with soluble starch
-
-
?
isopanose + H2O
?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
laminarin + H2O
?
-
lower activity with isozyme AI-1, low activity with isozymes AI-2 and AII
-
-
?
maize starch + H2O
?
-
-
-
?
malto-oligosaccharides + H2O
maltose
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
maltodextrin + H2O
malto-oligosaccharides
-
85% activity compared to starch
-
-
?
maltodextrin + H2O
maltooligosaccharides
maltodextrin G5 + H2O
maltodextrin G2 + maltodextrin G3
-
-
-
-
?
maltodextrin G6 + H2O
2 maltodextrin G3
-
-
-
-
?
maltodextrin G6 + H2O
maltodextrin G2 + maltodextrin G4
-
-
-
-
?
maltodextrin G7 + H2O
maltodextrin G3 + maltodextrin G4
-
-
-
-
?
maltoheptaose + 3 H2O
2 maltose + maltotriose
-
additional product: maltotetraose
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
-
-
?
maltoheptaose + H2O
D-glucose + maltose + maltotriose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
maltoheptaose + H2O
maltooligosaccharides
-
-
-
?
maltoheptaose + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltoheptaoside + H2O
?
P04745
all mutants possess the ability to hydrolyze heptasaccharide substrates and generate a similar product profile like the wild-type enzyme. The three mutants W203A, W284A, HSAmy-ar generate less products. They require higher enzyme concentration (600 nM vs. 60 nM for HSAmy and the other mutants) and more time (5 min vs. 2 min) 25°C, pH 6.9
-
-
?
maltohexaitol + H2O
maltotriose + maltotriitol
-
-
-
-
?
maltohexaose + H2O
3 maltose
-
-
-
?
maltohexaose + H2O
D-glucose + maltose + maltotriose
-
-
-
-
?
maltohexaose + H2O
maltopentaose + maltotetraose + maltotriose + maltose
-
45% of activity with potato starch
-
-
?
maltohexaose + H2O
maltose + ?
-
-
-
-
?
maltohexaose + H2O
maltotetraose + maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltooctaose + H2O
?
-
-
-
-
?
maltooligosaccharide + H2O
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
maltooligosaccharides + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
11% of activity with potato starch
-
-
?
maltooligosaccharides + H2O
maltotriose + maltotetraose
-
alpha-amylase activity
main products
-
?
maltopentaose + H2O
D-glucose + maltose + ?
-
-
-
?
maltopentaose + H2O
glucose + maltose + maltotriose
-
-
-
-
?
maltopentaose + H2O
malto-oligomers + maltose
maltopentaose + H2O
maltose + ?
-
-
-
?
maltopentaose + H2O
maltose + D-glucose + ?
-
-
-
?
maltopentaose + H2O
maltose + maltotriose
-
-
-
?
maltopentaose + H2O
maltotetraose + maltotriose + maltose
-
26% of activity with potato starch
-
-
?
maltopentaose + H2O
maltotetraose + maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltopentaose + H2O
maltotriose + maltose
-
-
major products
-
?
maltopentaose + H2O
maltotriose + maltose + D-glucose
-
-
-
?
maltopentaoside + H2O
?
P04745
all mutants possess the ability to hydrolyze pentasaccharide substrates and generate a similar product profile like the wild-type enzyme. The three mutants W203A, W284A, HSAmy-ar generate less products. They require higher enzyme concentration (600 nM vs. 60 nM for HSAmy and the other mutants) and more time (5 min vs. 2 min) 25°C, pH 6.9
-
-
?
maltose + H2O
2 D-glucose
maltose + H2O
?
-
-
-
-
?
maltose + H2O
D-glucose + ?
maltose + H2O
D-glucose + D-glucose
-
-
-
-
?
maltosyl fluoride + H2O
maltose + fluoride
-
-
-
?
maltotetraose + H2O
2 maltose
maltotetraose + H2O
glucose + maltose + maltotriose
-
-
-
-
?
maltotetraose + H2O
maltose + ?
maltotetraose + H2O
maltotriose + maltose
maltotriose
maltose + glucose + maltotetraose + maltopentaose + maltohexaose
-
the final optimum also mirrors the reverse reaction
-
r
maltotriose + H2O
D-glucose + maltose
-
-
-
?
maltotriose + H2O
maltose + ?
maltotriose + H2O
maltose + D-glucose
mung bean starch + H2O
?
-
-
-
?
oyster glycogen + H2O
?
-
-
-
?
p-nitrophenyl alpha-D-maltoside + H2O
p-nitrophenol + maltose
p-nitrophenyl maltoheptaoside + H2O
?
-
a maximum of substrate cleavage was identified at 152 MPa and 64°C, yielding approximately 25% higher substrate conversion after 30 min, as compared to the maximum at ambient pressure and 59°C
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenol + p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
intestine alpha-amylase
-
?
p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
muscle alpha-amylase
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
?
-
-
-
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenol + p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltetra[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
intestine and muscle alpha-amylase
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + D-glucose + ?
-
-
predominant product, no p-nitrophenol detected
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltetra[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
muscle alpha-amylase
-
?
p-nitrophenylpenta[alpha-D-glucopyranosyl(1-4)]-alpha-D-galactopyranoside
?
-
-
-
-
?
pea raw starch + H2O
?
-
-
-
-
?
pea starch + H2O
?
-
-
-
?
potato raw starch + H2O
?
-
-
-
-
?
potato soluble starch + H2O
?
potato starch + H2O
malto-oligosaccharides
potato starch + H2O
maltohexaose + maltopentaose + maltotriose
-
100% activity
major end-products of starch hydrolysis
-
?
potato starch + H2O
maltose + maltotriose
-
50.1% activity compared to soluble starch
-
-
?
potato starch + H2O
maltose + maltotriose + maltotetraose
pullulan + H2O
D-glucose + maltose
54.4% activity compared to amylose
-
-
?
pullulan + H2O
maltose + maltotriose
-
-
main products
-
?
pullulan + H2O
panose + ?
pullulan + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
rabbit glycogen + H2O
?
-
-
-
?
raw corn starch + H2O
?
-
-
-
-
?
raw potato starch + H2O
?
-
-
-
-
?
raw rice starch + H2O
D-glucose + maltose + maltotriose
wild-type enzyme AmyP recombinant chimeric enzyme mutant
-
-
?
raw soluble starch + H2O
?
-
22% activity compared to gelatinized soluble starch
-
-
?
raw starch + H2O
malto-oligosaccharides
-
isozymes RBSA-1 and BSA-2, raw starch from corn and potato, the latter is preferred
-
-
?
raw starch + H2O
maltooligosaccharides
raw starch + H2O
maltose + maltotriose
raw wheat starch + H2O
?
-
-
-
-
?
Remazol Brilliant Blue dyed starch + H2O
malto-oligosaccharides
-
-
-
?
Remazol Brilliant Blue-dyed starch + H2O
malto-oligosaccharides
-
-
-
?
rice flour + H2O
?
48.7% activity compared to soluble starch
-
-
?
rice starch + H2O
maltose + maltotriose
-
88.2% activity compared to soluble starch
-
-
?
rise starch + H2O
?
-
70% activity compared to soluble starch
-
-
?
soluble maize starch + H2O
?
soluble potato starch + H2O
maltopentaose + maltose + maltotriose
soluble potato starch + H2O
maltotriose + maltose + maltotetraose
-
major products of the enzymatic reaction with starch as substrate
-
?
soluble rice starch + H2O
?
55% activity compared to soluble potato starch
-
-
?
soluble starch + H2O
alpha-maltose + ?
-
-
-
-
?
soluble starch + H2O
D-glucose + maltose
93.3% activity compared to amylose
-
-
?
soluble starch + H2O
D-glucose + maltose + maltotriose + maltotetraose
-
-
-
?
soluble starch + H2O
glucose + maltose + maltotriose
soluble starch + H2O
malto-oligosaccharides
soluble starch + H2O
maltooligosaccharides
soluble starch + H2O
maltose + ?
-
maximal activity is achieved with horse-radish starch, undetectable activity towards potato starch
-
-
?
soluble starch + H2O
maltose + D-glucose
0.5% substrate solution, 66.2% activity compared to amylose
-
-
?
soluble starch + H2O
maltose + maltotriose
soluble wheat starch + H2O
?
79% activity compared to soluble potato starch
-
-
?
starch + butanol
butylglucoside + alpha-D-glucose
-
butylglucoside: wild-type ca. 4.5 mg/ml, mutant H222Q ca. 6.5 mg/ml, mutant H222E ca. 3.5 mg/ml, mutant H222D ca. 5.5 mg/mk, identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-D-glucose + maltose
pH 7.0, 85°C
wild-type (alpha-D-glucose: ca. 22 mg/ml, maltose: ca. 5.5 mg/ml), mutants: W177V (alpha-D-glucose: ca. 20 mg/ml, maltose: ca. 5 mg/ml), Y178V (alpha-D-glucose: ca. 19 mg/ml, maltose: ca. 4 mg/ml), and F179V (alpha-D-glucose: ca. 17.5 mg/ml, maltose: ca. 7 mg/ml), almost no maltotriose as product for all variants, identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-D-glucose + maltose + maltotriose
pH 7.0, 85°C
mutants: H222Q (alpha-D-glucose: ca. 21 mg/ml, maltose: ca. 5 mg/ml, maltotriose: ca. 2.5 mg/ml), H222D (alpha-D-glucose: ca. 21 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.5 mg/ml), H222E (alpha-D-glucose: ca. 13 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.0 mg/ml), and V259W (alpha-D-glucose: ca. 16 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.5 mg/ml), identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-maltose + ?
-
action mode is endolytic, hydrolysis products have an alpha-anomeric configuration. Degradation of 1% (w/v) starch results in the formation of oligosaccharides in the maltose to maltopentaose range at early time points, followed by an accumulation of maltose, maltotetraose, and small amounts of glucose after 1 h, and its final end products consisted of a high level of 58% (w/w) maltose without concomitant production of glucose
-
-
?
starch + H2O
D-glucooligomer
-
-
-
-
?
starch + H2O
D-glucose + ?
starch + H2O
D-glucose + maltose + maltotriose
starch + H2O
D-glucose + maltose + maltotriose + maltodextrins
starch + H2O
D-glucose disaccharides + D-glucose trisaccharides
starch + H2O
fragments of starch
starch + H2O
glucooligosaccharide
starch + H2O
malto-oligosaccharides
starch + H2O
maltohexaose + ?
-
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotriose
starch + H2O
maltooligosaccharides
starch + H2O
maltose + D-glucose
starch + H2O
maltose + malto-oligosaccharides + D-glucose
-
soluble starch
trace amounts of D-glucose
-
?
starch + H2O
maltose + maltotriose
starch + H2O
maltose + maltotriose + D-glucose
starch + H2O
maltose + maltotriose + maltotetraose
starch + H2O
maltotriose + ?
-
AmyD produces mainly maltotriose
-
-
?
starch + H2O
maltotriose + glucose + maltose + maltotetraose
-
pH 4, 55°C, various starches are tested: soluble potato starch as reference 100% relative activity, gelatinized amylose: 74%, potato native starch: 0.2%, potato gelatinized starch: 106%, maize native starch: 0.8%, maize gelatinized starch: 53%, rice native starch: 0.5%, and rice gelatinized starch: 52%
identified by thin-layer-chromatography, maltotriose represents 70% of the end products, only traces of glucose, small amounts of maltose and maltotetraose
-
?
starch + H2O
maltotriose + maltohexaose + maltoheptaose + maltose
-
soluble starch
first two are major products, maltohexose and maltose are intermediate products, maltotriose and maltohexaose are major products, maltoheptaose and maltose are intermediate products
-
?
starch + H2O
maltotriose + maltotetraose
-
alpha-amylase activity, preferred substrate
main products
-
?
starch + H2O
maltotriose + maltotetraose + maltopentaose
starch + H2O
oligosaccharides
insoluble blue starch, preferred substrate of mutant enzyme Y105A
-
-
?
starch + methanol
methylglucoside + alpha-D-glucose
-
methylglucoside: wild-type ca. 7.5 mg/ml, mutant H222Q ca. 13 mg/ml, mutant H222E ca. 11 mg/ml, mutant H222D ca. 11 mg/mk, identified and analyzed by thin-layer-chromatography and HPLC
-
?
sweet potato raw starch + H2O
?
-
-
-
-
?
sweet potato starch + H2O
maltose + maltotriose
-
109.1% activity compared to soluble starch
-
-
?
sweet sorghum starch + H2O
?
-
62% activity compared to potato soluble starch
-
-
?
tapioca root starch + H2O
?
-
88% activity compared to potato soluble starch
-
-
?
wheat flour + H2O
?
53.0% activity compared to soluble starch
-
-
?
wheat raw starch + H2O
?
-
-
-
-
?
wheat starch + H2O
maltohexaose + maltopentaose + maltotriose
-
78% activity compared to potato starch
major end-products of starch hydrolysis
-
?
wheat starch + H2O
maltose + maltotriose
-
92.0% activity compared to soluble starch
-
-
?
amylopectin + H2O
additional information
-
2 starch + H2O
2 malto-oligosaccharides + maltose
-
hydrolysis of soluble starch, and degradation of raw starch granules of different source, overview
-
-
?
2 starch + H2O
2 malto-oligosaccharides + maltose
-
-
-
-
?
2-chloro-4-nitrophenyl beta-D-maltoheptaoside + H2O
?
-
-
-
-
?
2-chloro-4-nitrophenyl beta-D-maltoheptaoside + H2O
?
-
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
-
acid-stable amylase and common neutral amylase can degrade the substrate at pH 5.4 to release 2-chloro-4-nitrophenol. In presence of 500 mM KSCN the reaction rate of common neutral amylase increases markedly whereas the reaction rate of acid-stable amylase decreases
-
-
?
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
-
acid-stable amylase and common neutral amylase can degrade the substrate at pH 5.4 to release 2-chloro-4-nitrophenol. In presence of 500 mM KSCN the reaction rate of common neutral amylase increases markedly whereas the reaction rate of acid-stable amylase decreases
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
alpha-cyclodextrin + H2O
?
-
9.2% of the activity with soluble starch
-
-
?
alpha-cyclodextrin + H2O
?
-
9.2% of the activity with soluble starch
-
-
?
alpha-cyclodextrin + H2O
?
-
the activity with alpha-cyclodextrin is 46% of the activity with starch in the same conditions at 0.5% (w/v) substrate concentrations
-
-
?
alpha-cyclodextrin + H2O
?
-
1.1% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
alpha-cyclodextrin + H2O
?
-
weak activity
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
-
?
alpha-cyclodextrin + H2O
?
-
cyclomaltodextrinase activity
-
-
?
alpha-cyclodextrin + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
alpha-cyclodextrin + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
alpha-cyclodextrin + H2O
?
-
13% activity compared to starch
-
-
?
alpha-maltotriosyl fluoride + H2O
maltotriose + fluoride
-
-
-
-
?
alpha-maltotriosyl fluoride + H2O
maltotriose + fluoride
-
-
-
?
amylopectin + H2O
?
69% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
intestine and muscle alpha-amylase
-
-
?
amylopectin + H2O
?
-
66% of the activity with potato starch, AmyD
-
-
?
amylopectin + H2O
?
-
55% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
55% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
80% activity compared to potato starch
-
-
?
amylopectin + H2O
?
-
80% activity compared to potato starch
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
preferred substrate
-
-
?
amylopectin + H2O
?
62.2% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
86% activity compared to potato soluble starch
-
-
?
amylopectin + H2O
?
-
67.9% activity compared to gelatinized soluble starch
-
-
?
amylopectin + H2O
?
-
86% activity compared to potato soluble starch
-
-
?
amylopectin + H2O
?
-
66.1% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
66.1% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
Halalkalibacterium halodurans
-
121% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
Halalkalibacterium halodurans 38C-2-1
-
121% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
68% of the activity with amylose
-
-
?
amylopectin + H2O
?
-
74.6% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
95% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
isozymes AI-1 and AI-2, and AII, good substrate
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
at 12% of the activity as compared to amylose
-
-
?
amylopectin + H2O
?
at 12% of the activity as compared to amylose
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
75% activity compared to soluble potato starch
-
-
?
amylopectin + H2O
?
75% activity compared to soluble potato starch
-
-
?
amylopectin + H2O
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
amylopectin + H2O
?
-
45.2% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
45.2% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
73% activity compared to starch
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
53.8% of the activity with starch
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
Caloglyphus redickorzevi
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
amylopectin + H2O
fragments of amylopectin
-
90% of activity with starch
-
-
?
amylopectin + H2O
fragments of amylopectin
-
90% of activity with starch
-
-
?
amylopectin + H2O
fragments of amylopectin
-
-
-
-
?
amylopectin + H2O
malto-oligosaccharides
-
78% activity compared to starch
-
-
?
amylopectin + H2O
malto-oligosaccharides
-
73% activity compared to corn starch
-
-
?
amylopectin + H2O
malto-oligosaccharides
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides
-
from potato, 74% of activity with soluble starch
-
-
?
amylopectin + H2O
maltooligosaccharides
-
-
-
?
amylopectin + H2O
maltooligosaccharides
-
137% of activity with soluble starch
-
-
?
amylopectin + H2O
maltooligosaccharides
-
55% of activity with potato starch
-
-
?
amylose + H2O
?
61% of the activity with soluble starch
-
-
?
amylose + H2O
?
-
intestine and muscle alpha-amylase
-
-
?
amylose + H2O
?
-
101% of the activity with potato starch, AmyD
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a low degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
90% activity compared to soluble starch
-
-
?
amylose + H2O
?
-
90% activity compared to soluble starch
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
120% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
45.5% activity compared to gelatinized soluble starch
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a high degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack decreases when temperature is raised
-
-
?
amylose + H2O
?
Halalkalibacterium halodurans
-
30% of the activity with soluble starch
-
-
?
amylose + H2O
?
Halalkalibacterium halodurans 38C-2-1
-
30% of the activity with soluble starch
-
-
?
amylose + H2O
?
-
activity is 55% compared to the activity with soluble starch
-
-
?
amylose + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
amylose + H2O
?
-
100% relative activity as reference for substrate specificity studies, pH 8.0. 65°C
-
-
?
amylose + H2O
?
amylose DP440, pH 6.8, 30°C
-
-
?
amylose + H2O
?
-
137% of the activity with soluble starch
-
-
?
amylose + H2O
?
-
isozymes AI-1 and AI-2, and AII, moderate activity
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a high degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
pH 6.5, 37°C, inhibition studies with acarviosin-containing oligosaccharides
-
-
?
amylose + H2O
?
85% activity compared to soluble potato starch
-
-
?
amylose + H2O
?
85% activity compared to soluble potato starch
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
best substrate, 117.8% activity compared to soluble starch
-
-
?
amylose + H2O
?
-
best substrate, 117.8% activity compared to soluble starch
-
-
?
amylose + H2O
?
-
55% activity compared to starch
-
-
?
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
amylose + H2O
fragments of amylose
-
1.6times higher activity than with starch
-
-
?
amylose + H2O
fragments of amylose
-
1.6times higher activity than with starch
-
-
?
amylose + H2O
fragments of amylose
-
-
-
-
?
amylose + H2O
fragments of amylose
-
-
-
-
?
amylose + H2O
fragments of amylose
-
-
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
78% activity compared to potato starch
-
-
?
amylose + H2O
malto-oligosaccharides
-
78% activity compared to potato starch
-
-
?
amylose + H2O
malto-oligosaccharides
-
145% activity compared to starch, the enzyme activity on the amylose as substrate is 1.98times greater than amylopectin
-
-
?
amylose + H2O
malto-oligosaccharides
-
-
-
-
?
amylose + H2O
malto-oligosaccharides
-
preferred substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
-
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
-
-
-
?
amylose + H2O
malto-oligosaccharides
-
amylose DP440 and amylose DP17
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
maltooligosaccharides
-
65% of activity with soluble starch
-
-
?
amylose + H2O
maltooligosaccharides
best substrate
-
-
?
amylose + H2O
maltooligosaccharides
-
-
-
-
?
amylose + H2O
maltooligosaccharides
-
69% of activity with soluble starch
-
-
?
amylose + H2O
maltooligosaccharides
-
73% of activity with potato starch
-
-
?
amylose + H2O
maltose + D-glucose
0.5% substrate solution, best substrate
-
-
?
amylose + H2O
maltose + D-glucose
0.5% substrate solution, best substrate
-
-
?
amylose DP17 + H2O
?
-
-
-
-
?
amylose DP17 + H2O
?
-
-
-
?
amylose DP440 + H2O
?
-
-
-
-
?
amylose DP440 + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
the activity with alpha-cyclodextrin is 48% of the activity with starch in the same conditions at 0.5% (w/v) substrate
-
-
?
beta-cyclodextrin + H2O
?
-
3.7% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
beta-cyclodextrin + H2O
?
insight into the action of alpha-amylase at the molecular level
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
12% activity compared to starch
-
-
?
beta-limit dextrin + H2O
?
-
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
cassava starch + H2O
?
-
129% activity compared to potato soluble starch
-
-
?
cassava starch + H2O
?
-
129% activity compared to potato soluble starch
-
-
?
corn flour + H2O
?
-
58% activity compared to potato soluble starch
-
-
?
corn flour + H2O
?
-
58% activity compared to potato soluble starch
-
-
?
corn starch + H2O
?
-
60% activity compared to soluble starch
-
-
?
corn starch + H2O
?
-
62% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
corn starch + H2O
?
-
107% activity compared to potato soluble starch
-
-
?
corn starch + H2O
?
-
107% activity compared to potato soluble starch
-
-
?
corn starch + H2O
?
-
-
-
-
?
corn starch + H2O
?
boiled starch
-
-
?
corn starch + H2O
?
-
-
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
-
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
1% starch solution
-
-
?
cyclodextrin + H2O
?
-
-
-
-
?
cyclodextrin + H2O
?
-
-
-
-
?
cyclodextrin + H2O
?
-
-
-
-
?
cyclomaltohexaose + H2O
?
-
-
-
-
?
cyclomaltohexaose + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
?
dextrin + H2O
?
-
activity is 60% compared to the activity with soluble starch
-
-
?
dextrin + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
fragments of dextrin
-
7% of activity with starch
-
-
?
dextrin + H2O
fragments of dextrin
-
7% of activity with starch
-
-
?
dextrin + H2O
maltooligosaccharides
-
27% of activity with soluble starch
-
-
?
dextrin + H2O
maltooligosaccharides
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
dextrin + H2O
maltooligosaccharides
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
-
?
gamma-cyclodextrin + H2O
?
-
2.6% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
-
?
gamma-cyclodextrin + H2O
?
-
21% of the activity with soluble starch
-
-
?
gamma-cyclodextrin + H2O
?
-
lower activity with isozyme AI-2, no activity with isozymes AI-1 and AII
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
-
?
gamma-cyclodextrin + H2O
?
-
cyclomaltodextrinase activity
-
-
?
gamma-cyclodextrin + H2O
?
at 3.9% of the activity as compared to amylose
-
-
?
gamma-cyclodextrin + H2O
?
at 3.9% of the activity as compared to amylose
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
gamma-cyclodextrin + H2O
?
-
39.1% activity compared to soluble starch
-
-
?
gamma-cyclodextrin + H2O
?
-
39.1% activity compared to soluble starch
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
32% of the activity with soluble starch
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
glycogen from Ascaris suum, intestine and muscle alpha-amylase
-
-
?
glycogen + H2O
?
-
glycogen from rabbit or Ascaris suum, intestine and muscle alpha-amylase
-
-
?
glycogen + H2O
?
-
3.6% of the activity with potato starch, AmyD
-
-
?
glycogen + H2O
?
-
35% activity compared to soluble starch
-
-
?
glycogen + H2O
?
-
35% activity compared to soluble starch
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
Halalkalibacterium halodurans
-
104% of the activity with soluble starch
-
-
?
glycogen + H2O
?
Halalkalibacterium halodurans 38C-2-1
-
104% of the activity with soluble starch
-
-
?
glycogen + H2O
?
22% of the activity with amylose
-
-
?
glycogen + H2O
?
-
activity is 29% compared to the activity with soluble starch
-
-
?
glycogen + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
16.7% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
isozymes AI-1 and AI-2, and AII, good substrate
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
85% activity compared to starch
-
-
?
glycogen + H2O
fragments of glycogen
-
7% of activity with starch
-
-
?
glycogen + H2O
fragments of glycogen
-
7% of activity with starch
-
-
?
glycogen + H2O
fragments of glycogen
-
29% of activity with starch
-
-
?
glycogen + H2O
malto-oligosaccharides
-
14% activity compared to starch
-
-
?
glycogen + H2O
malto-oligosaccharides
-
81% activity compared to corn starch
-
-
?
glycogen + H2O
malto-oligosaccharides
-
-
-
-
?
glycogen + H2O
malto-oligosaccharides
-
-
-
-
?
glycogen + H2O
malto-oligosaccharides
-
substrate from oyster
-
-
?
glycogen + H2O
malto-oligosaccharides
-
-
-
-
?
glycogen + H2O
malto-oligosaccharides
-
-
-
?
glycogen + H2O
maltooligosaccharides
-
from bovine muscle, 58% of activity with soluble starch
-
-
?
glycogen + H2O
maltooligosaccharides
-
-
-
?
glycogen + H2O
maltooligosaccharides
-
69% of activity with soluble starch
-
-
?
glycogen + H2O
maltose + ?
-
-
-
-
?
glycogen + H2O
maltose + ?
-
49.5% of the activity with starch
main product
-
?
glycogen + H2O
maltose + maltotriose
-
major products
-
?
glycogen + H2O
maltose + maltotriose
-
major products
-
?
glycogen + H2O
maltose + maltotriose
-
-
main products
-
?
hydrolyzed starch + H2O
maltose
0.5-2.0% soluble starch
-
-
?
hydrolyzed starch + H2O
maltose
0.5-2.0% soluble starch
-
-
?
maltodextran + H2O
?
-
no activity
-
-
?
maltodextran + H2O
?
-
-
-
?
maltodextrin + H2O
?
-
-
-
-
?
maltodextrin + H2O
?
-
-
-
-
?
maltodextrin + H2O
?
87.6% activity compared to soluble starch
-
-
?
maltodextrin + H2O
?
-
-
-
-
?
maltodextrin + H2O
?
white dextrin
-
-
?
maltodextrin + H2O
?
-
60% of the activity with amylose
-
-
?
maltodextrin + H2O
maltooligosaccharides
-
-
-
-
?
maltodextrin + H2O
maltooligosaccharides
-
100% of activity with potato starch
-
-
?
maltoheptaose + H2O
?
-
95% activity compared to potato starch
-
-
?
maltoheptaose + H2O
?
-
95% activity compared to potato starch
-
-
?
maltoheptaose + H2O
?
-
-
-
?
maltoheptaose + H2O
?
-
-
-
?
maltoheptaose + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
43% of activity with potato starch
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
58% of the activity with soluble starch
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
isozymes AI-1 and AI-2, and AII, low activity
-
-
?
maltopentaose + H2O
malto-oligomers + maltose
-
-
-
-
?
maltopentaose + H2O
malto-oligomers + maltose
-
preferred substrate
-
-
?
maltose + H2O
2 D-glucose
-
weak activity
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
18% of the activity with starch
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
Caloglyphus redickorzevi
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltose + H2O
D-glucose + ?
-
assat at 37°C
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
weak activity
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
isozymes AI-1 and AI-2, and AII, low activity
-
-
?
maltotetraose + H2O
maltose + ?
-
-
-
-
?
maltotetraose + H2O
maltose + ?
-
-
-
?
maltotetraose + H2O
maltotriose + maltose
-
-
identified by thin-layer-chromatography
-
?
maltotetraose + H2O
maltotriose + maltose
-
46% of activity with potato starch
-
-
?
maltotriose + H2O
?
-
low activity
-
-
?
maltotriose + H2O
?
-
lower activity with isozyme AII, no activity with isozymes AI-1 and AI-2
-
-
?
maltotriose + H2O
?
-
very low activity
-
-
?
maltotriose + H2O
maltose + ?
-
no activity against isomaltotriose (alpha-glucosyl-(1->6)-alpha-glucosyl-(1->6)-glucose)
-
-
?
maltotriose + H2O
maltose + ?
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
no activity
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
no activity
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
no activity
-
-
?
maltotriose + H2O
maltose + D-glucose
-
6% of activity with potato starch
-
-
?
maltotriose + H2O
maltose + D-glucose
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
maltotriose + H2O
maltose + D-glucose
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
p-nitrophenyl alpha-D-maltoside + H2O
p-nitrophenol + maltose
-
-
-
?
p-nitrophenyl alpha-D-maltoside + H2O
p-nitrophenol + maltose
-
-
-
?
p-nitrophenyl alpha-D-maltoside + H2O
p-nitrophenol + maltose
-
-
-
?
p-nitrophenyl alpha-D-maltoside + H2O
p-nitrophenol + maltose
-
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
poor substrate
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
good substrate
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
-
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
-
-
-
?
potato soluble starch + H2O
?
-
100% activity
-
-
?
potato soluble starch + H2O
?
-
100% activity
-
-
?
potato starch + H2O
?
-
60% activity compared to soluble starch
-
-
?
potato starch + H2O
?
-
95% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
potato starch + H2O
?
-
-
-
-
?
potato starch + H2O
?
1% w/v potato starch
-
-
?
potato starch + H2O
?
1% w/v potato starch
-
-
?
potato starch + H2O
?
1% w/v potato starch
-
-
?
potato starch + H2O
?
1% w/v potato starch
-
-
?
potato starch + H2O
?
1% w/v potato starch
-
-
?
potato starch + H2O
?
-
-
-
?
potato starch + H2O
malto-oligosaccharides
-
potato starch has low affinity toward alpha-amylase AI (12% activity compared to corn starch)
-
-
?
potato starch + H2O
malto-oligosaccharides
-
-
-
-
?
potato starch + H2O
malto-oligosaccharides
-
-
-
-
?
potato starch + H2O
maltose + maltotriose + maltotetraose
-
0.5% starch solution
-
-
?
potato starch + H2O
maltose + maltotriose + maltotetraose
0.5% starch solution
-
-
?
potato starch + H2O
maltose + maltotriose + maltotetraose
0.5% starch solution
-
-
?
potato starch + H2O
maltose + maltotriose + maltotetraose
0.5% starch solution
-
-
?
pullulan + H2O
?
-
-
-
?
pullulan + H2O
?
-
41.1% of the activity with soluble starch
-
-
?
pullulan + H2O
?
-
41.1% of the activity with soluble starch
-
-
?
pullulan + H2O
?
-
2.5% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
14.2% activity compared to soluble starch
-
-
?
pullulan + H2O
?
-
14.2% activity compared to soluble starch
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
no activity
-
-
?
pullulan + H2O
panose + ?
0.5% substrate solution, 18.9% activity compared to amylose
-
-
?
pullulan + H2O
panose + ?
at 72.5% of the activity as compared to amylose. The enzyme is an alpha-amylase with neopullulanase-like activity
-
-
?
pullulan + H2O
panose + ?
at 72.5% of the activity as compared to amylose. The enzyme is an alpha-amylase with neopullulanase-like activity
-
-
?
pullulan + H2O
panose + ?
0.5% substrate solution, 18.9% activity compared to amylose
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
the enzyme can attack some of the (1->6)-alpha-D-glucosidic linkages in partial hydrolyzates of pullulan
-
-
?
pullulan + H2O
panose + ?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
Thermomonospora viridis
-
-
-
-
?
raw rice starch + H2O
?
recombinant chimeric enzyme mutant
-
-
?
raw rice starch + H2O
?
-
-
-
-
?
raw sago starch + H2O
?
high level of activity
-
-
?
raw sago starch + H2O
?
high level of activity
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
-
?
raw starch + H2O
?
-
-
-
?
raw starch + H2O
?
-
the fungal enzyme shows high activity on raw starch
-
-
?
raw starch + H2O
?
the recombinant enzyme shows low degradation of raw starch in a concentration-dependent manner
-
-
?
raw starch + H2O
maltooligosaccharides
from potato, corn, rice, and wheat
-
-
?
raw starch + H2O
maltooligosaccharides
-
raw starch from corn, 20% of activity with soluble starch
-
-
?
raw starch + H2O
maltose + maltotriose
hydrolyzed raw starch isolated from a jack fruit seed cotyledons, recombinant enzyme can hydrolyze raw jackfruit seed starch up to 52% after 6 h treatment at 30°C
-
-
?
raw starch + H2O
maltose + maltotriose
hydrolyzed raw starch isolated from a jack fruit seed cotyledons, recombinant enzyme can hydrolyze raw jackfruit seed starch up to 52% after 6 h treatment at 30°C
-
-
?
rice starch + H2O
?
-
43% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
rice starch + H2O
?
boiled starch
-
-
?
soluble maize starch + H2O
?
60% activity compared to soluble potato starch
-
-
?
soluble maize starch + H2O
?
60% activity compared to soluble potato starch
-
-
?
soluble potato starch + H2O
maltopentaose + maltose + maltotriose
best substrate
-
-
?
soluble potato starch + H2O
maltopentaose + maltose + maltotriose
best substrate
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
1% w/v starch solution
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
best substrate, 0.5% starch solution
-
-
?
soluble starch + H2O
?
-
best substrate, 0.5% starch solution
-
-
?
soluble starch + H2O
?
-
97.5% hydrolysis of soluble starch by soluble enzyme, 92.2% hydrolysis of soluble starch by the enzyme immobilized in calcium alginate breads
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
alpha-amylase PA
-
-
?
soluble starch + H2O
?
-
alpha-amylase PA
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
best substrate
-
-
?
soluble starch + H2O
?
-
maltose, maltotriose, and maltotetraose are the major products from starch hydrolysis but prolonged reaction leads to the production of glucose, maltose, and maltotriose
-
-
?
soluble starch + H2O
?
-
maltose, maltotriose, and maltotetraose are the major products from starch hydrolysis but prolonged reaction leads to the production of glucose, maltose, and maltotriose
-
-
?
soluble starch + H2O
?
-
0.5% starch solution
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
Halalkalibacterium halodurans
-
-
-
-
?
soluble starch + H2O
?
Halalkalibacterium halodurans 38C-2-1
-
-
-
-
?
soluble starch + H2O
?
79% of the activity with amylose
at the initial stage of the reaction, maltose and maltotriose are formed, then the amount of maltose increases with time
-
?
soluble starch + H2O
?
-
the enzyme hydrolyzes 69% of the wheat starch after a 2 h incubation at 70°C in an aqueous/hexadecane two-phase system. The main hydrolysis products are maltose, maltotriose, maltotetraose, maltopentaose, and maltohexaose showing that the amylase cleaves the internal alpha-1,4 linkages and indicating that the enzyme is an endo-type amylase. The enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
pH 5.0, 95°C
varying amounts of maltooligosaccharides, depending on reaction time
-
?
soluble starch + H2O
?
-
pH 5.0, 95°C
varying amounts of maltooligosaccharides, depending on reaction time
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
glucose + maltose + maltotriose
-
-
-
-
?
soluble starch + H2O
glucose + maltose + maltotriose
-
-
-
-
?
soluble starch + H2O
malto-oligosaccharides
-
-
-
?
soluble starch + H2O
malto-oligosaccharides
-
-
-
?
soluble starch + H2O
maltooligosaccharides
-
endolytic activity. Small maltooligosaccharides (D2-D4) are formed more predominantly than larger maltooligosaccharides (D5-D7)
-
-
?
soluble starch + H2O
maltooligosaccharides
-
endolytic activity. Small maltooligosaccharides (D2-D4) are formed more predominantly than larger maltooligosaccharides (D5-D7)
-
-
?
soluble starch + H2O
maltooligosaccharides
0.5% soluble starch
-
-
?
soluble starch + H2O
maltose + maltotriose
-
-
-
?
soluble starch + H2O
maltose + maltotriose
-
-
-
?
soluble starch + H2O
maltose + maltotriose
-
-
products of amylolytic attack are mixed oligosaccharides including mainly maltose and maltotriose
-
?
soluble starch + H2O
maltose + maltotriose
-
-
products of amylolytic attack are mixed oligosaccharides including mainly maltose and maltotriose
-
?
soluble starch + H2O
maltose + maltotriose
-
the recombinant enzyme is more active towards linear starchy substrates than branched ones. The hydrolysis products are mainly comprised of maltose and maltotriose
-
-
?
starch + H2O
?
-
pH 6.5, 37°C
-
-
?
starch + H2O
?
-
intestine and muscle alpha-amylase
-
-
?
starch + H2O
?
hydrolysis of alpha-1,4-glucosidic bonds
-
-
?
starch + H2O
?
hydrolysis of alpha-1,4-glucosidic bonds
-
-
?
starch + H2O
?
-
soluble starch as substrate, pH 5.0, 50°C, 100% relative enzyme activity
the liberated reducing sugars (glucose equivalents) are estimated by the dinitrosalicylic acid method
-
?
starch + H2O
?
soluble starch, 2000000 Dalton, only soluble at temperatures close to 100°C, in phosphate buffer, pH 7.4, assay at 37°C
-
-
?
starch + H2O
?
-
1% w/v starch solution
-
-
?
starch + H2O
?
-
1% w/v starch solution
-
-
?
starch + H2O
?
-
strong digesting ability towards various raw starches. The degradation rates of corn, wheat and potato starch granules at 1% concentration are 57.5%, 53%, 45.1% at 8 h and 63.2%, 56.4%, 48.6% at 12 h, respectively. Efficiently hydrolyzes raw corn starch at a concentration of 20% and pH 5.0
-
-
?
starch + H2O
?
-
strong digesting ability towards various raw starches. The degradation rates of corn, wheat and potato starch granules at 1% concentration are 57.5%, 53%, 45.1% at 8 h and 63.2%, 56.4%, 48.6% at 12 h, respectively. Efficiently hydrolyzes raw corn starch at a concentration of 20% and pH 5.0
-
-
?
starch + H2O
?
-
pH 6.5, 37°C
-
-
?
starch + H2O
?
alpha-amylases are classical calcium-binding enzymes, which randomly hydrolyze internal alpha-1,4-glucosidic linkages in starch to produce smaller molecular mass maltodextrins, maltooligosaccharides and glucose
-
-
?
starch + H2O
?
-
rice starch, starch of pearl millet, corn starch, potato starch, wheat starch
-
-
?
starch + H2O
?
-
soluble starch as substrate
the liberated reducing sugars are determined using dinitrosalicylic acid reagent
-
?
starch + H2O
?
-
rice starch, starch of pearl millet, corn starch, potato starch, wheat starch
-
-
?
starch + H2O
?
pH 6.5, 50°C
-
-
?
starch + H2O
?
-
endo-acting activity
-
-
?
starch + H2O
?
-
the main hydrolysis products are maltose, maltotriose, maltotetraose, maltopentaose, and maltohexaose. The enzyme hydrolyzes 69% of the wheat starch after a 2 h incubation at 70°C in an aqueous/hexadecane two-phase system
-
-
?
starch + H2O
?
-
soluble starch, 93.9% relative activity compared to amylose as substrate, pH 8.0, 65°C
-
-
?
starch + H2O
?
-
salivary alpha-amylase digests a portion of ingested starch in the stomach before it enters the intestine and is exposed to pancreatic amylase. A role of salivary alpha-amylase is bacterial clearance from the mouth and prevention of bacterial attachment to oral surfaces
-
-
?
starch + H2O
?
P04745
25°C, pH 6.9
-
-
?
starch + H2O
?
-
potato starch, pH 6.0, room temperature
-
-
?
starch + H2O
?
0.1-2.0% starch solution
-
-
?
starch + H2O
?
-
1% starch solution, alpha-amylase is an endo-hydrolyase, which randomly acts within starch chains producing a mixture of maltooligosaccharides along with maltose and glucose
-
-
?
starch + H2O
?
-
1% starch solution, alpha-amylase is an endo-hydrolyase, which randomly acts within starch chains producing a mixture of maltooligosaccharides along with maltose and glucose
-
-
?
starch + H2O
?
0.1-2.0% starch solution
-
-
?
starch + H2O
?
-
the optimum starch concentration for the enzyme production is 32 g/l. Higher concentrations show substrate inhibition
-
-
?
starch + H2O
?
-
soluble starch, best substrate for isozymes AI-1 and AI-2, and AII
-
-
?
starch + H2O
?
endoglycolytic activity
-
-
?
starch + H2O
?
corn starch is preferred over wheat starch and sweet-potato starch. Potato starch is a poor substrate
-
-
?
starch + H2O
?
at 66.2% of the activity as compared to amylose
-
-
?
starch + H2O
?
at 66.2% of the activity as compared to amylose
-
-
?
starch + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
starch + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
starch + H2O
?
-
inhibition studies using extract of different medicinal plants, pH 6.9
absorbance of reaction products are measured at 540 nm
-
?
starch + H2O
?
pH 6.5, 37°C
-
-
?
starch + H2O
?
-
50°C, pH 6.0 or 9.0
-
-
?
starch + H2O
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
starch + H2O
?
-
best substrate, potato starch
-
-
?
starch + H2O
?
-
pH 5.5, 55°C
-
-
?
starch + H2O
?
Wangia sp. C52
-
-
-
-
?
starch + H2O
?
-
pH 6.5, 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
Caloglyphus redickorzevi
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + ?
-
assay at 37°C
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
-
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
-
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
various sources of starch are tested, japonica rice as control with 100% relative activity, India rice: 294% and 508% relative activity for Amy I and Amy II, respectively, corn: 10.7% and 2.8% relative activity for Amy I and Amy II, respectively, wheat: 27.1% and 47.5% relative activity for Amy I and Amy II, respectively, potato: 10.6% and 4.47% relative activity for Amy I and Amy II, respectively, sweet potato: 13.5% and 1.88% relative activity for Amy I and Amy II, respectively, cassava: 1.22% relative activity for Amy II
reactions product identified by thin-layer-chromatography
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
1% potato starch solution
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
-
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
quantitative analysis of reaction products of wild-type and H286 mutant enzymes, overview
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
starch + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
soluble starch, 68% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
starch + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
soluble starch, 68% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
starch + H2O
D-glucose disaccharides + D-glucose trisaccharides
-
degradation of raw starch, isozyme Amyl III
-
-
?
starch + H2O
D-glucose disaccharides + D-glucose trisaccharides
-
degradation of raw and cooked starch granules by raw-starch-digesting alpha-amylase, Amyl III, starch of wheat bran, and and corn, microscopy of untreated granules and partially degraded granules, overview
-
-
?
starch + H2O
D-glucose disaccharides + D-glucose trisaccharides
-
degradation of raw starch, isozyme Amyl III
-
-
?
starch + H2O
D-glucose disaccharides + D-glucose trisaccharides
-
degradation of raw and cooked starch granules by raw-starch-digesting alpha-amylase, Amyl III, starch of wheat bran, and and corn, microscopy of untreated granules and partially degraded granules, overview
-
-
?
starch + H2O
dextrin
-
-
-
-
?
starch + H2O
dextrin
-
-
-
-
?
starch + H2O
dextrin
-
-
-
?
starch + H2O
dextrin
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
fragments of starch
-
-
-
-
?
starch + H2O
glucooligosaccharide
-
high enzyme production during stationary phase of growth, lack of catabolite repression
-
-
?
starch + H2O
glucooligosaccharide
-
high enzyme production during stationary phase of growth, lack of catabolite repression
-
-
?
starch + H2O
glucooligosaccharide
Thermomonospora vulgaris
-
enzyme production is induced by 2% starch or solid CaCO3
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
raw starch from corn and potato
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
ir
starch + H2O
malto-oligosaccharides
-
raw starch from corn and potato, the latter is preferred
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
100% activity
maltoheptaose is observed as a predominant product. When further hydrolysis is performed, glucose, maltose, maltotriose, maltotetraose, maltopentaose and maltohexaose appear. Glucose and maltose are produced after 2 h of incubation, and after 24 h, the main products are maltotriose, maltose and glucose
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch from potato
-
-
?
starch + H2O
malto-oligosaccharides
-
gelatinized starch from potato
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch from potato
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
starch granules, high affinity for the substrate is mediated by the enzyme's separate starch binding domain, SBD
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
the alpha-amylase from the resistant no-cost strain exhibits higher activity towards starch compared to the resistant cost strain
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
soluble starch
-
-
?
starch + H2O
malto-oligosaccharides
-
-
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotriose
-
-
major end products
-
?
starch + H2O
maltohexaose + maltopentaose + maltotriose
-
active on wheat starch, corn starch, potato starch, the latter is the best starch substrate
major end products, see also EC 3.2.1.116
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
?
starch + H2O
maltooligosaccharides
synthesis of alpha-amylase not catabolite-repressed by glucose in strain KCC103, difference to other Bacillus species
-
-
?
starch + H2O
maltooligosaccharides
endolytic activity by forming maltooligosaccharides on hydrolysis of soluble starch, similar product profiles at pH 4 and pH 7, rather small maltooligosaccharides (D2D4) than larger maltooligosaccharides (D5D7) formed, proportional levels of sugars produced after 24 h hydrolysis of soluble starch indicated
-
-
?
starch + H2O
maltooligosaccharides
synthesis of alpha-amylase not catabolite-repressed by glucose in strain KCC103, difference to other Bacillus species
-
-
?
starch + H2O
maltooligosaccharides
endolytic activity by forming maltooligosaccharides on hydrolysis of soluble starch, similar product profiles at pH 4 and pH 7, rather small maltooligosaccharides (D2D4) than larger maltooligosaccharides (D5D7) formed, proportional levels of sugars produced after 24 h hydrolysis of soluble starch indicated
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
soluble starch from potato
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
-
-
-
?
starch + H2O
maltooligosaccharides
-
alpha-amylase activity, preferred substrate, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
starch + H2O
maltose + ?
-
1% starch w/v
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
pH 8.0, 100°C
-
-
?
starch + H2O
maltose + ?
-
preferred substrate
main product
-
?
starch + H2O
maltose + ?
-
and larger maltooligosaccharides
-
?
starch + H2O
maltose + D-glucose
-
-
-
-
?
starch + H2O
maltose + D-glucose
-
raw starch from corn and soluble starch, endo mode of action
25% maltose, 75% glucose
-
?
starch + H2O
maltose + D-glucose
-
-
-
-
?
starch + H2O
maltose + D-glucose
-
raw starch from corn and soluble starch, endo mode of action
25% maltose, 75% glucose
-
?
starch + H2O
maltose + maltotriose
-
major products
-
?
starch + H2O
maltose + maltotriose
-
major products
-
?
starch + H2O
maltose + maltotriose
-
-
-
-
?
starch + H2O
maltose + maltotriose
-
soluble starch
main products
-
?
starch + H2O
maltose + maltotriose
-
pH 6.5, 37°C
the main products
-
?
starch + H2O
maltose + maltotriose
-
pH 6.5, 37°C
the main products
-
?
starch + H2O
maltose + maltotriose
-
potato starch
major products
-
?
starch + H2O
maltose + maltotriose + D-glucose
-
-
major reaction products of the amylase are maltose and maltotriose, and the minor product is glucose
-
?
starch + H2O
maltose + maltotriose + D-glucose
-
-
major reaction products of the amylase are maltose and maltotriose, and the minor product is glucose
-
?
starch + H2O
maltose + maltotriose + maltotetraose
-
-
-
?
starch + H2O
maltose + maltotriose + maltotetraose
preferred substrate
-
-
?
starch + H2O
maltotriose + maltotetraose + maltopentaose
-
-
-
-
?
starch + H2O
maltotriose + maltotetraose + maltopentaose
-
potato starch
-
-
?
wheat starch + H2O
?
-
60% activity compared to soluble starch
-
-
?
wheat starch + H2O
?
-
56.5% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
wheat starch + H2O
?
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
predominant initial products are: maltose, maltotriose, maltohexaose and maltoheptaose
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
maltotriose
?
amylopectin + H2O
additional information
-
-
94% of the activity with starch
-
-
?
amylopectin + H2O
additional information
-
-
94% of the activity with starch
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
95% of the activity obtained with starch
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
92% of the activity with amylose
-
-
?
amylopectin + H2O
additional information
-
-
92% of the activity with amylose
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylopectin + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
predominant initial products are: maltose, maltotriose, maltohexaose and maltoheptaose
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
short chain, DP 17
yield of maltotriose is 69%
?
amylose + H2O
additional information
-
-
34% of activity with starch
-
-
?
amylose + H2O
additional information
-
-
34% of activity with starch
-
-
?
amylose + H2O
additional information
-
-
short chain, DP 17
-
-
?
amylose + H2O
additional information
-
-
short chain, DP 17
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
short chain, DP 17
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
65% of the activity obtained with starch
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
short chain amylose
-
-
?
amylose + H2O
additional information
-
-
-
glucose + maltose
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
amylose + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
68% of the activity with starch
-
-
?
glycogen + H2O
additional information
-
-
68% of the activity with starch
-
-
?
glycogen + H2O
additional information
-
-
-
immediate products are maltohexaose and maltoheptaose
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
maltotriose
?
glycogen + H2O
additional information
-
-
86% of the activity with starch
-
-
?
glycogen + H2O
additional information
-
-
86% of the activity with starch
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
65% of the activity obtained with starch
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
-
-
-
?
glycogen + H2O
additional information
-
-
weak activity
-
-
?
isopanose + H2O
additional information
-
-
-
glucose + maltose + isomaltose
?
isopanose + H2O
additional information
-
-
-
at low substrate concentratins, 0.5%, equimolar maltose and glucose are produced, at high substrate concentrations, 4.0%, a small amount of isomaltoside + glucose + maltose is produced. The enzyme can hydrolyze alpha-1,6-glucosidic linkage as well as alpha-1,4-glucosidic linkage
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
maltotetraose + maltotriose
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
-
-
?
maltoheptaose + H2O
additional information
-
-
-
maltotetraose + maltotriose
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
glucose + maltopentaose
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
-
-
?
maltohexaose + H2O
additional information
-
-
-
maltose + maltotetraose or maltotriose
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
no activity
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
-
-
?
maltopentaose + H2O
additional information
-
-
-
glucose + maltose + maltotriose + a slight amount of maltotetraose
?
maltopentaose + H2O
additional information
-
-
-
maltose + maltotriose
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
maltotetraose + H2O
additional information
-
-
-
maltose with some glucose and maltotriose
?
maltotetraose + H2O
additional information
-
-
no activity
-
-
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
maltotetraose + H2O
additional information
-
-
-
maltose + maltose
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
maltotetraose + H2O
additional information
-
-
-
glucose + maltose + maltotriose
?
maltotetraose + H2O
additional information
-
-
-
maltose + maltose
?
maltotetraose + H2O
additional information
-
-
-
maltose + maltose
?
maltotetraose + H2O
additional information
-
-
-
-
-
?
additional information
?
-
the enzyme has some glycosyl transferase activity
-
-
?
additional information
?
-
-
the enzyme has some glycosyl transferase activity
-
-
?
additional information
?
-
high-molecular-mass compounds containing alpha-1,4 linkages are the best substrates for the enzyme. After 5 min reaction, no hydrolytic activity can be detected using maltose, xylan, pullulan or alpha-, beta- and gamma-cyclodextrins as substrates
-
-
?
additional information
?
-
alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units
-
-
?
additional information
?
-
recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product
-
-
?
additional information
?
-
alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units
-
-
?
additional information
?
-
recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product
-
-
?
additional information
?
-
-
the extracellular enzyme hydrolyses alpha-1,4 glucosidic linkages randomly throughout the starch molecule in an endo-fashion producing oligosaccharides and monosaccharides, including maltose, glucose and alpha limit dextrin
-
-
?
additional information
?
-
-
no activity with pullulan and maltose
-
-
?
additional information
?
-
-
the extracellular enzyme hydrolyses alpha-1,4 glucosidic linkages randomly throughout the starch molecule in an endo-fashion producing oligosaccharides and monosaccharides, including maltose, glucose and alpha limit dextrin
-
-
?
additional information
?
-
-
no activity with pullulan and maltose
-
-
?
additional information
?
-
-
applicability of recombinant chimeric mutant Ba-Gt-amy and wild-type amylase Ba-amy in raw starch hydrolysis, method evaluation
-
-
?
additional information
?
-
-
adsorption to and hydrolysis of raw starch from corn and potato, overview
-
-
?
additional information
?
-
-
adsorption to and hydrolysis of raw starch from corn and potato, overview
-
-
?
additional information
?
-
-
no activity towards maltohexaose, maltopentaose, and maltotetraose
-
-
?
additional information
?
-
-
BMA.2 is active on potato starch, wheat starch, corn starch, amylose, amylopectin, and maltoheptaose, highest activity on amylose
-
-
?
additional information
?
-
-
no activity towards maltohexaose, maltopentaose, and maltotetraose
-
-
?
additional information
?
-
-
BMA.2 is active on potato starch, wheat starch, corn starch, amylose, amylopectin, and maltoheptaose, highest activity on amylose
-
-
?
additional information
?
-
-
does not hydrolyze alpha- and beta-cyclodextrin
-
-
?
additional information
?
-
-
a saccharifying enzyme
-
-
?
additional information
?
-
-
adsorption to and hydrolysis of raw starch from corn and potato, effect on isozymes, overview, isozyme RBLA is a liquifying alpha-amylase
-
-
?
additional information
?
-
maltooligosaccharide bind to the carbohydrate-binding domain, CBM58, of SusG. SusG is flexible in its carbohydrate selectivity because it binds to and degrades pullulan, amylopectin, and amylose. It shows low activity on alpha- and beta-cyclodextrins
-
-
?
additional information
?
-
substrate specificity, overview. Reaction product analysis by anion exchange chromatography. The enzyme reaction products are in the range of glucose to maltotetraose, whereas maltooligosaccharides smaller than maltotetraose are partially hydrolyzed. Maltose is not degraded. Maltooligosaccharides larger than maltotetraose, such as maltoheptaose, cycloamylose, and amylose, are fully hydrolyzed. Relatively small cyclodextrins, such as alpha-cyclodextrin and beta-cyclodextrin, are not hydrolyzed by enzyme BiLA, although gamma-cyclodextrin is partially hydrolyzed. Macromolecules containing alpha-1,6 linkages, such as amylopectin, starch, and glycogen, are also partially hydrolyzed to maltooligosaccharides smaller than G4. Pullulan, a polysaccharide polymer consisting of maltotriose units, is not hydrolyzed
-
-
?
additional information
?
-
-
does not hydrolyze beta-cyclodextrin and dextran
-
-
?
additional information
?
-
-
the enzyme hydrolyses alpha-1,4-glycosidic bonds and not alpha-1,6-linkages. It has no activity toward maltose, alpha-cyclodextrin, beta-cyclodextrin, panose, acarbose and dextran
-
-
?
additional information
?
-
-
no activity detected using cassava starch as substrate for Amy I
-
-
?
additional information
?
-
-
trace activity towards alpha-cyclodextrin, no hydrolysis of pullulan, no hydrolysis of maltose
-
-
?
additional information
?
-
-
trace activity towards alpha-cyclodextrin, no hydrolysis of pullulan, no hydrolysis of maltose
-
-
?
additional information
?
-
-
no activity with pullulan and sucrose
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation
-
-
?
additional information
?
-
-
applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation
-
-
?
additional information
?
-
applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation
-
-
?
additional information
?
-
applicability of recombinant chimeric mutant Ba-Gt-amy in raw starch hydrolysis, method evaluation
-
-
?
additional information
?
-
-
soybean alpha-amylase shows high specificity for its primary substrate starch, followed by amylopectin and dextrin (III), lower activity with amylopectin, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
no hydrolytic activity towards pullulan or dextran
-
-
?
additional information
?
-
Halalkalibacterium halodurans 38C-2-1
-
no hydrolytic activity towards pullulan or dextran
-
-
?
additional information
?
-
-
AmyH might be a substrate of the Twin-ariginine translocase Tat pathway
-
-
?
additional information
?
-
-
no hydrolytic activity is detected on alpha-cyclodextrin, beta-cyclodextrin, and pullulan
-
-
?
additional information
?
-
-
no hydrolytic activity with alpha-cyclodextrin, beta-cyclodextrin or pullulan
-
-
?
additional information
?
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan
-
-
?
additional information
?
-
P04745
interaction analysis of human salivary alpha-amylase and Sorghum procyanidin tetramer, structure, overview
-
-
?
additional information
?
-
substrate specificities of wild-type and mutant enzymes, oligosaccharide action patterns of mutant enzymes, overview, Tyr105 and Thr212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of alpha-amylase 1, modelling of oligosaccharide substrate docking at the substrate binding area
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, oligosaccharide action patterns of mutant enzymes, overview, Tyr105 and Thr212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of alpha-amylase 1, modelling of oligosaccharide substrate docking at the substrate binding area
-
-
?
additional information
?
-
-
the enzyme is a maltohexaose-producing alpha-amylase
-
-
?
additional information
?
-
-
the enzyme is highly efficient in removing starch stains from the cotton cloth
-
-
?
additional information
?
-
-
the enzyme is highly efficient in removing starch stains from the cotton cloth
-
-
?
additional information
?
-
-
no activity with maltodextrins of G2-G4
-
-
?
additional information
?
-
-
isozyme substrate specificity, no activity of all isozymes with pullulan, alpha-cyclodextrin, and beta-cyclodextrin, overview
-
-
?
additional information
?
-
-
substrate preference in decreasing order: starch, amylopectin, maltose, amylose and glycogen
-
-
?
additional information
?
-
-
chimeric enzyme engineered from two rice alpha-amylases isoenzymes, Amy1A and Amy3D. Amy1 shows high activity in soluble-starch hydrolysis and low activity in oligosaccharide degradation, while Amy3D shows low activity in soluble-starch hydrolysis and high activity in oligosaccharide degradation. The chimeric enzyme shows high activities in both soluble-starch hydrolysis and oligosaccharide degradation
-
-
?
additional information
?
-
the enzyme Amy can hydrolyze typical substrates into glucose and maltose, substrate specificity, overview. Enzyme Amy broad substrate range and transglycosylation activity when compared with intracellular alpha-amylase AmyB. Amy exhibits transglycosylation activity when reacted with maltose and maltotriose
-
-
?
additional information
?
-
the crustacean cardioactive peptide isolated from midgut and central nervous system of cockroaches exhibits alpha-amylase activity in the midgut and might be involved in digestion of carbohydrate in a paracrine manner, CCAP also shows myotropic activity and might also be involved in stimulation of midgut contraction
-
-
?
additional information
?
-
-
the crustacean cardioactive peptide isolated from midgut and central nervous system of cockroaches exhibits alpha-amylase activity in the midgut and might be involved in digestion of carbohydrate in a paracrine manner, CCAP also shows myotropic activity and might also be involved in stimulation of midgut contraction
-
-
?
additional information
?
-
-
substrate specificity, hydrolytic pattern, PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, but no transglycosylation activity, overview
-
-
?
additional information
?
-
does not hydrolyze pullulan, cyclodextrins, sucrose
-
-
?
additional information
?
-
-
does not hydrolyze pullulan, cyclodextrins, sucrose
-
-
?
additional information
?
-
very weakly hydrolyzes pullulan to form panose or isopanose
-
-
?
additional information
?
-
very weakly hydrolyzes pullulan to form panose or isopanose
-
-
?
additional information
?
-
-
no activity with pullulan
-
-
?
additional information
?
-
-
alpha-cyclodextrin, beta-cyclodextrin, gamma-cyclodextrin, and malto-beta-cyclodextrin are poor substrates. Thin layer chromatography and high performance anion exchange chromatography analysis of hydrolysis products from maltodextrins (G2-G5) by recombinant enzyme Rbamy5, overview. Maltose is not hydrolyzed
-
-
?
additional information
?
-
alpha-cyclodextrin, beta-cyclodextrin, gamma-cyclodextrin, and malto-beta-cyclodextrin are poor substrates. Thin layer chromatography and high performance anion exchange chromatography analysis of hydrolysis products from maltodextrins (G2-G5) by recombinant enzyme Rbamy5, overview. Maltose is not hydrolyzed
-
-
?
additional information
?
-
-
alpha-cyclodextrin, beta-cyclodextrin, gamma-cyclodextrin, and malto-beta-cyclodextrin are poor substrates. Thin layer chromatography and high performance anion exchange chromatography analysis of hydrolysis products from maltodextrins (G2-G5) by recombinant enzyme Rbamy5, overview. Maltose is not hydrolyzed
-
-
?
additional information
?
-
alpha-cyclodextrin, beta-cyclodextrin, gamma-cyclodextrin, and malto-beta-cyclodextrin are poor substrates. Thin layer chromatography and high performance anion exchange chromatography analysis of hydrolysis products from maltodextrins (G2-G5) by recombinant enzyme Rbamy5, overview. Maltose is not hydrolyzed
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
activity of Amy1 towards soluble starch, glycogen, amylopectin, amylose in descending order
-
-
?
additional information
?
-
-
ScAmy43 does not hydrolyze native starches
-
-
?
additional information
?
-
-
maltose is not hydrolyzed by the alpha-amylase
-
-
?
additional information
?
-
-
maltose is not hydrolyzed by the alpha-amylase
-
-
?
additional information
?
-
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
additional information
?
-
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
additional information
?
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
?
additional information
?
-
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
?
additional information
?
-
enzyme TfAmy48 shows an endo-acting pattern. It has no activity with raw starch, alpha-cyclodextrin, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
enzyme TfAmy48 shows an endo-acting pattern. It has no activity with raw starch, alpha-cyclodextrin, and carboxymethyl cellulose
-
-
?
additional information
?
-
enzyme TfAmy48 shows an endo-acting pattern. It has no activity with raw starch, alpha-cyclodextrin, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
action pattern on maltooligosaccharides
-
-
?
additional information
?
-
-
substrate specificity of the bifunctional enzyme, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, and performs transglycosylation reactions, overview
-
-
?
additional information
?
-
no hydrolysis of pullulan and cyclodextrin
-
-
?
additional information
?
-
-
no activity with alpha- and beta-cyclodextrins
-
-
?
additional information
?
-
-
no activity with alpha- and beta-cyclodextrins
-
-
?
additional information
?
-
-
hydrolysis of alpha-1,4-glucosidic linkages, glycogen and beta-cyclodextrin are poor substrates for AmyC, no activity with pullulan and maltose
-
-
?
additional information
?
-
-
hydrolysis of alpha-1,4-glucosidic linkages, glycogen and beta-cyclodextrin are poor substrates for AmyC, no activity with pullulan and maltose
-
-
?
additional information
?
-
AmyB enzymatic activity is negligible when acarbose, a maltotetraose is present, indicating that AmyB cleaves maltose units from the nonreducing end of maltooligosaccharides
-
-
?
additional information
?
-
-
AmyB enzymatic activity is negligible when acarbose, a maltotetraose is present, indicating that AmyB cleaves maltose units from the nonreducing end of maltooligosaccharides
-
-
?
additional information
?
-
inability to hydrolyze pullulan and beta-cyclodextrin with less than 10% of the specific activity of starch
-
-
?
additional information
?
-
-
inability to hydrolyze pullulan and beta-cyclodextrin with less than 10% of the specific activity of starch
-
-
?
additional information
?
-
AmyB enzymatic activity is negligible when acarbose, a maltotetraose is present, indicating that AmyB cleaves maltose units from the nonreducing end of maltooligosaccharides
-
-
?
additional information
?
-
inability to hydrolyze pullulan and beta-cyclodextrin with less than 10% of the specific activity of starch
-
-
?
additional information
?
-
-
key enzyme in digestive system
-
-
?
additional information
?
-
no substrates: granular starch or glycogen, maltose, maltotriose
-
-
?
additional information
?
-
-
alpha-Amylase production is highly dependent on starch availability and is supressed in the presence of glucose or other reducing sugars whereas the transformed Xanthomonas expressing the hyperthermophilic alpha-amylase from Pyrococcus woesei produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium
-
-
?
additional information
?
-
-
the digestive endo-type enzyme plays an essential role in the carbohydrate metabolism and energy production of the insect, Zabrotes subfasciatus is able to infest stored beans of Phaseolus vulgaris causing severe crop losses in Latin America and Africa
-
-
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
-
maltotriose + maltose, glucose is also formed
?
starch + H2O
additional information
-
-
soluble starch
after 24 h: 6.1% glucose, 18.0% maltose, 21.0% maltotriose, 1.3% maltotetraose, 1.3% maltopentaose and 1.1% maltohexaose
?
starch + H2O
additional information
-
-
corn starch
after 24 h: 6.1% glucose, 18.0% maltose, 21.0% maltotriose, 1.3% maltotetraose, 1.3% maltopentaose and 1.1% maltohexaose
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
after 24 h: 6.1% glucose, 18.0% maltose, 21.0% maltotriose, 1.3% maltotetraose, 1.3% maltopentaose and 1.1% maltohexaose
?
starch + H2O
additional information
-
-
corn starch
after 24 h: 6.1% glucose, 18.0% maltose, 21.0% maltotriose, 1.3% maltotetraose, 1.3% maltopentaose and 1.1% maltohexaose
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
enzyme form Amyl I hydrolyzes waxy maize starch to produce mainly maltose, maltotriose, and some maltooligosaccharides with higher degree of polymerization, the enzyme forms Amyl II and Amyl III produce maltose and some maltooligosaccharides of higher molecular weight than maltotetraose
?
starch + H2O
additional information
-
-
waxy corn starch
enzyme form Amyl I hydrolyzes waxy maize starch to produce mainly maltose, maltotriose, and some maltooligosaccharides with higher degree of polymerization, the enzyme forms Amyl II and Amyl III produce maltose and some maltooligosaccharides of higher molecular weight than maltotetraose
?
starch + H2O
additional information
-
-
soluble starch
enzyme form Amyl I hydrolyzes waxy maize starch to produce mainly maltose, maltotriose, and some maltooligosaccharides with higher degree of polymerization, the enzyme forms Amyl II and Amyl III produce maltose and some maltooligosaccharides of higher molecular weight than maltotetraose
?
starch + H2O
additional information
-
-
waxy corn starch
enzyme form Amyl I hydrolyzes waxy maize starch to produce mainly maltose, maltotriose, and some maltooligosaccharides with higher degree of polymerization, the enzyme forms Amyl II and Amyl III produce maltose and some maltooligosaccharides of higher molecular weight than maltotetraose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
after 15 min: formation of maltodextrins, after 60 min: formation of glucose + maltose + maltotriose + maltotetraose + maltohexaose + maltoheptaose
?
starch + H2O
additional information
-
-
soluble starch
after 15 min: formation of maltodextrins, after 60 min: formation of glucose + maltose + maltotriose + maltotetraose + maltohexaose + maltoheptaose
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
soluble starch
the major products are maltotriose + maltopentaose
?
starch + H2O
additional information
-
-
soluble starch
main products in the early stage of hydrolysis are maltopentaose, maltohexaose and maltoheptaose, on further incubation maltotriose and maltopentaose increase while maltohexaose, maltoheptaose and maltooctaose decrease
?
starch + H2O
additional information
-
-
soluble starch
initially produces large amounts of maltose and maltotriose. Gradually as the amount of maltotriose decreases the amounts of glucose and maltose increase
?
starch + H2O
additional information
-
-
soluble starch
major products: maltotriose + maltopentaose + maltohexaose + maltose
?
starch + H2O
additional information
-
-
soluble starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
soluble starch
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
initially produces large amounts of maltose and maltotriose. Gradually as the amount of maltotriose decreases the amounts of glucose and maltose increase
?
starch + H2O
additional information
-
-
soluble starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
soluble starch
the major products are maltotriose + maltopentaose
?
starch + H2O
additional information
-
-
soluble starch
main products in the early stage of hydrolysis are maltopentaose, maltohexaose and maltoheptaose, on further incubation maltotriose and maltopentaose increase while maltohexaose, maltoheptaose and maltooctaose decrease
?
starch + H2O
additional information
-
-
soluble starch
major products: maltotriose + maltopentaose + maltohexaose + maltose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
digestion of raw potato starch is almost as far as that of corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
sweet potato starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
waxy corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
wheat starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
digestion of raw potato starch is almost as far as that of corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
sweet potato starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
waxy corn starch
glucose + maltose + small amounts of maltooligosaccharides ranging from maltotriose to maltoheptaose
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
Bacteria SS71
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
main products of the 6 h reaction and the 18 h reaction are glucose, maltose, maltotriose and maltotetraose
?
starch + H2O
additional information
-
-
-
main products of the 6 h reaction and the 18 h reaction are glucose, maltose, maltotriose and maltotetraose
?
starch + H2O
additional information
-
-
-
one enzyme form produces maltose and maltohexaose, another form produces exclusively maltopentaose from polysaccharide substrates
?
starch + H2O
additional information
-
-
soluble starch
main products are maltose and maltotriose, minor products are maltotetraose and maltopentaose in the early stage of reaction. Small amounts of glucose are detected after 24 h
?
starch + H2O
additional information
-
-
soluble starch
main products are maltose and maltotriose, minor products are maltotetraose and maltopentaose in the early stage of reaction. Small amounts of glucose are detected after 24 h
?
starch + H2O
additional information
-
Gammarus palustris
-
-
predominant formation of maltotriose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
insoluble starch
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
main products are maltose, maltotriose, and higher dextrins
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
raw starches
-
-
?
starch + H2O
additional information
-
-
-
maltotetraose + maltopentaose are the main products
?
starch + H2O
additional information
-
-
-
maltohexaose is the main product
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
-
maltose + higher oligomers of glucose
?
starch + H2O
additional information
-
-
-
maltose + higher oligomers of glucose
?
starch + H2O
additional information
-
-
soluble starch
products in the late stage of reaction: maltose + maltotriose with less amounts of maltotetraose and maltopentaose and traces of glucose
?
starch + H2O
additional information
-
-
soluble starch
products in the late stage of reaction: maltose + maltotriose with less amounts of maltotetraose and maltopentaose and traces of glucose
?
starch + H2O
additional information
-
-
soluble starch
glucose + maltose + maltotriose + maltotetraose
?
starch + H2O
additional information
-
-
soluble starch
glucose + maltose + maltotriose + maltotetraose
?
starch + H2O
additional information
-
-
-
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
maltose and traces of maltotriose
?
starch + H2O
additional information
-
-
-
major products are maltotriose and maltose
?
starch + H2O
additional information
-
-
-
maltose and traces of maltotriose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
soluble starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
rice starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
yam starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
cassava starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
plantain starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
sorghum starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
cocyam starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
corn starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
soluble starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
rice starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
yam starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
cassava starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
plantain starch
mainly glucose and maltose
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
-
-
?
starch + H2O
additional information
-
-
-
maltotetraose + maltopentaose
?
starch + H2O
additional information
-
-
-
maltotetraose + maltopentaose
?
starch + H2O
additional information
-
-
-
production of high levels of maltose
?
starch + H2O
additional information
-
-
soluble starch
-
-
?
starch + H2O
additional information
-
-
-
production of high levels of maltose
?
starch + H2O
additional information
-
-
-
-
?
starch + H2O
additional information
-
-
-
glucose + maltose + maltotriose and maltotetraose are the principal products
?
starch + H2O
additional information
-
-
-
glucose + maltose + maltotriose and maltotetraose are the principal products
?
starch + H2O
additional information
-
-
-
maltohexaose + maltopentaose + maltotriose and low levels of glucose, maltose and maltotetraose
?
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Cr3+
-
140% relative activity at 10 mM
Cs+
-
1 mM, 1.13fold activation of wild-type enzyme
CuCl
-
1 mM, 34% inhibition
HgCl2
-
1 mM, 13% inhibition
KCN
Thermomonospora vulgaris
-
10 mM, 82% inhibition
MoO42-
-
10-100 mM, stimulates
Na2SO4
-
1 M, 4fold increase in activity
PMSF
activates 12% at 1 mM
PO43-
-
100 mM, stimulates
Rb+
1 mM, increases activity by 10%
Urea
-
132% relative activity at 8 mM urea for salivary gland alpha-amylase
ZnCl2
-
5 mM, pH 4.0, 55°C, 104% relative activity
Ag+
-
1 mM, pH 8.0, 24 h at 4°C, slight activation for Amy I and Amy II
Ag+
-
0.5 mM, enhances activity
Al3+
-
1 mM, pH 8.0, 24 h at 4°C, 110% and 73% residual activity for Amy I and Amy II, respectively
Al3+
-
120% relative activity at 10 mM
Ba2+
-
the activity is increased by approximately 15% by 1 mM Ba2+
Ba2+
measured activity about 8090%
Ba2+
-
35% increase of activity at 2 mM
Ba2+
-
1 mM, pH 8.0, 24 h at 4°C, 104% and 95% residual activity for Amy I and Amy II, respectively
Ba2+
-
163% relative activity at 5 mM, at 80°C and pH 5.0
Ba2+
-
1 mM, 2.24fold activation
Ba2+
activates 7.4% at 1 mM
Ba2+
-
5 mM, slight activation
Ba2+
activates 38% at 5 mM
Ca2+
-
-
Ca2+
calcium-dependent alpha-amylase, maximum activity at 2.5 mM CaCl2
Ca2+
Ca2+ ions have effects on the structure and thermal propeties of alpha-amylase (AGXA) from thermophilic Anoxybacillus sp. strain GXS-BL. With calcium ions, the values of Topt, T50, t1/2, Tm and DELTAH in enzyme AGXA are significantly higher than those of enzyme AGXA without calcium ions, showing calcium ions have stabilizing effects on alpha-amylase structure with the increased temperature. Four Ca2+ ions (Ca1-4)are bound to the model structure. Ca1 is in the region between domain A and domain B, coordinated by the N139, D182, H217, and E173 residues and three water molecules. Ca2 and Ca3 are both located in domain A, with Ca2 coordinated by the N44, N46, N49, D50, G63, and D65 residues and a water molecule, and Ca3 coordinated by the N92, E109, and E110 residues and three water molecules. Ca4 is in the region between domain A and domain C, coordinated by the E400 residue and five water molecules
Ca2+
activates slightly at 1-5 mM
Ca2+
-
increases the thermostability of the enzyme, two Ca2+ ions per enzyme molecule
Ca2+
-
stabilizes the partially purified enzyme against thermal inactivation
Ca2+
-
16% activation at 1 mM, although Ca2+ is a good stabilizer it cannot activate the enzyme significantly, Ca2+ shows 41% inhibition of the enzyme at 10 mM
Ca2+
-
1 Ca2+ bound per enzyme molecule
Ca2+
-
increases the thermostability of the enzyme, four Ca2+ ions per enzyme molecule
Ca2+
-
enhances the enzyme activity with 5 mM Ca2+, 120% relative activity, and with 10 mM 96% relative activity, pH 5.0, 50°C
Ca2+
the Ca2+-binding residue Asp233 affects significantly the alpha-amylase specific activity
Ca2+
-
increases the thermostability of the enzyme, five Ca2+ ions per enzyme molecule
Ca2+
presence of an extra Ca2+-binding region between the A and C domains responsible for higher thermostability of this enzyme
Ca2+
-
catalytic and/or structure-stabilizing Ca2+ ions are tightly bound to the enzyme
Ca2+
activates 9% at 1 mM, 59% at 10 mM
Ca2+
-
40 mM calcium acetate, enhances activity of membrane-bound enzyme to 268% of control
Ca2+
-
increases the thermostability of the enzyme, three Ca2+ ions per enzyme molecule
Ca2+
-
1 mM, 1.35fold activation of wild-type enzyme, 1.24fold activation of mutant enzyme L134R/S320A
Ca2+
activity not significantly enhanced in presence of 1 mM CaCl2
Ca2+
-
Bacillus subtilis alpha-amylase requires roughly 4times more calcium for full activity than other alpha-amylases of nonbacterial nature
Ca2+
2 ions per enzyme molecule
Ca2+
-
2-mercaptoethanol interfers with activation by Ca2+, glutathione enhances it
Ca2+
-
128% activity at 10 mM
Ca2+
-
the activity of the alpha-amylase AI is increased 1.5fold in the presence of 4 mM Ca2+
Ca2+
-
1 mM, pH 8.0, 24 h at 4°C, 105% and 106% residual activity for Amy I and Amy II, respectively
Ca2+
slightly activating at 5-10 mM
Ca2+
-
2 mM, about 1.2fold activation
Ca2+
-
180% relative activity at 5 mM, at 80°C and pH 5.0
Ca2+
-
200% relative activity at 10 mM
Ca2+
-
Ca2+ at 10 mM has only a slightly stimulating effect, the enzyme is Ca2+-independent
Ca2+
-
contains one gatom of Ca2+ per mol of enzyme
Ca2+
-
slightly improves enzymatic activity
Ca2+
-
stabilizes the enzyme
Ca2+
-
calcium stabilizes the conformation of alpha-amylase and also involved in substrate binding, but inhibits enzyme activity
Ca2+
-
197% relative activity at 20 mM Ca2+ for salivary gland alpha-amylase
Ca2+
-
slight activator at concentrations below 150 mM, activating only a maximum of 3% at 100 mM, and a slight inhibitor at higher concentrations (8% of the initial activity at 200 mM)
Ca2+
-
10 mM, 1.4fold activation
Ca2+
-
10 mM, increase of activity to 140%
Ca2+
-
strictly dependent, retaining below 20% activity in the absence of CaCl2. The optimal concentration is ca. 0.2 mM
Ca2+
-
AMY1 shows the highest activity at 5 mM calcium concentration and maintains its activity at a broad range from 0.1 to 10 mM of calcium ion. AMY2 shows the highest acitivity at 15-20 mM of calcium, compared with the lowest 20% of activity at 0.1 mM of calcium concentration, 37°C, substrate insoluble blue starch. There is no significant difference in hydrolyzing activity on the soluble starch substrate between AMY1 and AMY2, with the increase of calcium concentration. The increase in calcium up to 50 mM causes the decrease by 0-30% in the activity of both AMYs
Ca2+
-
10 mM, 1.35fold activation
Ca2+
-
no effect on enzyme activity by Ca2+, but structural stabilization of the protein molecule by calcium ions
Ca2+
highly activating at 5 mM
Ca2+
-
optimal activation at 15 mM
Ca2+
-
activates, activity profile
Ca2+
-
95% loss of activity after removal of Ca2+ by EDTA, addition of Ca2+ results in the recovery of 12% of the original activity, alpha-amylase III
Ca2+
in the crystal structure, one bound calcium ion is found, coordinated to the side chains of Asn100 and Asp167, the main-chains of Arg158 and His201, and three water molecules
Ca2+
activates 28.2% at 1 mM
Ca2+
in the presence of calcium, the affinity of the enzymes (wild type and mutants) toward starch is increased, the thermostability of the wild type and A53S mutant is calcium dependent at different temperatures, in the presence of 2 mM CaCl2 at 60°C, the percentage of residual activity in both the wild type and A53S mutant changes after 30 min of incubation
Ca2+
-
5 mM, required for activation
Ca2+
-
5 mM, about 70% activation
Ca2+
-
1 mM, 37°C, 30 min, pH 6.5, 148% relative activity
Ca2+
-
increases the thermostability of the enzyme, one Ca2+ ion per enzyme molecule
Ca2+
-
the enzyme is Ca2+-protein. Removal of Ca2+ by dialysis against water causes irreversible inactivation of the enzyme
Ca2+
activates 55% at 5 mM
Ca2+
1 mM, increases activity by 20%
Ca2+
-
activates 52% at 5 mM
Ca2+
2 mM, 127% of initial activity
CaCl2
-
the reusability of the immobilized enzymes are similar in starch hydrolysis reaction medium containing either 5 mM or 0.25 mM CaCl2
CaCl2
-
5 mM, slight activation
CaCl2
2 mM, pH 6.5, 50°C, 115% relative activity
CaCl2
-
76% activation of isozyme alpha-amylase I at 1 mM
CaCl2
-
maximal activity at 0.1 mM, higher concentrations inhibit activity
CaCl2
-
5 mM, pH 4.0, 55°C, 111% relative activity
CaCl2
-
incubated in different concentrations 0.5-100 mM at 25°C overnight, with 10 mM EDTA, significant activation, with two apparent dissociation constants K1: 0.3 mM and K2: 5.4 mM
chloride
presence of chloride ions is essential for activity. 20 mM NaCl is sufficient for maximum activity. NaCl is not inhibitory below 250 mM
chloride
-
is a weak allosteric enzyme activator
Cl-
Gammarus palustris
-
activates isoenzyme IC and IW
Cl-
-
10-100 mM, activates
Cl-
-
activation above 10 mM
Co2+
5 mM, strong stimulation
Co2+
-
58% activation at 1 mM
Co2+
-
activates the recombinant chimeric mutant amylase
Co2+
-
activates and enhances structural enzyme stability
Co2+
-
activation of isozyme BAA at 10 mM
Co2+
-
162% relative activity at 5 mM, at 80°C and pH 5.0
Co2+
-
1 mM, 3.06fold activation
Co2+
activates the recombinant chimeric mutant amylase
Co2+
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
Co2+
-
5 mM, about 70% activation
Co2+
1 mM CoCl2, slightly enhances activity
Co2+
-
0.5 mM, enhances activity
Cu2+
-
enhances the enzyme activity with 5 mM Cu2+, 120% relative activity, and with 10 mM 87% relative activity, pH 5.0, 50°C
Cu2+
measured activity about 8090%
Cu2+
-
slightly improves enzymatic activity
Cu2+
-
5 mM, slight activation
Cu2+
-
1 mM, 37°C, 30 min, pH 6.5, 100% relative activity
EDTA
-
112% relative activity at 2 mM EDTA for salivary gland alpha-amylase
EDTA
2 mM, pH 6.5, 50°C, 40% relative activity
Fe2+
-
activates
Fe2+
-
the activity is increased by approximately 15% by 1 mM Fe2+
Fe2+
-
1 mM, 2.72fold activation
Fe2+
-
5 mM, slight activation
Fe2+
activates 22% at 5 mM
Fe2+
-
0.5 mM, enhances activity
Fe3+
activates 152% at 1 mM
Fe3+
-
133% relative activity at 5 mM, at 80°C and pH 5.0
Fe3+
-
activates slightly
K+
activates 10% at 1 mM
K+
slightly activating at 5-10 mM
K+
-
105% relative activity at 10 mM
K+
-
131% relative activity at 5 mM, at 80°C and pH 5.0
K+
-
248% relative activity at 20 mM K+ for midgut alpha-amylase and 223% relative activity at 20 mM K+ for salivary gland alpha-amylase
K+
activity of the enzyme in KCl is equal to that in NACl, indicating that the type of monovalent cation is not critical to the activity
K+
-
slight activation of isozymes AI-1 and AII, slight inhibition of isozyme AI-2
K+
-
optimal activation at 10 mM
K+
-
5 mM, slight activation
K+
1 mM, increases activity by 16%
KCl
2 mM, pH 6.5, 50°C, 105% relative activity
KCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, 70°C, and pH 8.5
KCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, and retains about 6090% of the optimal activity at 23.5 M. The enzyme is less active in the presence of 0.51.5 M of each salt, and no activity is observed in absence of the salts. The inactivation at low-salt concentrations is reversible by increasing the salt concentration
Li+
slightly activating at 5-10 mM
Li+
-
slight activation of isozymes AI-1 and AI-2, slight inhibition of isozyme AII
Li+
-
5 mM, slight activation
Mg2+
-
required
Mg2+
-
13% activation at 1 mM
Mg2+
-
activates the recombinant chimeric mutant amylase
Mg2+
-
38% activation at 5 mM
Mg2+
-
118% relative activity at 5 mM, at 80°C and pH 6.5
Mg2+
-
the activity is increased by approximately 15% by 10 mM Mg2+
Mg2+
-
40 mM magnesium acetate, enhances activity of the membrane-bound enzyme to 216% of the control
Mg2+
2 ions per enzyme molecule
Mg2+
-
1 mM, pH 8.0, 24 h at 4°C, 111% and 107% residual activity for Amy I and Amy II, respectively
Mg2+
slightly activating at 5-10 mM
Mg2+
-
slightly improves enzymatic activity
Mg2+
-
1 mM, 1.72fold activation
Mg2+
activates the recombinant chimeric mutant amylase
Mg2+
-
inhibitor when added in concentrations from 50 mM to 200 mM. The maximum inhibitory effect is obtained at 100 mM, inhibiting only 10% of the initial activity
Mg2+
-
slight activation of isozymes AI-1 and AI-2, and AII
Mg2+
-
optimal activation at 10 mM
Mg2+
activates 6.9% at 1 mM
Mg2+
-
5 mM, slight activation
Mg2+
-
1 mM, 37°C, 30 min, pH 6.5, 98% relative activity
Mg2+
1 mM MhCl2, slightly enhances activity
Mg2+
activates 13% at 5 mM
Mg2+
-
activates 34% at 5 mM
MgCl2
-
1 mM, 22% inhibition
MgCl2
-
5 mM, pH 4.0, 55°C, 103% relative activity
Mn2+
-
activates
Mn2+
-
activates at 10 mM
Mn2+
measured activity about 8090%
Mn2+
-
1 mM, pH 8.0, 24 h at 4°C, 108% and 102% residual activity for Amy I and Amy II, respectively
Mn2+
-
140% relative activity at 10 mM
Mn2+
-
191% relative activity at 5 mM, at 80°C and pH 5.0
Mn2+
-
slightly improves enzymatic activity
Mn2+
-
1 mM, 1.34fold activation
Mn2+
-
activation of isozymes AI-1 and AI-2, and AII
Mn2+
-
1 mM, 37°C, 30 min, pH 6.5, 96% relative activity
Mn2+
-
0.5 mM, enhances activity
Na+
activates 15% at 1 mM
Na+
-
activation of isozyme BAA at 10 mM
Na+
activates 15% at 1 mM, 61% at 10 mM
Na+
-
activity is promoted by 0.5-2.0% NaCl
Na+
slightly activating at 5-10 mM
Na+
-
142% relative activity at 5 mM, at 80°C and pH 5.0
Na+
-
120% relative activity at 10 mM Na+ for midgut alpha-amylase and 183% relative activity at 20 mM Na+ for salivary gland alpha-amylase
Na+
-
optimal salinity: 10% NaCl
Na+
-
activation of isozymes AI-1 and AI-2, and AII
Na+
-
optimal activation at 5 mM
Na+
-
5 mM, slight activation
NaCl
-
the enzyme is stable against 1.5 M NaCl
NaCl
enzyme AmyD-1 displays extreme salt tolerance, with the highest activity in the presence of 2.0 M NaCl and 60.5% of activity in 5.0 M NaCl, 40% inhibition at 5 M
NaCl
-
the enzyme is resistant to 4.5% NaCl
NaCl
-
the enzyme is resistant to 11% NaCl
NaCl
Amy-E not only is halotolerant but also its activity is stimulated at high salt concentrations in the range of 1-5 M, activates 20% at 2 M
NaCl
2 mM, pH 6.5, 50°C, 100% relative activity
NaCl
-
AmyH is very halophilic, but is also active in absence of salt, denaturation by urea occurs only in absence of NaCl
NaCl
maximal activity at 2.6 M NaCl. 83% and 95% of the maximum activity are observed at 0.6 and 4.2 M NaCl, respectively
NaCl
-
optimal NaCl concentration in the absence of chloroform is 4.3 M. No activity is detected below 1.7 M NaCl. In the presence of chloroform, optimal NaCl concentration is 4.3 M, and activity is not detected below 0.9 M
NaCl
-
the enzyme is resistant against 4.5% NaCl
NaCl
-
maximal activity at 3 M NaCl
NaCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KC, 70°C, and pH 8.5
NaCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, and retains about 6090% of the optimal activity at 23.5 M. The enzyme is less active in the presence of 0.51.5 M of each salt, and no activity is observed in absence of the salts. The inactivation at low-salt concentrations is reversible by increasing the salt concentration
NaCl
activates, optimal at 2 M for highest enzyme activity, profile overview
NaCl
-
the enzyme is active over a broad range of salt concentrations, with optimum activity at 0.9 M. At 1.7, 2.6, and 4.3 M NaCl AmyB ist 80, 60, and 12% active, respectively. AmyB is a halophilic enzyme, but is still above 45% active in the absence of salt
NaCl
-
18% activation of isozyme alpha-amylase I at 1 mM, 21% at 10 mM
NaCl
-
activation above 10 mM, 28% activation at 250 mM
NaCl
-
the enzyme is stable against 3.5 M NaCl
NaCl
-
the enzyme is stable against 11-17%
NaCl
the enzyme is stable against 10-17%
NaCl
-
the enzyme is stable against 12%
NaCl
-
the enzyme is stable against 0.5-4.0 M, a salt-tolerant alpha-amylase
Ni2+
measured activity about 8090%
Ni2+
-
1 mM, 1.23fold activation
Ni2+
-
1 mM, 37°C, 30 min, pH 6.5, 100% relative activity
Ni2+
activates 19% at 5 mM
Pb2+
-
1 mM, pH 8.0, 24 h at 4°C, 101% and 87% residual activity for Amy I and Amy II, respectively
Pb2+
-
5 mM, slight activation
Pb2+
-
1 mM, 37°C, 30 min, pH 6.5, 91% relative activity
Pb2+
-
activates slightly
Sr2+
-
1 mM, 1.11fold activation of wild-type enzyme, no activation of mutant enzyme L134R/S320A
Sr2+
-
1 mM, 37°C, 30 min, pH 6.5, 92% relative activity
Zn2+
-
22% activation at 5 mM
Zn2+
-
5 mM, slight activation
additional information
-
alpha-amylase requires metal ions for activity and structural stability
additional information
Li+, Na+, K+, Co2+, Cu2+, Mg2+, Zn2+, and Fe3+ have no stimulatory effect on activity
additional information
-
no requirement for Ca2+
additional information
-
poor effects by Mg2+, Na+, Ni2+, Zn2+, Cu2+, Fe2+, and Ba2+
additional information
-
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
-
the enzyme is poorly affected by Ca2+, Mg2+, Li+, Cu2+, Ba2+, and Mn2+
additional information
-
BH072 alpha-amylase is a Ca2+-independent enzyme
additional information
-
the enzyme shows Ca2+-independency, no effect by Ca2+ at 1-5 mM. Poor effects by 1-5 mM of Na+, K+, and Mg2+
additional information
-
activity is not stimulated by the presence of Ca2+, Fe2+, Ba2+, K+, and Mn2+
additional information
-
no stimulation by Ca2+, no or poor effect on activity by Mn2+, Fe2+, and K+
additional information
-
the enzyme is Ca2+-independent
additional information
-
no activation by Ca2+ or other divalent cations
additional information
no or poor effects by Mg2+, K+, and Zn2+ at 1-10 mM
additional information
-
no or poor effects by Mg2+, K+, and Zn2+ at 1-10 mM
additional information
-
the enzyme shows no requirement for metals
additional information
-
not affected by Mg2+ and Cu2+
additional information
-
Li+ has negligible effect on activity
additional information
-
isozyme Amy3 is a chloride-independent alpha-amylase
additional information
isozyme Amy3 is a chloride-independent alpha-amylase
additional information
no or poor effects by 5-10 mM of Mn2+, Cu2+, Zn2+, and Fe2+
additional information
-
not stimulated by Na+
additional information
-
the enzyme is Ca2+-independent
additional information
-
the activity of the purified enzyme is Ca2+-independent
additional information
-
Ca2+-independent
additional information
-
does not require Ca2+ for its stability or activity
additional information
-
no quantitative change in the activity even at high concentrations of acrylamide, 0.05 to 0.6 mM. The addition of CsCl decreases the fluorescence quenching with no influence on enzyme activity
additional information
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
-
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory
additional information
-
when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory
additional information
-
alpha-amylase I is no affected by NaNO3, BaCl2, and MgCl2
additional information
-
no effect by 1 mM EGTA
additional information
-
no effect on isozymes by Ca2+
additional information
no effect by Mg2+ at 5 mM
additional information
-
not activated by several metal ions tested, including Ca2+ up to 10 mM
additional information
-
the enzyme is not affected by Mn2+ at 1-100 mM
additional information
poor effects by 1 mM of K+ and Na+
additional information
-
does not require Ca2+
additional information
the enzyme does not require Ca2+ for activity
additional information
-
the enzyme does not require Ca2+ for activity
additional information
-
does not require Ca2+
additional information
-
additional provision of Cl- (up to 30 mM NaCl) in the reaction mixture does not affect significantly the activity of alpha-amylases
additional information
calcium ions show neither inhibitory nor potentiating activity on alpha-amylase activity, alpha-amylase extracted from marine Streptomyces strain A3 is mainly calcium independent
additional information
-
no requirement for Ca2+
additional information
Ni2+ and Ca2+ do not stimulate the activity of AmyB
additional information
-
Ni2+ and Ca2+ do not stimulate the activity of AmyB
additional information
-
no effect by 5 mM Ni2+
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(2H)-1,4-benzoxazin-3(4H)-one
-
-
1,2,3,4,6-pentagalloyl-beta-D-glucose
-
mixed non-competitive inhibition, KEI: 0.0026 mM, KEIS: 0.0039 mM, tested in a concentration range of 0.04 to 0.5 mM, reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM inhibitor concentration, respectively, pH 6.0, 37°C
1-cyclohexyl-3-(morpholinyl-4-ethyl)-carbodiimide
-
40 mM, 50% inhibition after 20 min, 100 mM, 44% inhibition after 10 min in the presence of 1% starch
2,4-dihydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
2,4-Dinitro-1-fluorobenzene
-
6 mM
2-amino-7-hydroxyphenoxazine-3-one
-
-
2-amino-7-methoxyphenoxazine-3-one
-
-
2-amino-phenoxazine-3-one
-
-
2-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
2-hydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
3,4',5,7-tetrahydroxyflavanone
-
identified in the Sysygium cumini seed extract which results in 98% inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
CHAPS, 39.2% inhibition at 1% v/v
4-chloromercuribenzoate
-
98% inhibition of isozyme alpha-amylase I at 0.5 mM
4-chloromercuribenzoic acid
-
52% inhibition at 4 mM
4-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
4-hydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
5,5'-dithiobis-[2-nitrobenzoic acid]
-
10 mM, 35% inhibition
6-methoxy-benzoxazolin-2(3H)-one
-
-
7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
acacetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 14.1% maximum inhibition
Acalpha indica leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 15% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
acarviosine-glucose
binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis
acarviostatin 103
-
component isolated from Streptomyces sp. strain PW638, also inhibitory to alpha-glucosidase, EC 3.2.1.3
acarviostatin I03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin II03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin III03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin IV03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
Aegle marmelos leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 6% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
AlCl3
-
5 mM, complete inhibition
alpha-acarviosinyl-1,4-alpha-D-glucopyranosyl-1,6-D-glucopyranosylidene-spiro-thiohydantoin
-
i.e. PTS-G-TH, mixed-competitive type inhibition
alpha-AI-Pc1
-
alpha-amylase inhibitors from Phaseolus coccineus
-
alpha-AI1
-
alpha-amylase inhibitor 1 from cultivated Phaseolus vulgaris
-
alpha-AI2
-
alpha-amylase inhibitor 2 from wild Phaseolus vulgaris
-
alpha-amylase inhibitors from Dipteryx alata seeds
-
alpha-D-methylglucopyranose
-
-
alpha-D-phenylglucoside
-
-
alphaAI-PF
-
alpha amylase inhibitor from Palo Fierro seeds
-
ammonium persulfate
54% inhibition at 5 mM
ammonium sulfate
non-competitive inhibitor at concentrations higher than 20 mM
amylase wheat inhibitor
-
-
-
amylase-inhibitor
-
14 kinds of alpha-amylase inhibitors from Streptomyces sp. No. 280
-
apigenin-7-glucoside
-
IC50 is 0.17 mM
ascorbate
-
28.4% inhibition at 5 mM, 34.9% at 10 mM
ATP
-
90% inhibition at 5 mM, reversible by addition of Ca2+ or Mg2+
Benzene
-
10%, 40% inhibition
benzoxazolin-2(3H)-one
-
-
betulinic acid
-
identified in the Sysygium cumini seed extract which results in 98% inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
Bi2+
-
0.5 mM BiOCl2, 16% inhibition
Bio-tex
liquid commercial detergent, 75% residual activity
-
catechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 13.1% maximum inhibition
cetyltrimethylammonium bromide
-
CTAB
CH2ICOOH
-
10 mM, complete inhibition
Citric acid
-
25 mM, 54% inhibition
corosolic acid
-
triterpene acid isolated from Lagerstroemia speciosa leaves, weak inhibitory activity
Cs+
-
5 mM, 32% loss of activity
Cs2+
-
1 mM, 37°C, 30 min, pH 6.5, 89% relative activity
Cyclohexane
-
inhibitory effect of cyclooctane on amylase stability is stronger than that of cyclohexane
cyclooctane
-
inhibitory effect of cyclooctane on amylase stability is stronger than that of cyclohexane
cynarin
-
IC50 is above 2.0 mM
D-gluconic acid lactone
-
-
daidzein
-
a isoflavone, 0.888 mM, pH 6.0, room temperature, 23.3% maximum inhibition
dihydrocaffeic acid
-
IC50 is above 14.0 mM
diisopropyl fluorophosphate
-
1 mM, 34% inhibition of the membrane-bound enzyme
Dimethyl formamide
-
38.2% inhibition at 1 mM, 72.0% at 5 mM
diosmetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 19.2% maximum inhibition
dodecyltrimethylammonium bromide
epicatechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 10.3% maximum inhibition
eupafolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 99.4% maximum inhibition
FeCl3
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 21% loss of activity, alpha-amylase I
ferulic acid
-
IC50 is above 5.0 mM
fucoidan
-
fucoidan derived from algal species Ascophyllum nodosum and Fucus vesiculosus. Fucoidan extracted from Fucus vesiculosus does not inhibit alpha-amylase activity, while fucoidan from Ascophyllum nodosum decreases alpha-amylase activity by 7100% at 5 mg/ml. Both fucoidans are inhibitory to alpha-glucosidase, EC 3.2.1.20
genistein
-
a isoflavone, 0.888 mM, pH 6.0, room temperature, 25.1% maximum inhibition
genkwanin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 17.5% maximum inhibition
glucopyranosylidene-spiro-thiohydantoin
-
i.e. G-TH, mixed-competitive type inhibition
glucose
-
1 M, 34% inhibition. No inhibition up to 0.25 M
glucosyl-alpha-cyclodextrin
0.2%, 19% inhibition
Glutardialdehyde
-
0.4%, 57% loss of activity
Green Balance
solid commercial detergent, when used with tap water, 51% residual activity
-
guanidine hydrochloride
-
0.05 to 0.6 mM, as the concentraion is increased, the loss of of the whole conformational structure occurs and the relative activity decreases from 80% at 0.05 mM to 29% at 0.6 mM compared to the control, pH 8.0, 100°C
guanidinium hydrochloride
slight inhibition at 5-10 mM
Gymnema sylvestre leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 3% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
hesperetin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 39.8% maximum inhibition
Hg+
5 mM, complete inhibition
inhibitor from Amaranthus hybrid
-
no effect on alpha-amlyase at pH 6.0, but high inhibitory effect with maximal 80% at pH 9.0, 50°C
-
inhibitor from Phaseolus coccineus 35619
-
no effect at pH 9.0, inhibits the enzyme activity up to 78% at pH 6.0, 50°C
-
inhibitor from Phaseolus vulgaris cv. Radical
-
no effect at pH 9.0, inhibits the enzyme activity up to 87% at pH 6.0, 50°C
-
iodoacetamide
-
slight inhibition
isoacarbose
binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis, binding highly perturbs catalytic residue D300
Isoamylalcohol
-
70% inhibition at 10%, 90% at 20%
isochlorogenic acid
-
IC50 is 0.56 mM
isorhamnetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 35.4% maximum inhibition
kaempferol
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 34.5% maximum inhibition
KCN
-
25 mM, 70% inhibition
KI
-
0.05 to 0.6 mM, with 88% relative enzyme activity at 0.05 M decreasing to 42% at 0.6 mM compared to the control, also loss of fluorescence intensity, pH 8.0, 100°C
KSCN
-
500 mM, the reaction rate of acid-stable amylase decreases
L-Cys
-
25 mM, 26% inhibition
Limonia acidissimia seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 20% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
linear alkylbenzene sulfonate
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 71% residual relative activity, assay at 80°C and pH 5.6
luteolin-7-glucoside
-
IC50 is 0.28 mM
maltopentaose
-
30 mM, 51% inhibition
maltotetraose
-
30 mM, 51% inhibition
maltotriose
-
30 mM, 42% inhibition
MgSO4
2 mM, pH 6.5, 50°C, 75% relative activity
montbretin A
-
glycosylated acyl-flavonols, originally isolated from an extract of Crocosmia crocosmiiflora, measured in the presence and in the absence of 5 mM dithiothreitol, competitive inhibitor, more effective than montbretin B and C due to its free meta-hydroxyl group of the cinnamic acid moiety
montbretin B
-
glycosylated acyl-flavonols, originally isolated from an extract of Crocosmia crocosmiiflora, less effective than montbretin A due to the hydroxy group of montbretin A in the cinnamic acid moiety, respnsible for the tight binding
montbretin C
-
glycosylated acyl-flavonols, a methyl ether of the cinnamic acid moiety, originally isolated from an extract of Crocosmia crocosmiiflora, less effective than montbretin A due to the hydroxy group of montbretin A in the cinnamic acid moiety, respnsible for the tight binding
Moringa oleifera leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 16% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
1 mM, 22% loss of the activity of the membrane-bound enzyme
n-hexane
Cardamine battagliae
-
-
Na2-EDTA
-
0.01 M, 1% loss of activity after 1 h, in presence of 0.01 M CaCl2, complete inactivation after 1 h
naringenin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 26.9% maximum inhibition
NiCl2
-
30 mM, 39% inhibition
NiSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 79% loss of activity, alpha-amylase I
O-4,6-dideoxy-4-{[4,5,6-trihydroxy-3-hydroxymethyl-2-cyclohexen-1-yl]amino}-alpha-D-glucopyranosyl-(1-4)-O-alpha-D-glucopyranosyl-(1-4)-D-glucose
-
trivial name acarbose, uncompetitive inhibition vs. amylose and maltodextrin, mixed noncompetitive inhibition vs. maltoheptaose
p-chloromercuribenzoate
-
0.05 mM, 52% inhibition of intestine alpha-amylase, 68% inhibition of muscle alpha-amylase
p-hydroxymercuribenzoate
-
-
p-hydroxymercurybenzoate
activity severely inhibited, indicates the role of sulfydryl group in catalysis
PbCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 35% loss of activity, alpha-amylase I
PEG 8000
-
15-20% inhibition at 1-2%
-
phenyl methyl sulfonyl fluoride
-
1 mM, 70% inhibition
phenylmercuric acetate
-
-
phenylmethylsulfonyl fluoride
-
60% inhibition at 4 mM
polyethylene glycol 400
-
1500 Da PEG, inhibits the enzyme activity by 14% at 0.02% w/v
-
Propanol
-
30% inhibition at 10%, 50% at 20%
protein EDI-1
-
the alpha-amylase inhibitory fraction from Triticum dicoccon Schrank composed of emmer dimeric inhibitor 1 (EDI-1) and emmer dimeric inhibitor 2 (EDI-2) sharing very high identity levels with related proteins from Triticum aestivum
-
protein EDI-2
-
the alpha-amylase inhibitory fraction from Triticum dicoccon Schrank composed of emmer dimeric inhibitor 1 (EDI-1) and emmer dimeric inhibitor 2 (EDI-2) sharing very high identity levels with related proteins from Triticum aestivum
-
protein VrD1
-
an insecticidal plant defensin
-
proteinaceous inhibitor from wheat WI-1
inhibitor of isozyme Amy2 but not Amy1
-
proteinaceous inhibitor from wheat WI-3
-
-
Psidium guajava var. Pomiferum leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 98% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
quercetagetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 97.6% maximum inhibition
quercetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 82.1% maximum inhibition
Rhamnetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 8.1% maximum inhibition
rice bifunctional alpha-amylase/subtilisin inhibitor
-
purification, crystallization and preliminary X-ray crystallographic analysis of the inhibitor
-
rosmarinic acid
-
IC50 is 1.4 mM
scutellarein
-
a flavone, 0.888 mM, pH 6.0, room temperature, 98.4% maximum inhibition
Secale cereale inhibitor
-
Sinapic acid
-
IC50 is above 6.7 mM
Sn2+
-
1 mM, complete inhibition
Sodium citrate
-
23.1% inhibition at 5 mM
Sorghum procyanidin tetramer
P04745
thermodynamics, and binding and inhibition kinetics, overview
-
starch
-
concentrations above 32 g/l
Sysygium cumini seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, phenolics, terpenoids, and alkaloids are identified, mass spectrometry revlealed the presence of betulinic acid and 3,5,7,4'-tetrahydroxyflavanone, 98% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Tannic acid
-
IC50 is 0.14 mM
Tinospora cordifolia leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 13% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Trigonella foenum graecum seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 10% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Tris
starch-hydrolyzing activity in presence of Tris of different concentrations, pH 7.4, 37°C
Vigna unguiculata defensin
-
wheat alpha-amylase inhibitor 0.19
-
inhibitor 0.19 isolated from wheat kernels, inhibits both isozymes AoA1 and AoA2 in vitro and in vivo, stoichiometry of inhibition of isozymes, biological activity of inhibitor 0.19, overview
-
wheat alpha-amylase inhibitor 0.35
-
inhibitor 0.35 isolated from wheat kernels, inhibits both isozymes AoA1 and AoA2 in vitro and in vivo, stoichiometry of inhibition of isozymes, biological activity of inhibitor 0.53, overview
-
wheat amylase inhibitor
-
wheat seed amylase inhibitor
-
Zizyphus mauritiana seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 12% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
(NH4)2SO4
slight inhibition at 5-10 mM
1,10-phenanthroline
-
22% inhibition at 10 mM
1,10-phenanthroline
-
10.7% inhibition at 10 mM
1,10-phenanthroline
-
1 mM, 39% loss of activity of the membrane-bound enzyme
2-mercaptoethanol
-
37.6% inhibition at 1 mM, 43.7% at 5 mM
2-mercaptoethanol
-
87% residual activity at 5 mM
2-mercaptoethanol
-
20% inhibition at 1 mM, 30% at 5 mM
2-mercaptoethanol
85.9% inhibition at 1 mM
2-mercaptoethanol
-
1 mM, 23% loss of activity
2-mercaptoethanol
59% inhibition at 10 mM
4-bromophenacyl bromide
-
4-bromophenacyl bromide
-
complete inhibition at 4 mM
4-bromophenacyl bromide
19% inhibition at 2 mM
acarbose
-
-
acarbose
a pseudotetrasaccharide inhibitor of alpha-amylase and alpha-glucosidase, binding structure, overview
acarbose
enzyme binding and docking study
acarbose
Caloglyphus redickorzevi
-
-
acarbose
binding mechanism, acarbose rearrangement mechanism implied by the kinetic and structural analysis, and potential pathways of rearrangement, enzyme-inhibitor complex crystal structure analysis
acarbose
-
0.888 mM, pH 6.0, room temperature, 99.2% maximum inhibition
acarbose
-
IC50 is 0.023 mM
acarbose
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarbose
activity is reduced to 56.4% in the presence of 0.00002 mM of inhibitor and inhibition reaches 77% at 0.00008 mM concentration
acarbose
enzyme binding and docking study
acetone
inhibits 34% at 20% v/v, and 61% at 50% v/v
Ag+
-
-
Ag+
-
2 mM, 61.2% inhibition
Ag+
-
5 mM AgNO3, 82% inhibition
Ag+
-
1 mM, 50% loss of activity
Ag+
-
1 mM, 51% inhibition
Ag+
-
0.1 mM, 11% inhibition
Ag+
-
5 mM AgNO3, 95% inhibition
Ag+
-
2 mM, complete inhibition
Ag+
-
1 mM, 37°C, 30 min, pH 6.5, 36% relative activity
Ag+
-
1 mM AgCl2, 77% loss of activity
Ag2+
activity severely inhibited, indicates the role of sulfydryl group in catalysis
AgNO3
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 12% loss of activity, alpha-amylase I
AgNO3
-
2 mM, complete inhibition
Al3+
5 mM, weak inhibition
Al3+
-
2 mM, 38.7% inhibition
Al3+
-
1 mM, pH 8.0, 24 h at 4°C, 110% and 73% residual activity for Amy I and Amy II, respectively
Al3+
-
10 mM, 86% loss of activity
Al3+
-
10 mM, 58% inhibition
Al3+
-
10 mM, 90% inhibition
Al3+
-
complete inhibition of isozyme AI-1, nearly complete inhibition of isozyme AI-2, moderate inhibition of isozyme AII, at 5 mM
alpha-amylase inhibitors from Dipteryx alata seeds
-
-
-
alpha-amylase inhibitors from Dipteryx alata seeds
-
-
-
alpha-cyclodextrin
the addition of alpha-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
alpha-cyclodextrin
-
weak inhibition
alpha-cyclodextrin
-
1-10 mM, 25-35% inhibition
alpha-cyclodextrin
0.2%, 10% inhibition
Ba2+
-
5.3% inhibition at 1 mM, 11.1% at 5 mM
Ba2+
-
strong inhibition of isozyme BAA
Ba2+
-
5 mM BaCl2, 28% inhibition
Ba2+
-
1 mM, 23% inhibition of wild-type enzyme, 28% inhibition of mutant enzyme L134R/S320A
Ba2+
-
1 mM, pH 8.0, 24 h at 4°C, 104% and 95% residual activity for Amy I and Amy II, respectively
Ba2+
-
80% residual activity at 10 mM
Ba2+
-
0.1 M, complete inhibition
Ba2+
-
0.1 mM, 60% inhibition
Ba2+
-
slight inhibition of isozymes AI-1 and AI-2, and AII
Ba2+
-
5 mM BaCl2, 22% inhibition
Ba2+
-
1 mM, 37°C, 30 min, pH 6.5, 29% relative activity
Ba2+
-
1 mM BaCl2, 40% loss of activity
Ba2+
2 mM, 72% residual activity
BaCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 16% loss of activity, alpha-amylase I
BaCl2
-
5 mM, pH 4.0, 55°C, 25% relative activity
beta-cyclodextrin
the addition of beta-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
beta-cyclodextrin
-
1-10 mM, 10-25% inhibition
beta-cyclodextrin
0.2%, 19% inhibition
butanol
inhibits 15% at 20% v/v, and 21% at 50% v/v
butanol
-
10%, 80% inhibition
Ca2+
5 mM, weak inhibition
Ca2+
-
11.4% inhibition at 10 mM, 56.2% at 50 mM
Ca2+
7% inhibition at 1 mM
Ca2+
-
10 mM CaCl2, inhibition of enzyme form Amyl II and Amyl III, no inhibition of enzyme form Amyl I
Ca2+
-
0.01 M CaCl2, 3% loss of activity after 1 h, in presence of 0.01 M Na2-EDTA, complete inactivation after 1 h
Ca2+
-
16% activation at 1 mM, although Ca2+ is a good stabilizer it cannot activate the enzyme significantly, Ca2+ shows 41% inhibition of the enzyme at 10 mM
Ca2+
-
1 mM, 25-30% inhibition between pH 8.0 and 10.0
Ca2+
-
strong inhibition of isozyme BAA
Ca2+
60% inhibition at 5 mM
Ca2+
-
about 80% relative activity at 10 mM Ca2+
Ca2+
-
calcium stabilizes the conformation of alpha-amylase and also involved in substrate binding, but inhibits enzyme activity
Ca2+
-
40% residual activity at 20 mM Ca2+ for midgut alpha-amylase and 46% residual activity at 10 mM Ca2+ for salivary gland alpha-amylase
Ca2+
-
5 mM CaCl2, 21% inhibition
Ca2+
-
added alone Ca2+ is inhibitory
CaCl2
-
above 0.1 mM
CaCl2
-
4 mM, 30% inhibition
CaCl2
-
inhibition above 100 mM, approx. 50% inhibition at 500 mM
caffeic acid
-
IC50 is 4.8 mM
caffeic acid
-
mixed-type inhibition, almost all activities of isozymes PPA-I and PPA-II are lost in the presence of 4 mM
Cd2+
-
-
Cd2+
-
1 mM, 91% inhibition
Cd2+
-
2 mM, 43% inhibition
Cd2+
-
1 mM, 33% inhibition of wild-type enzyme, 48% inhibition of mutant enzyme L134R/S320A
Cd2+
-
1 mM, 40% loss of activity
Cd2+
-
10 mM, complete inhibition
Cd2+
-
complete inhibition of isozyme AII, high inhibition of isozymes AI-1 and moderate of AI-2, at 5 mM
Cd2+
-
2 mM, 65% inhibition
Cd2+
complete inhibition at 5 mM
Cd2+
Thermomonospora vulgaris
-
1 mM CdSO4, 82% inhibition
CdCl2
-
5 mM, 14% inhibition; 5 mM, 38% inhibition; 5 mM, 43% inhibition
CdCl2
-
30 mM, 95% inhibition
chlorogenic acid
-
IC50 is 1.4 mM
chlorogenic acid
-
5-caffeoylquinic acid, mixed-type inhibition, complete inhibition of isozymes PPA-I is observed at 1.5 mM and that of isozyme PPA-II is at 2.0 mM
Cl-
-
-
Co2+
63% inhibition at 1 mM
Co2+
-
11.1% inhibition at 1 mM, 89.4% at 5 mM
Co2+
-
16% residual activity at 5 mM
Co2+
27% inhibition at 1 mM, 68% at 10 mM
Co2+
-
5 mM, 16% inhibition
Co2+
-
1 mM, 17% loss of activity
Co2+
-
1 mM, pH 8.0, 24 h at 4°C, 92% and 93% residual activity for Amy I and Amy II, respectively
Co2+
-
70% residual activity at 10 mM
Co2+
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
Co2+
47% inhibition of wild-type and mutant enzymes at 5 mM
Co2+
-
5 mM CoCl2, 91% inhibition
Co2+
75.9% inhibition at 1 mM
Co2+
-
1 mM, 37°C, 30 min, pH 6.5, 23% relative activity
Co2+
-
1 mM CoCl2, 65% loss of activity
Co2+
inhibits 60% at 5 mM
Co2+
complete inhibition at 1 mM
Co2+
-
28% inhibition at 5 mM
CoCl2
-
30 mM, 50% inhibition
CoCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 22% loss of activity, alpha-amylase I
CoCl2
-
21% inhibition of isozyme alpha-amylase I at 0.5 mM, 29% at 5 mM
CoCl2
1 mM, 52% inhibition
Cu2+
5 mM, complete inhibition
Cu2+
-
addition to growth medium in logarithmic phase, maximum inhibition of about 70-80% of enzyme expression at 0.47 mM. Addition to enzyme assay, 38.2% inhibition at 1.5 mM
Cu2+
-
76% inhibition at 0.5 mM, complete inhibition at 1 mM
Cu2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Cu2+
54% inhibition at 1 mM, 76% at 5 mM
Cu2+
-
29% inhibition at 1 mM
Cu2+
-
25% inhibition at 5 mM
Cu2+
-
complete inhibition at 1-5 mM
Cu2+
-
strong inhibition of isozyme BAA
Cu2+
18% inhibition at 1 mM, 48% at 10 mM
Cu2+
-
2 mM, almost complete inhibition
Cu2+
-
5 mM CuSO4, 16% inhibition
Cu2+
-
1 mM, 55% inhibition of wild-type enzyme, 49% inhibition of mutant enzyme L134R/S320A
Cu2+
-
1 mM, 99% loss of activity
Cu2+
complete inhibition at 5 mM
Cu2+
-
7% residual activity at 2 mM
Cu2+
-
1 mM, 67% loss of activity
Cu2+
-
1 mM, 52% inhibition
Cu2+
-
1 mM, pH 8.0, 24 h at 4°C, 36% and 64% residual activity for Amy I and Amy II, respectively
Cu2+
-
1 mM, 28% inhibition
Cu2+
-
complete inhibition at 5 mM, at 80°C and pH 5.0
Cu2+
-
86% residual activity at 10 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
10 mM, 88% loss of activity
Cu2+
-
0.1 M, complete inhibition
Cu2+
-
10 mM, 58% inhibition
Cu2+
-
10 mM, 49% inhibition
Cu2+
-
nearly complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Cu2+
62% inhibition of wild-type and mutant enzymes at 5 mM
Cu2+
-
1 mM, 25% residual activity
Cu2+
-
5 mM CuSO4, complete inhibition
Cu2+
64.1% inhibition at 1 mM
Cu2+
-
2 mM, complete inhibition
Cu2+
5 mM, complete inhibition
Cu2+
-
complete inhibition at 4 mM
Cu2+
-
1 mM CuCl2, 28% loss of activity
Cu2+
inhibits 75% at 5 mM
Cu2+
Thermomonospora vulgaris
-
1 mM CuSO4, 82% inhibition
Cu2+
-
5 mM, 90% inhibition
Cu2+
52.2% residual activity at 1 mM
Cu2+
1 mM, 99% loss of activity
Cu2+
-
25% inhibition at 5 mM
Cu2+
2 mM, no residual activity
CuCl2
-
5 mM, 88% inhibition; 5 mM, 89% inhibition; 5 mM, 94% inhibition
CuCl2
-
10 mM, 95% inhibition
CuCl2
1 mM, complete inhibition
CuCl2
-
5 mM, pH 4.0, 55°C, 26% relative activity
CuSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 25% loss of activity, alpha-amylase I
CuSO4
2 mM, pH 6.5, 50°C, 50% relative activity
CuSO4
-
4 mM, complete inhibition
CuSO4
-
2 mM, 33% inhibition
Dextran
-
complete inhibition at 1%
Dextran
-
1%, 20% inhibition
dithiothreitol
inhibits the enzyme activity at concentrations higher than 80 mM
dithiothreitol
-
1 mM, 50% inhibition
DMSO
inhibits 20% at 20% v/v, and 31% at 50% v/v
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 40% inhibition at 60°C
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 20% inhibition at 60°C
DTNB
-
55.2% inhibition at 5 mM
DTNB
-
10 mM, complete inhibition
DTNB
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
DTT
-
61.9% inhibition at 1 mM, 84.8% at 5 mM
DTT
-
20% inhibition at 1 mM
DTT
20.1% inhibition at 1 mM
DTT
74% inhibition at 1 mM
EDTA
-
63% inhibition at 10 mM
EDTA
-
0.05 mM, 64% inhibition of intestine alpha-amylase, complete inhibition of muscle alpha-amylase
EDTA
-
30% inhibition at 10 mM, 20% at 5 mM
EDTA
-
80% of the enzyme activity is lost when the enzyme is incubated with 10 mM EDTA, indicating the enzyme is a metalloenzyme, pH 5.0, 50°C
EDTA
-
resistant at 30°C, inhibition at 90°C, inhibition is partially recovered by Cu2+ or Fe2+
EDTA
-
19.3% inhibition at 5 mM
EDTA
-
12% residual activity at 5 mM; BMA.2 belongs to the EDTA-sensitive alpha-amylases
EDTA
-
10 mM, 90% inhibition
EDTA
-
85% residual activity at 10 mM EDTA
EDTA
41% inhibition at 1 mM, 79% at 10 mM
EDTA
-
0.1 mM, 61.3% inhibition
EDTA
-
10 mM, 67% inhibition
EDTA
-
nearly complete inhibition at 1 mM
EDTA
-
50 mM, abolished 50% of the activity
EDTA
50% of the activity abolished in presence of 50 mM EDTA
EDTA
-
5 M, 32% loss of activity
EDTA
-
1 mM, pH 8.0, 24 h at 4°C, 98% and 76% residual activity for Amy I and Amy II, respectively
EDTA
slight inhibition at 5-10 mM
EDTA
-
10% residual activity at 5 mM, at 80°C and pH 5.0
EDTA
-
21% residual activity at 10 mM, alpha-amylase is completely inactivated after 6 min of incubation at 80°C in the presence of 5 mM EDTA
EDTA
-
over 80% inhibition at 1 mM
EDTA
AmyUS100DELTAG retains 40 and 25% of its original activity at 40 and 60°C, respectively, when incubated with 200 mM of EDTA, compared to 12 and 0% for AmyUS100
EDTA
-
1 mM, 36% inhibition
EDTA
-
37% residual activity at 4 mM EDTA for midgut alpha-amylase and 30% residual activity at 4 mM EDTA for salivary gland alpha-amylase
EDTA
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, complete loss of activity, alpha-amylase I
EDTA
-
515 mM, with or without chloroform
EDTA
-
pH 7.5, irreversible loss of activity, half-life: 29 h at 25 mM, 64 h at 12 mM, 670 h at 6 mM and 3500 at 3 mM
EDTA
-
92% inhibition of isozyme alpha-amylase I at 1 mM
EDTA
-
10 mM, 57% inhibition
EDTA
-
strong inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
EDTA
-
25 mM, 92% inhibition
EDTA
-
5 mM, 15% inhibition
EDTA
81.9% inhibition at 1 mM
EDTA
-
1-10 mM, about 60-65% inhibition
EDTA
-
0.01 M, 58% loss of activity
EDTA
-
5, 10, and 20 mM, pH 4.0, 55°C, 95% relative activity, enzyme is not sensitive to chelating agent, probably not a metalloenzyme
EDTA
-
1 mM, 85% loss of activity
EDTA
-
reverses stimulation by Ca2+
EDTA
Thermomonospora vulgaris
-
-
EDTA
Thermomonospora vulgaris
-
inhibition is completely nullified by Ca2+
EDTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
EDTA
-
2 mM, 25% inhibition
EDTA
1 mM, almost complete loss of activity
EDTA
-
10 mM, 5% inactivation after 5 min, complete inactivation after 4 h
EDTA
-
a distinct decrease of enzyme activity. The activity can not be regained after the addition of excess CaCl2, demonstrating the irreversibility of inactivation
EGTA
-
10 mM, 91% inhibition
EGTA
-
10 mM, 53% inhibition of the membrane-bound enzyme
EGTA
-
1-10 mM, about 50% inhibition
EGTA
-
5, 10, and 20 mM, pH 4.0, 55°C, 100% relative activity, enzyme is not sensitive to chelating agent, probably not a metalloenzyme
EGTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
ethanol
inhibits 9% at 20% v/v, and 18% at 50% v/v
ethanol
-
20% inhibition at 10%, 40% at 20%
ethanol
-
10%, 36% inhibition
Fe2+
-
-
Fe2+
8% inhibition at 1 mM, 27% at 5 mM
Fe2+
-
90% inhibition at 1-5 mM
Fe2+
-
35% inhibition at 5 mM
Fe2+
-
94.1% inhibition at 1 mM, complete inhibition at 5 mM
Fe2+
-
5 mM FeSO4, 71% inhibition
Fe2+
-
complete inhibition at 5 and 10 mM
Fe2+
-
1 mM, 47% loss of activity
Fe2+
-
1 mM, pH 8.0, 24 h at 4°C, 68% and 24% residual activity for Amy I and Amy II, respectively
Fe2+
-
2 mM, complete inhibition
Fe2+
-
10 mM, 90% loss of activity
Fe2+
-
0.1 M, complete inhibition
Fe2+
-
0.1 mM, 23% inhibition
Fe2+
strong inhibition of wild-type and mutant enzymes at 5 mM
Fe2+
-
5 mM FeSO4, 91% inhibition
Fe2+
55.3% inhibition at 1 mM
Fe2+
-
2 mM, 49% inhibition
Fe2+
-
1 mM, 37°C, 30 min, pH 6.5, 81% relative activity
Fe2+
-
1 mM FeCl2, 38% loss of activity
Fe2+
Thermomonospora vulgaris
-
10 mM, 86% inhibition
Fe2+
1 mM, 98% loss of activity
Fe3+
-
9% inhibition at 1 mM
Fe3+
-
complete inhibition at 1-5 mM
Fe3+
30% inhibition at 1 mM, 62% at 10 mM
Fe3+
-
2 mM, almost complete inhibition
Fe3+
complete inhibition at 5 mM
Fe3+
-
1 mM, 51% loss of activity
Fe3+
-
10% residual activity at 10 mM
Fe3+
-
10 mM, 95% loss of activity
Fe3+
-
10 mM, 92% inhibition
Fe3+
-
0.1 mM, 45% inhibition
Fe3+
-
complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Fe3+
-
1 mM, 37°C, 30 min, pH 6.5, 57% relative activity
Fe3+
-
5 mM, 90% inhibition
Fe3+
1 mM, complete loss of activity
FeCl2
-
5 mM, complete inhibition
FeCl2
-
5 mM, pH 4.0, 55°C, 85% relative activity
FeSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 86% loss of activity, alpha-amylase I
FeSO4
2 mM, pH 6.5, 50°C, 47% relative activity
FeSO4
-
4 mM, 80% inhibition
fisetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 85.6% maximum inhibition
fisetin
-
IC50 is 0.44 mM
gamma-cyclodextrin
the addition of gamma-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
gamma-cyclodextrin
0.2%, 18% inhibition
glycerol
-
0.05 mM, 68% inhibition of intestine alpha-amylase
glycerol
-
20-25% inhibition at 1-2%
glycerol
-
1%, 26% inhibition
glycine
-
almost complete inhibition at 1%
glycine
-
2%, 20% inhibition
H2O2
-
82.3% inhibition at 0.5%, 43.7% at 5 mM
Hg2+
-
addition to growth medium in logarithmic phase, 0.025 mM, no enzyme expression. Addition to enzyme assay, 69% inhibition at 0.5 mM
Hg2+
-
1 mM HgCl2, 89.5% inhibition
Hg2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 5 mM, 94% inhibition at 1 mM
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
partially reversed by Cys
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
complete inhibition at 5 and 10 mM
Hg2+
-
2 mM, almost complete inhibition
Hg2+
-
5 mM HgCl2, 98% inhibition
Hg2+
-
1 mM, complete inhibition of wild-type enzyme and mutant enzyme L134R/S320A
Hg2+
activity severely inhibited, indicates the role of sulfydryl group in catalysis
Hg2+
-
1 mM, complete inactivation
Hg2+
-
complete inhibition at 2 mM
Hg2+
-
2 mM, complete inhibition
Hg2+
-
1 mM, 82% loss of activity
Hg2+
-
1 mM, 25% inhibition
Hg2+
-
1 mM, pH 8.0, 24 h at 4°C, 35% and 31% residual activity for Amy I and Amy II, respectively
Hg2+
-
1 mM, 66% inhibition
Hg2+
-
complete inhibition at 5 mM, at 80°C and pH 5.0
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
10 mM, 88% loss of activity
Hg2+
-
0.1 M, 98% inhibition
Hg2+
-
10 mM, 55% inhibition
Hg2+
-
complete inhibition
Hg2+
-
10 mM, 98% inhibition
Hg2+
-
complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Hg2+
73% inhibition of wild-type and mutant enzymes at 5 mM
Hg2+
-
1 mM, 15% residual activity
Hg2+
-
5 mM HgCl2, 99% inhibition
Hg2+
-
5 mM, 28% inhibition
Hg2+
-
2 mM, complete inhibition
Hg2+
-
5 mM, 64% loss of activity
Hg2+
-
5 mM, 85% inhibition
Hg2+
-
complete inhibition at 4 mM
Hg2+
-
1 mM, 37°C, 30 min, pH 6.5, 44% relative activity
Hg2+
-
1 mM HgCl2, 88% inhibition
Hg2+
complete inhibition at 5 mM
Hg2+
-
0.5 mM HgCl2, 60% inhibition
Hg2+
complete inhibition at 1 mM
Hg2+
-
62% inhibition at 5 mM
HgCl2
-
5 mM, complete inhibition
HgCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 95% loss of activity, alpha-amylase I
HgCl2
-
10 mM, complete inhibition
HgCl2
-
4 mM, 71% inhibition
HgCl2
-
2 mM, complete inhibition
iodoacetate
-
around 100 mM
iodoacetate
-
0.5 mM, 98% inhibition
iodoacetate
-
1 mM, 60% inhibition
iodoacetate
Thermomonospora vulgaris
-
-
iodoacetic acid
5 mM
iodoacetic acid
-
0.05 mM, complete inhibition of intestine and muscle alpha-amylase
iodoacetic acid
-
88% inhibition of isozyme alpha-amylase I at 0.5 mM
iodoacetic acid
-
slight inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
K+
11% inhibition at 1 mM, 21% at 5 mM
K+
-
inhibits enzyme activity, 60 and 42% relative activity with 5 and 10 mM K+, pH 5.0, 50°C
K+
-
78% residual activity at 40 mM K+ for midgut alpha-amylase
K+
-
10 mM, 23% inhibition
K+
-
slight activation of isozymes AI-1 and AII, slight inhibition of isozyme AI-2
lauryl sulfobetaine
-
2.5 mM, approx. 30% inhibition at 60°C
lauryl sulfobetaine
-
2.5 mM, approx. 20% inhibition at 60°C
Li+
-
slight activation of isozymes AI-1 and AI-2, slight inhibition of isozyme AII
Li+
26.2% inhibition at 1 mM
luteolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 88.8% maximum inhibition
luteolin
-
IC50 is 0.17 mM
maltose
non-competitive inhibitor at concentrations higher than 20 mM
maltose
-
uncompetitive inhibition
maltose
-
0.25 M, 69% inhibition
maltose
-
86.2% relative inhibition, three concentrations of 10, 50, and 100 mM tested
maltose
-
product inhibition, the active site able to accomodate larger inhibitory complxes, resulting in a mixed type inhibition of starch hydrolysis
methanol
inhibits 7% at 20% v/v, and 13% at 50% v/v
methanol
-
20% inhibition at 10%, 40% at 20%
methanol
-
20%, 45% inhibition
Mg2+
-
-
Mg2+
22% inhibition at 1 mM
Mg2+
23% inhibition at 1 mM, 24% at 5 mM
Mg2+
-
shows no significant effect with 5 mM Mg2+, 92% relative activity, lead to inhibition with 10 mM, 48% relative activity, pH 5.0, 50°C
Mg2+
-
strong inhibition of isozyme BAA
Mg2+
-
1 mM, 11% inhibition of wild-type enzyme, 5% inhibition of mutant enzyme L134R/S320A
Mg2+
65% inhibition at 5 mM
Mg2+
-
10 mM, 50% loss of activity
Mg2+
-
82% residual activity at 2 mM
Mg2+
-
67% residual activity at 5 mM, at 80°C and pH 5.0
Mg2+
-
40% residual activity at 10 mM
Mg2+
-
30% inhibition at 1 mM, 50% at 5 mM
Mg2+
-
26% residual activity at 5 mM Mg2+ for midgut alpha-amylase and 28% residual activity at 10 mM Mg2+ for salivary gland alpha-amylase
Mg2+
-
0.1 M, 9% inhibition
Mg2+
-
10 mM, 13% inhibition
Mg2+
-
5 mM MgSO4, 18% inhibition
Mg2+
-
11% inhibition at 4 mM
Mg2+
-
1 mM MgCl2, 30% loss of activity
Mg2+
Thermomonospora vulgaris
-
10 mM MgCl2, 86% inhibition
Mg2+
-
added alone Mg2+ is inhibitory
Mg2+
69.4% residual activity at 1 mM
Mg2+
1 mM, 14% loss of activity
Mg2+
2 mM, 58% residual activity
Mn2+
5 mM, complete inhibition
Mn2+
-
inhibits enzyme activity, 50 and 21% relative activity with 5 and 10 mM Mn2+, pH 5.0, 50°C
Mn2+
-
7.1% inhibition at 1 mM, 22.4% at 5 mM
Mn2+
-
1 mM, 20% inhibition
Mn2+
-
strong inhibition of isozyme BAA
Mn2+
14% inhibition at 1 mM, 39% at 10 mM
Mn2+
-
2 mM, almost complete inhibition
Mn2+
-
complete inhibition at 1 mM
Mn2+
-
1 mM, 20% inhibition of wild-type enzyme, 15% inhibition of mutant enzyme L134R/S320A
Mn2+
70% inhibition at 5 mM
Mn2+
-
12% residual activity at 2 mM
Mn2+
-
2 mM, about 70% inhibition
Mn2+
-
80% inhibition at 1-5 mM
Mn2+
-
0.1 M, 85% inhibition
Mn2+
-
complete inhibition
Mn2+
-
5 mM MnCl2, 73% inhibition
Mn2+
49.1% inhibition at 1 mM
Mn2+
-
22% inhibition at 4 mM
Mn2+
-
1 mM, 55% loss of activity
Mn2+
inhibits 11% at 5 mM
Mn2+
Thermomonospora vulgaris
-
1 mM MnSO4, 84% inhibition
Mn2+
complete inhibition at 1 mM
Mn2+
1 mM, complete loss of activity
MnCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 46% loss of activity, alpha-amylase I
MnCl2
2 mM, pH 6.5, 50°C, 40% relative activity
MnCl2
1 mM, 55% inhibition
MnCl2
-
5 mM, pH 4.0, 55°C, 44% relative activity
myricetin
-
pH 7.0
myricetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 79% maximum inhibition
N-bromosuccinimide
1 mM
N-bromosuccinimide
-
6 mM
N-bromosuccinimide
-
0.1 mM, complete inhibition
N-bromosuccinimide
-
strong
N-bromosuccinimide
-
in the presence of 14 mM N-bromosuccinimide alpha-helix content and alpha-amlyase gt activity decrease with no observable change in beta-sheets, pH 8.0, 100°C
N-bromosuccinimide
-
1 mM, complete inhibition after 5 min
N-ethylmaleimide
-
slight inhibition
N-ethylmaleimide
-
1 mM, complete inhibition
N-ethylmaleimide
-
10 mM, 22% inhibition
Na+
-
-
Na+
12% inhibition at 1 mM, 28% at 5 mM
Na+
-
86% residual activity at 5 mM
Na+
-
alpha-amylase in 1 M NaCl and 5 mM NaCl retains 73% and 43% of its original activity after 24 h at 4ºC, respectively
Na+
-
25% residual activity at 5 mM Na+ for midgut alpha-amylase and 32% residual activity at 5 mM Na+ for salivary gland alpha-amylase
NaCl
83% of the initial activity remains in 2 M NaCl
NaCl
-
52% inhibition at 500 mM
NaCl
enzyme AmyD-1 displays extreme salt tolerance, with the highest activity in the presence of 2.0 M NaCl and 60.5% of activity in 5.0 M NaCl, 40% inhibition at 5 M
NaCl
-
the enzyme retains 63% and 40% of its original activity after 24 h at 4ºC, when NaCl concentration is 3 M and 5 M, respectively
NaCl
-
50% inhibition at 50 mM
NEM
-
-
NEM
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
Ni2+
-
addition to growth medium in logarithmic phase, maximum inhibition of enzyme expression of about 70-80% at 0.85 mM. Addition to enzyme assay, 11.5% inhibition at 1.5 mM
Ni2+
-
1 mM, 82% inhibition
Ni2+
-
5 mM NiCl2, 52% inhibition
Ni2+
-
complete inhibition at 1 mM
Ni2+
-
1 mM, 23% inhibition of wild-type enzyme, 24% inhibition of mutant enzyme L134R/S320A
Ni2+
-
73% residual activity at 2 mM
Ni2+
-
1 mM, 37% loss of activity
Ni2+
-
2 mM, about 15% inhibition
Ni2+
-
60% residual activity at 10 mM
Ni2+
-
no inhibition at 1 mM, 50% at 5 mM
Ni2+
-
10 mM, 58% loss of activity
Ni2+
-
10 mM, 42% inhibition
Ni2+
-
complete inhibition
Ni2+
-
10 mM, 59% inhibition
Ni2+
-
high inhibition of isozymes AI-1 and AI-2, and AII
Ni2+
-
5 mM NiCl2, 91% inhibition
Ni2+
65.9% inhibition at 1 mM
Ni2+
1 mM, 99% loss of activity
Pb2+
5 mM, complete inhibition
Pb2+
-
74.5% inhibition at 1 mM, complete inhibition at 5 mM
Pb2+
-
2 mM, 38% inhibition
Pb2+
-
1 mM, 48% loss of activity
Pb2+
-
1 mM, pH 8.0, 24 h at 4°C, 101% and 87% residual activity for Amy I and Amy II, respectively
Pb2+
-
90% inhibition at 1 mM
Pb2+
-
5 mM, 80% inhibition
Pb2+
-
10 mM, 45% inhibition
Pb2+
-
0.1 mM, 11% inhibition
Pb2+
80.6% inhibition at 1 mM
Pb2+
-
2 mM, 53% inhibition
Pb2+
-
1 mM, 50% loss of activity
Pb2+
1 mM, complete loss of activity
Pb2+
-
20% inhibition at 5 mM
PCMB
-
-
PCMB
-
0.5 mM, 20% inhibition
PCMB
-
1 mM, 92% loss of activity
PHMB
-
-
PMSF
-
36.5% inhibition at 1mM, 53.7% at 5 mM
PMSF
-
1 mM, 14% loss of activity of the membrane-bound enzyme
PMSF
-
complete inhibition at 1.5 mM
PMSF
-
10% inhibition at 1 mM, 90% at 5 mM
PMSF
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
PMSF
21.2% inhibition at 1 mM
quinic acid
-
IC50 is above 13.0 mM
quinic acid
-
poor inhibitor, activities higher than 80% remain for both isozymes even in the presence of 15 mM quinic acid, while they decrease sharply when the quinic acid concentration increases from 15 to 35 mM. Complete inhibition of isozyme PPAI is given with 35.0 mM, and that of isozyme PPA-II is with 40 mM quinic acid
Rb+
-
20 mM
Rb+
-
5 mM, 33% inhibition
Rb+
-
5 mM, 30% loss of activity
SDS
with 0.1%, 0.2% and 0.5% SDS, the enzyme shows 64%, 43% and 33% activity as compared with the activity in the absence of SDS
SDS
non-reversible inactivation
SDS
39% inhibition at 10%
SDS
-
61.8% inhibition at 0.1% w/v
SDS
-
retains 30 and 12% relative activity after inhibition with 5 and 10 mM SDS, respectively, pH 5.0, 50°C
SDS
-
14.9% inhibition at 2%
SDS
-
71% residual activity at 1% (v/v)
SDS
-
90% inhibition at 20 mM, complete inhibition at 80 mM
SDS
slight inhibition at 5-10 mM
SDS
-
40% inhibition at 0.1-0.2%
SDS
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 45% residual relative activity, assay at 80°C and pH 5.6
SDS
-
25% residual activity at 2 mM SDS for midgut alpha-amylase and 49% residual activity at 4 mM SDS for salivary gland alpha-amylase
SDS
71.0% inhibition at 1 mM
SDS
-
2%, pH 4.0, 55°C, 11% relative activity
SDS
1%, complete inactivation
SDS
39% inhibition at 60 mM
Secale cereale inhibitor
-
inhibitor is isolated from rye, Secale cereale, and active against alpha-amylase, dimeric crystal structure determination at 2.21 A resolution, overview
-
Secale cereale inhibitor
-
inhibitor is isolated from rye, Secale cereale, and active against alpha-amylase, dimeric crystal structure determination at 2.21 A resolution, overview
-
Sodium dodecyl sulfate
-
2.5 mM, approx. 60% inhibition at 60°C
Sodium dodecyl sulfate
-
2.5 mM, approx. 20% inhibition at 60°C
Sodium dodecyl sulfate
-
0.2%, 58% inhibition
sodium dodecylsulfate
-
-
sodium dodecylsulfate
0.1%, almost complete loss of activity
Sr2+
-
5 mM SrCl2, 36% inhibition
Sr2+
-
slight inhibition of isozymes AI-1 and AI-2, and AII
Sr2+
-
5 mM SrCl2, 28% inhibition
Triton X-100
45% inhibition at 10%
Triton X-100
-
12.4% inhibition at 10%
Triton X-100
-
83% residual activity at 5% (v/v)
Triton X-100
17% inhibition at 1 mM, 51.5% at 10 mM
Triton X-100
-
15% inhibition at 0.1%, 20% at 0.2%
Triton X-100
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 71% residual relative activity, assay at 80°C and pH 5.6
Triton X-100
-
0.2%, 40% inhibition
Triton X-100
-
18% inhibition
Tween 20
-
8.9% inhibition at 20%, 9.2% activation at 10%
Tween 20
-
85% residual activity at 5% (v/v)
Tween 20
-
20% inhibition at 0.1-0.2%
Tween 20
89.4% inhibition at 1% v/v
Tween 20
-
26% inhibition
Tween 80
-
8.3% inhibition at 20%
Tween 80
-
10% inhibition at 0.1%, 25% at 0.2%
Tween 80
adversely affects alpha-amylase in the immobilized state as compared to the free enzyme
Tween 80
-
22% inhibition
Tween-20
-
-
Tween-20
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 94% residual relative activity, assay at 80°C and pH 5.6
Tween-80
-
-
Tween-80
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 88% residual relative activity, assay at 80°C and pH 5.6
Urea
-
91% inhibition at 2 mM
Urea
64.5% inhibition at 1%
Urea
-
retains 58 and 16% relative activity after inhibition with 5 and 10 mM urea, respectively, pH 5.0, 50°C
Urea
-
8 M, 86% inhibition
Urea
-
87.5% inhibition at 8 M
Urea
slight inhibition at 5-10 mM
Urea
-
0.6 M, 50% decrease of enzyme activity compared to control, the circular dichroism spectra in the presence of urea reveals the unfolding of the enzyme which leads to changes in both alpha-helices as well as beta-sheets content. These conformational chages could be responsible for the decline in the alpha-amylase activity
Urea
-
19% residual activity at 8 mM urea for midgut alpha-amylase and 62% residual activity at 4 mM urea for salivary gland alpha-amylase
Urea
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
Urea
58.5% inhibition at 1 mM
Urea
-
5 M, pH 4.0, 55°C, 63% relative activity
Urea
51% inhibition at 6 M
Urea
25.8% residual activity at 1 mM
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 62% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 5% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, ca. 38% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
Vigna unguiculata defensin
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, ca. 12% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C, low inhibition activity in pig is probably related to extended loops in the structural core of the amylase, reducing the contact between defensin VuD1 and the catalytic site
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 60% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C, Lys1 from the defensin VuD1 appears to interact with residue Asp204 from the anylase ZSA, which is located inside the catalytic site, analyzed by in silico docking experiments
-
wheat amylase inhibitor
-
maximal inhibition at pH 7
-
wheat amylase inhibitor
a proteinaceous inhibitor
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
from Triticum aestivum; from Triticum aestivum
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
-
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
wheat flour protein inhibitor, formation of an enzyme-inhibitor complex
-
wheat amylase inhibitor
a proteinaceous inhibitor
-
wheat seed amylase inhibitor
-
-
-
wheat seed amylase inhibitor
-
-
-
wheat seed amylase inhibitor
-
-
Zn2+
5 mM, weak inhibition
Zn2+
-
addition to growth medium in logarithmic phase, 0.03 mM, about 50% inhibition of enzyme expression, at 1 mM 100% inhibition. Addition to enzyme assay, 36.3% inhibition at 1.5 mM
Zn2+
-
93% inhibition at 1 mM
Zn2+
36% inhibition at 1 mM
Zn2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Zn2+
26% inhibition at 1 mM, 73% at 5 mM
Zn2+
-
25% inhibition at 1 mM
Zn2+
-
88% inhibition at 1-5 mM
Zn2+
-
shows no significant effect with 5 mM Zn2+, 90% relative activity, lead to inhibition with 10 mM, 56% relative activity
Zn2+
-
59.2% inhibition at 1 mM, 94.3% at 5 mM
Zn2+
-
16% residual activity at 5 mM
Zn2+
-
1 mM, complete inhibition
Zn2+
-
strong inhibition of isozyme BAA
Zn2+
-
about 30% residual activity at 10 mM
Zn2+
-
2 mM 30.3% inhibition
Zn2+
-
5 mM ZnSO4, 95% inhibition
Zn2+
-
1 mM, 28% inhibition of wild-type enzyme, 37% inhibition of mutant enzyme L134R/S320A
Zn2+
-
1 mM, 87% inactivation
Zn2+
20% inhibition at 5 mM
Zn2+
-
22% residual activity at 10 mM
Zn2+
-
5% residual activity at 2 mM
Zn2+
-
1 mM, 78% loss of activity
Zn2+
-
1 mM, 87.6% inhibition
Zn2+
-
1 mM, pH 8.0, 24 h at 4°C, 94% and 64% residual activity for Amy I and Amy II, respectively
Zn2+
-
2 mM, about 85% inhibition
Zn2+
-
50% residual activity at 5 mM, at 80°C and pH 5.0
Zn2+
-
64% residual activity at 10 mM
Zn2+
-
10 mM, 80% loss of activity
Zn2+
-
0.1 M, 85% inhibition
Zn2+
-
10 mM, 60% inhibition
Zn2+
-
0.1 mM, 30% inhibition
Zn2+
-
complete inhibition of isozyme AI-1, high inhibition of isozymes AII and AI-2, at 5 mM
Zn2+
54% inhibition of wild-type and mutant enzymes at 5 mM
Zn2+
-
1 mM, 53% residual activity
Zn2+
-
5 mM ZnSO4, complete inhibition
Zn2+
80.5% inhibition at 1 mM
Zn2+
5 mM, complete inhibition
Zn2+
-
80% inhibition at 4 mM
Zn2+
-
1 mM, 37°C, 30 min, pH 6.5, 83% relative activity
Zn2+
-
1 mM ZnCl2, 45% loss of activity
Zn2+
inhibits 79% at 5 mM
Zn2+
-
0.5 mM ZnSO4, 43% inhibition
Zn2+
Thermomonospora vulgaris
-
10 mM, 84% inhibition
Zn2+
70.4% residual activity at 1 mM
Zn2+
-
35% inhibition at 5 mM
Zn2+
2 mM, no residual activity
ZnCl2
-
5 mM, 37% inhibition
ZnCl2
-
5 mM, 70% inhibition; 5 mM, 74% inhibition; 5 mM, 80% inhibition
ZnCl2
-
30 mM, complete inhibition
ZnCl2
-
10 mM, 93% inhibition
ZnCl2
1 mM, complete inhibition
ZnSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 47% loss of activity, alpha-amylase I
ZnSO4
2 mM, pH 6.5, 50°C, 37% relative activity
additional information
-
the enzyme activity is significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declines with increasing proteinaceous concentration. Proteinaceous extracts from Phaseolus vulgaris seeds are made from bean flour through heat treatment and dialysis
-
additional information
beta-mercaptoethanol, mannitol, glycerol, polyethylene glycol, and Triton X-100 do not have any significant effect even at high concentration
-
additional information
-
Cr6+ addition to growth medium in logarithmic phase, maximum inhibition of about 70-80% at 1.15 mM; effect of a combination of different concentrations of two (Ni2+ + Zn2+, Cu2+ + Zn2+, Hg2+ + Ni2+, Hg2+ + Zn2+) or three metals (Hg2+ + Zn2+ + Ni2+) added to the logarithmic growth phase examined: in all cases an inhibitory effect higher than of the single metal is observed; Mn2+ addition to growth medium in logarithmic phase, 10% inhibition at about 1.1 mM of enzyme expression
-
additional information
-
Vigna unguiculata defensin i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, no inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
additional information
-
no inhibition by Mn2+
-
additional information
-
the enzyme activity is not affected by Tween 20, Tween 40, Tween 60, and Tween 80 at 0.1% w/v
-
additional information
-
no or poor inhibition by Ba2+, K+, Ca2+, Mn2+, and Co2+ at 5-50 mM and by SDS, PMSF, Triton X-100, and Tween 20 at 1-5%
-
additional information
-
no effect by 5-10 mM of urea and glycerol, poor effects by 0.5-1% sodium tetraborate
-
additional information
-
no inhibition by PMSF; not inhibited by phenylmethylsulfonyl fluoride
-
additional information
-
not inhibited by 100 mM EDTA
-
additional information
-
not affected by NaCl, KCl, phenylmethylsulfonyl fluoride, and beta-mercaptoethanol
-
additional information
-
no inhibition by EGTA or EDTA at 1-10 mM
-
additional information
-
wild-type and mutant enzymes exhibit sensitivity towards GdnHCl-induced denaturation, effects of several commercial detergent products on the activities of the enzyme mutants, overview
-
additional information
-
the enzyme is resistant to SDS
-
additional information
-
mo inhibition by EDTA or EGTA
-
additional information
no effect by 5 mM EDTA
-
additional information
-
not inhibitory: EDTA, Ca2+
-
additional information
-
isozyme Amy3 is not inhibited by the proteinaceous inhibitor from bean alphaAI-1; isozymes Amy1 and Amy2 are not inhibited by the proteinaceous inhibitor from bean alphaAI-1 and by the proteinaceous inhibitor from wheat WI-3
-
additional information
isozyme Amy3 is not inhibited by the proteinaceous inhibitor from bean alphaAI-1; isozymes Amy1 and Amy2 are not inhibited by the proteinaceous inhibitor from bean alphaAI-1 and by the proteinaceous inhibitor from wheat WI-3
-
additional information
no or poor effects by glucose, sucrose, maltose, mannitol, trehalose, sorbitol, myo-inositol, and iodoacetate at 5-10 mM
-
additional information
-
not inhibited by phytic acid
-
additional information
-
no or poor effect by 10-20% of acetone and benzol
-
additional information
-
no inhibition by phytate at up to 10 mM
-
additional information
-
not inhibited by aromatic hydrocarbon (benzene, etc.)
-
additional information
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
-
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
-
no effect by the addtion of 0.1% dimethyl sulfoxide and 0.01% Triton X-100
-
additional information
-
the inhibitory activity of the flavonoids toward human alpha-amylase depends on the formation of 1. hydrogen bonds between the hydroxyl groups in position R7 and/or R4' of the polyphenol ligands and the catalytic residues of the binding site Asp197 and Glu233 and 2. formation of a conjugated pi-system between either the AC- or B-ring system and Trp59, that stabilizes the interaction with the active site
-
additional information
-
structure-activity relationship of benzoxazinones and related compounds in inhibition of the enzyme, overview
-
additional information
-
not inhibitory: D-glucose
-
additional information
not inhibitory: NaCl up to 250 mM
-
additional information
-
not inhibitory: NaCl up to 250 mM
-
additional information
-
treatment with glycosidases leads to loss of 50% activity
-
additional information
-
no inhibition with Murraya koenigii leaf extract
-
additional information
-
no inhibition with voglibose, 23-hydroxyursolic acid, maslinic acid, asiatic acid, arjunolic acid, and oleanolic acid
-
additional information
enzyme inhibition by lotus leaf flavonoids, LLF, commercial leaf extract preparation including the aglycones quercetin, myricetin, kaempferol, isorhamnetin and diosmetin, inhibitory kinetics and mechanism of flavonoids from lotus (Nelumbo nucifera Gaertn.) leaf against pancreatic alpha-amylase, overview. Binding analysis reveals that binding of LLF to alpha-amylase changes the conformation and microenvironment of alpha-amylase, resulting in inhibition of the enzyme activity. Thus LLF have the potential to be an ingredient in functional food for the prevention of type-2 diabetes. The crude extract of Nelumbo nucifera Gaertn. leaf flavonoids show high inhibitory activity against porcine pancreatic alpha-amylase with IC50 values of 2.20 mg/ml in vitro biochemistry tests
-
additional information
-
no inhibition by the plant defensin VrD2. A VrD2 chimera that is produced by transferring the proposed functional loop of VrD1 onto the structurally equivalent loop of VrD2 inhibits alpha-amylase activity
-
additional information
enzyme TfAmy48 shows excellent compatibility with some commercial laundry detergents, overview. No or poor effects by 1 mM PMSF, 2 mM diiodopropyl fluorophosphate, 10 mM EDTA, or 1 mm EGTA
-
additional information
-
enzyme TfAmy48 shows excellent compatibility with some commercial laundry detergents, overview. No or poor effects by 1 mM PMSF, 2 mM diiodopropyl fluorophosphate, 10 mM EDTA, or 1 mm EGTA
-
additional information
-
the enzyme is inhibited by several metal ions
-
additional information
EDTA, dithiothreitol, N-bromosuccinimide, 2-mercaptoethanol (1 mM), and SDS (2% (w/v)) have no effect on activity
-
additional information
-
EDTA, dithiothreitol, N-bromosuccinimide, 2-mercaptoethanol (1 mM), and SDS (2% (w/v)) have no effect on activity
-
additional information
Li+ and Na+ do not show significant inhibitory effect
-
additional information
-
Li+ and Na+ do not show significant inhibitory effect
-
additional information
-
from Peganum harmala, Centaurium erythraea and Aristolochia baetica causes strong inhibition of alpha-amylase activity
-
additional information
-
no inhibitionj by alphaAI-PF, i.e. alpha amylase inhibitor from Palo Fierro seeds
-
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2.3
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.8, 30°C, recombinant AMY1-SBD fusion enzyme
0.45 - 1.3
2-chloro-4-nitrophenyl alpha-maltotrioside
0.6 - 10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
3.6 - 12.5
2-chloro-4-nitrophenyl-alpha-D-maltotrioside
0.01 - 0.281
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
0.45
4,6-ethylidene-[G7]-p-nitrophenyl[G1]-alpha-D-maltoheptaoside
-
37°C, pH 6.0
0.065 - 0.26
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
2.46
4-nitrophenyl alpha-D-maltohexaoside
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
4.48 - 4.63
4-nitrophenyl-alpha-D-maltoside
11.1
acarbose
-
pH 4.5, 90°C, recombinant enzyme
2.61 - 52
alpha-cyclodextrin
4.5
alpha-maltosyl fluoride
-
30°C, pH 7.0
0.51
alpha-maltotriosyl fluoride
-
30°C, pH 7.0
0.12 - 2.36
amylose DP17
-
0.23
amylose DP440
-
pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme
-
2.16 - 13.6
beta-cyclodextrin
3.6
cyclomaltohexaose
-
-
16.7
Dextrin
-
micromol of D-glucosidic bond per liter
2.35 - 5.12
gamma-cyclodextrin
0.3 - 1.5
insoluble blue starch
-
0.071 - 0.079
maltodextrin
0.21 - 3.37
maltoheptaose
2.28
maltohexaitol
-
at pH 7.3, at 30°C
0.06 - 0.27
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
0.000624 - 3.05
soluble starch
-
additional information
amylopectin
0.45
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.1 mM NO3-
0.57
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM N3-
0.58
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.2 mM ClO3-
0.58
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM NO3-
0.69
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM N3-
0.76
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM Cl-
1.2
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM Br-
1.3
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM I-
0.6
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212W
0.669
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380A
0.67
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y380A mutant, pH 5.5, 30°C, kcat/Km: 28 1/s/mg/ml
0.7
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
wild-type enzyme, pH 5.5, 30°C, kcat/Km: 38 1/s/mg/ml
0.724
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380F
0.735
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme S378T
0.758
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
alpha-amylase 1
0.861
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme S378P
0.87
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y380M mutant, pH 5.5, 30°C, kcat/Km: 39 1/s/mg/ml
0.871
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380M
0.91
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
H395A mutant, kcat below 10 1/s, pH 5.5, 30°C
1.16
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
-
malt enzyme
1.3
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105W
1.4
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212P
1.4
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y380A/H395A mutant, pH 5.5, 30°C, kcat/Km: 25 1/s/mg/ml
1.7
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, wild-type enzyme
2
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212Y
2.49
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
-
recombinant enzyme
3.1
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105A/T212W
4.9
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105F
6
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105A/T212Y
10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
above, pH 5.5, 37°C, mutant Y105A
10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y105A mutant, Km above 10 mM, kcat below 10 1/s, pH 5.5, 30°C
10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y105A/Y380A mutant, Km above 10 mM, pH 5.5, 30°C, kcat/Km: 1300 1/s/mg/ml
10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
Y105A/Y380M mutant, Km above 10 mM, kcat below 10 1/s, pH 5.5, 30°C
3.6
2-chloro-4-nitrophenyl-alpha-D-maltotrioside
-
commercial substrate, pH 7.0
12.5
2-chloro-4-nitrophenyl-alpha-D-maltotrioside
-
22°C, pH 6.1
0.01
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, kcat/Km: L134R/S320A, 680000 1/s/M, 25°C, pH 6.0
0.0113
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 740000 1/s/M, 25°C, pH 6.0
0.0117
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 710000 1/s/M, 25°C, pH 6.0
0.012
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 770000 1/s/M, 25°C, pH 6.0
0.137
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1910000 1/s/M, 37°C, pH 4.5
0.147
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 1420000 1/s/M, 37°C, pH 6.5
0.171
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1350000 1/s/M, 37°C, pH 4.5
0.185
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 37°C, pH 5.5
0.186
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1210000 1/s/M, 37°C, pH 4.5
0.19
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1100000 1/s/M, 37°C, pH 6.5
0.193
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1070000 1/s/M, 37°C, pH 5.5
0.2
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1230000 1/s/M, 37°C, pH 5.5
0.201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 920000 1/s/M, 37°C, pH 6.5
0.201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 870000 1/s/M, 37°C, pH 5.5
0.205
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 880000 1/s/M, 37°C, pH 6.5
0.281
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 140000 1/s/M, 37°C, pH 4.5
0.065
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
0.065
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
0.13
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
0.223
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
0.23
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
0.26
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
4.48
4-nitrophenyl-alpha-D-maltoside
-
isozyme PPA-I, at pH 6.9 and 30°C
4.63
4-nitrophenyl-alpha-D-maltoside
-
isozyme PPA-II, at pH 6.9 and 30°C
2.61
alpha-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
14.9
alpha-cyclodextrin
-
pH 5.6, 40°C
52
alpha-cyclodextrin
-
-
3.5
amylopectin
-
calculated as low molecular weight products
18.2
amylopectin
-
micromol of D-glucosidic bond per liter
0.00016
amylose
-
30°C, pH 5.5
0.00021
amylose
-
30°C, pH 5.5
0.26
amylose
-
calculated as low molecular weight products
0.38
amylose
-
DP 17, malt enzyme, calculated as low molecular weight products
0.45
amylose
-
DP 17, recombinant enzyme, calculated as low molecular weight products
0.77
amylose
-
short chain
3.25
amylose
pH 6.5, 40°C, recombinant enzyme
15
amylose
-
short chain amylose, as anhydro-glucose units
18.2
amylose
-
micromol of D-glucosidic bond per liter
0.12
amylose DP17
pH 5.5, 37°C, mutant T212Y
-
0.29
amylose DP17
pH 5.5, 37°C, mutant T212W
-
0.37
amylose DP17
-
pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme
-
0.48
amylose DP17
pH 5.5, 37°C, mutants Y105W and T212P
-
0.57
amylose DP17
pH 5.5, 37°C, wild-type enzyme
-
0.58
amylose DP17
pH 5.5, 37°C, mutant Y105F
-
2
amylose DP17
pH 5.5, 37°C, mutant Y105A/T212W
-
2.27
amylose DP17
pH 5.5, 37°C, mutant Y105A/T212Y
-
2.36
amylose DP17
below, pH 5.5, 37°C, mutant Y105A
-
2.16
beta-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
12.3
beta-cyclodextrin
-
pH 5.6, 40°C
13.6
beta-cyclodextrin
-
-
2.35
gamma-cyclodextrin
-
pH 5.6, 40°C
4.4
gamma-cyclodextrin
-
-
5.12
gamma-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
9.6
glycogen
-
pH 7.0, 40 °C, alpha-amylase I
36.4
glycogen
-
from rat liver, calculated as low molecular weight products
51.1
glycogen
-
from oyster, calculated as low molecular weight products
0.3
insoluble blue starch
pH 5.5, 37°C, mutant T212W
-
0.3
insoluble blue starch
pH 5.5, 37°C, mutant Y105A/T212W
-
0.4
insoluble blue starch
below, pH 5.5, 37°C, mutant Y105A
-
0.4
insoluble blue starch
pH 5.5, 37°C, mutant Y105F
-
0.4
insoluble blue starch
pH 5.5, 37°C, wild-type enzyme
-
0.5
insoluble blue starch
pH 5.5, 37°C, mutant Y105W
-
0.6
insoluble blue starch
pH 5.5, 37°C, mutant T212Y
-
1
insoluble blue starch
pH 5.5, 37°C, mutant Y105A/T212Y
-
1.5
insoluble blue starch
pH 5.5, 37°C, mutant T212P
-
0.071
maltodextrin
-
30°C, pH 5.5
0.079
maltodextrin
-
30°C, pH 5.5
0.21
maltoheptaose
-
30°C, pH 5.5
0.22
maltoheptaose
-
30°C, pH 5.5
1.42
maltoheptaose
pH 6.5, 40°C, recombinant enzyme
3.37
maltoheptaose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
0.43
maltohexaose
-
-
0.71
maltohexaose
-
pH 5.6, 40°C
0.12
maltopentaose
-
-
0.55
maltopentaose
-
pH 5.6, 40°C
1.69
maltopentaose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
1.92
maltopentaose
pH 6.5, 40°C, recombinant enzyme
2.86
maltose
pH 6.5, 40°C, recombinant enzyme
6.4
maltose
-
pH 5.6, 40°C
0.48
maltotetraose
-
pH 5.6, 40°C
0.65 - 1.33
maltotetraose
-
value depends on assay method
0.198
maltotriose
-
-
1.26
maltotriose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
2.28
maltotriose
pH 6.5, 40°C, recombinant enzyme
28.6
maltotriose
-
pH 5.6, 40°C
62.9
maltotriose
-
pH 4.5, 90°C, recombinant enzyme
0.06
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 8.0, F256W mutant
0.27
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 8.0, wild-type
0.57
pullulan
-
mutant Y374A
1.4
pullulan
-
wild-type enzyme
4.13
pullulan
-
pH 5.6, 40°C
20
pullulan
-
calculated as low molecular weight products
0.000624
soluble starch
-
pH 8.0, 55°C
-
0.057
soluble starch
-
pH 5.5, 50°C
-
0.07
soluble starch
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
-
0.13
soluble starch
pH 6.5, 40°C, recombinant enzyme
-
1.2
soluble starch
-
pH 9.0, 52-55°C
-
1.7
soluble starch
-
pH 6.5, 60°C
-
1.9
soluble starch
-
pH 10.0, 40°C
-
1.92
soluble starch
-
pH 5.9, 37°C
-
3.05
soluble starch
-
pH 5.5, 80°C
-
0.005
starch
-
pH 7.0, 55°C
0.16
starch
-
pH 5.6, 40°C
0.19
starch
-
mutant Y374A
0.23
starch
-
wild-type enzyme
0.52
starch
-
pH 4.5, 90°C, recombinant enzyme
3.3
starch
-
soluble starch, Merck, calculated as low molecular weight products
4.3
starch
-
soluble starch, Zulkowsky type starch, calculated as low molecular weight products
6.5
starch
-
pH 7.0, 40°C, alpha-amylase I
18.7
starch
-
micromol of D-glucosidic bond per L
25.1
starch
mutant enzyme D233N
157
starch
mutant enzyme D231N
161.7
starch
mutant enzyme D438G
167.6
starch
wild type enzyme
additional information
amylopectin
-
0.0012 mg/ml, intestine alpha-amylase
additional information
amylopectin
-
0.002 mg/ml, muscle alpha-amylase
additional information
amylopectin
Km value is 1.9 ml/ml at 5°C, pH 8.3 and 2.5 mg/ml at 15°C, pH 8.3
additional information
amylopectin
-
Km-value: 10.3 mg/ml, pH 7.0, 50°C
additional information
amylopectin
-
Km-value: 8.95 mg/ml, 45°C, pH 5.0
additional information
amylopectin
Km-value: 8.95 mg/ml, 45°C, pH 5.0
additional information
amylose
-
0.002 mg/ml, intestine alpha-amylase
additional information
amylose
-
0.004 mg/ml, muscle alpha-amylase
additional information
amylose
-
0.1 mg/ml, 37°C, pH 5.3
additional information
amylose
-
0.11 mg/ml, 37°C, pH 5.3
additional information
amylose
0.13 mg/ml, wild-type enzyme, pH 5.5, 30°C, kcat/Km: 1300 1/s/mg/ml
additional information
amylose
-
0.13 mg/ml, wild-type enzyme, pH 5.5, 30°C, kcat/Km: 1300 1/s/mg/ml
additional information
amylose
0.19 mg/ml, H395A mutant, pH 5.5, 30°C, kcat/Km: 394 1/s/mg/ml
additional information
amylose
-
0.19 mg/ml, H395A mutant, pH 5.5, 30°C, kcat/Km: 394 1/s/mg/ml
additional information
amylose
0.30 mg/ml, Y380A/H395A mutant, pH 5.5, 30°C, kcat/Km: 543 1/s/mg/ml
additional information
amylose
-
0.30 mg/ml, Y380A/H395A mutant, pH 5.5, 30°C, kcat/Km: 543 1/s/mg/ml
additional information
amylose
0.35 mg/ml, Y380M mutant, pH 5.5, 30°C, kcat/Km: 425 1/s/mg/ml
additional information
amylose
-
0.35 mg/ml, Y380M mutant, pH 5.5, 30°C, kcat/Km: 425 1/s/mg/ml
additional information
amylose
0.36 mg/ml, Y380A mutant, pH 5.5, 30°C, kcat/Km: 264 1/s/mg/ml
additional information
amylose
-
0.36 mg/ml, Y380A mutant, pH 5.5, 30°C, kcat/Km: 264 1/s/mg/ml
additional information
amylose
1.0 mg/ml, Y105A/Y380M mutant, pH 5.5, 30°C, kcat/Km: 56 1/s/mg/ml
additional information
amylose
-
1.0 mg/ml, Y105A/Y380M mutant, pH 5.5, 30°C, kcat/Km: 56 1/s/mg/ml
additional information
amylose
1.2 mg/ml, Y105A/Y380A mutant, pH 5.5, 30°C, kcat/Km: 51 1/s/mg/ml
additional information
amylose
-
1.2 mg/ml, Y105A/Y380A mutant, pH 5.5, 30°C, kcat/Km: 51 1/s/mg/ml
additional information
amylose
1.4 mg/ml, Y105A mutant, pH 5.5, 30°C, kcat/Km: 132 1/s/mg/ml
additional information
amylose
-
1.4 mg/ml, Y105A mutant, pH 5.5, 30°C, kcat/Km: 132 1/s/mg/ml
additional information
amylose
-
Km: 2.34 mg and Vmax: 3.047 mg/min
additional information
amylose
-
Km-value: 6.17 mg/ml, 45°C, pH 5.0
additional information
amylose
Km-value: 6.17 mg/ml, 45°C, pH 5.0
additional information
Ascaris suum glycogen
-
0.0002 mg/ml, muscle alpha-amylase
-
additional information
Ascaris suum glycogen
-
0.0018 mg/ml, intestine alpha-amylase
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Thermomonospora vulgaris
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Gammarus palustris
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
0.572 mg/ml for soluble starch
-
additional information
additional information
-
0.39 mg/ml for starch
-
additional information
additional information
-
1.6 mg/ml for starch
-
additional information
additional information
-
1.0 g/l for starch
-
additional information
additional information
-
4.4 mg/ml for starch
-
additional information
additional information
-
0.362 g/ml for enzyme form alpha-I, 0.379 g/ml for enzyme form alpha-II, 0.542 g/ml for enzyme form alpha-III
-
additional information
additional information
-
2.5 mg/ml for starch
-
additional information
additional information
-
2.0 g/l for starch
-
additional information
additional information
-
2.3 mg/ml for soluble starch
-
additional information
additional information
-
1.64 mg/ml for soluble starch
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
detailed kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
isothermal titration and microcalorimetric analysis, thermodynamics and kinetics
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
0.24 mg/ml for soluble starch, variant enzyme M77
-
additional information
additional information
-
0.34 mg/ml for soluble starch, wild-type enzyme
-
additional information
additional information
-
0.63 mg/ml for soluble starch, variant enzyme 21B
-
additional information
additional information
-
0.8 mg/ml for soluble starch, variant enzyme M111
-
additional information
additional information
-
Km for potato starch in the hydrolysis reaction is between 0.02 and 0.05% starch (w/v), AmyD
-
additional information
additional information
-
KM for soluble starch is 1.1 mg/ml, KM-value for potato starch or ice starch is 0.9 mg/ml
-
additional information
additional information
-
KM for soluble starch is constant at pH 5.0-7.0 and increases greatly with decreasing pH from 5.0 to 2.8 and slightly with increasing pH from 7.5 to 9.2, alpha-amylase PA
-
additional information
additional information
-
Km for soluble starch: 0.43 mg/ml
-
additional information
additional information
-
KM for starch is 2.6 mg/ml
-
additional information
additional information
-
Km value for starch is 1.6 mg/ml
-
additional information
additional information
Km values: about 0.5 mg/ml for soluble starch and 4.45 mg/ml for glycogen at pH 9.5 and 50°C
-
additional information
additional information
-
Km values: about 0.5 mg/ml for soluble starch and 4.45 mg/ml for glycogen at pH 9.5 and 50°C
-
additional information
additional information
-
KM-value for soluble starch is 0.72mg/ml
-
additional information
additional information
-
Km-value for soluble starch: 0.0074 mg/ml
-
additional information
additional information
-
KM-value for starch is 0.97 mg/ml
-
additional information
additional information
-
Km-value: 5.2 mg/ml for soluble starch, 14.46 mg/ml for beta-cyclodextrin, 9.18 mg/ml for gamma-cyclodextrin
-
additional information
additional information
KM-values for amylose: 0.363 mg/ml for mutant enzyme Y380A, 0.351 mg/ml for mutant enzyme Y380M, 0.391 mg/ml for mutant enzyme Y380F, 0.203 mg/ml for mutant enzyme S378P, 0.208 mg/ml for mutant enzyme S378T, 0.19 mg/ml for alpha-amylase 1
-
additional information
additional information
-
KM-values for amylose: 0.363 mg/ml for mutant enzyme Y380A, 0.351 mg/ml for mutant enzyme Y380M, 0.391 mg/ml for mutant enzyme Y380F, 0.203 mg/ml for mutant enzyme S378P, 0.208 mg/ml for mutant enzyme S378T, 0.19 mg/ml for alpha-amylase 1
-
additional information
additional information
reaction products determined by HPLC, kinetic properties of native and purified protein shown
-
additional information
additional information
-
kinetics with different substrates, overview
-
additional information
additional information
kinetics with different substrates, overview
-
additional information
additional information
-
apparent Km is 36 mg/ml using cassava starch as substrate
-
additional information
additional information
Km is 11.0 mg/ml, using soluble potato starch as substrate, at pH 7.0 and 30°C
-
additional information
additional information
-
the Km value for starch is 3 mg/ml at 65°C using potato starch (1% (w/v)) as a substrate in 20 mM Tris-HCl, pH 7.4
-
additional information
additional information
-
the KM values of native and non-glycosylated alpha-amylases are 0.052 and 0.098 mg/ml
-
additional information
additional information
-
activation thermodynamics for kinetic stability of native and modified enzymes, overview
-
additional information
additional information
-
kinetics of recombinant mutant enzymes, overiew
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
apparent Km and Vmax values for the hydrolysis of soluble starch are 4 mg/ml and 1111 units/mg for the wild-type enzyme, and 2 mg/ml and 844.5 units/mg for the mutant enzyme, respectively
-
additional information
additional information
classical Michaelis-Menten kinetics, Km for soluble potato starch is 1.22 mg/ml
-
additional information
additional information
-
classical Michaelis-Menten kinetics, Km for soluble potato starch is 1.22 mg/ml
-
additional information
additional information
-
Km and Vmax values of A4 are 4 mg starch/ml and 0.00074 mmol reducing sugar, respectively
-
additional information
additional information
Km for raw starch is 0.79 mg/ml
-
additional information
additional information
-
Km for raw starch is 0.79 mg/ml
-
additional information
additional information
Km for starch is 2.0 mg/ml and for amylpectin 1.1 mg/ml for isozyme HaAmy2
-
additional information
additional information
Km for starch is 2.0 mg/ml and for amylpectin 1.1 mg/ml for isozyme HaAmy2
-
additional information
additional information
-
Km for starch is 2.0 mg/ml and for amylpectin 1.1 mg/ml for isozyme HaAmy2
-
additional information
additional information
Km for starch is 9.2 mg/ml and for amylpectin 1.3 mg/ml for isozyme HaAmy1
-
additional information
additional information
Km for starch is 9.2 mg/ml and for amylpectin 1.3 mg/ml for isozyme HaAmy1
-
additional information
additional information
-
Km for starch is 9.2 mg/ml and for amylpectin 1.3 mg/ml for isozyme HaAmy1
-
additional information
additional information
-
Km is 0.5 mg/ml and Vmax is 3.571 mmol/ml/mg
-
additional information
additional information
-
Km is 1.7 mg/ml and Vmax is 0.5 mg/ml/min
-
additional information
additional information
-
Km is 1.73 mg/ml and Vmax is 1.24 mg/ml/min
-
additional information
additional information
-
Km is 11.71 mg/ml and Vmax is 0.14 mg/ml/min
-
additional information
additional information
Wangia sp. C52
-
Km is 2.08 mg/ml and Vmax is 1.26 mg/ml/min
-
additional information
additional information
-
Km is 2.71 mg/ml, pH 7.0, 50°C, kinetics and thermodynamics, overview
-
additional information
additional information
-
Km is 4.79 mg/ml and Vmax is 0.322 mM/min
-
additional information
additional information
-
Km is 5.8 mg/ml and Vmax is 0.25 mg/ml/min
-
additional information
additional information
-
Km of BH072 alpha-amylase is 4.27 mg/ml
-
additional information
additional information
Km of soluble starch hydrolysis is 2.29 mg/ml, thermodynamics, overview
-
additional information
additional information
Lineweaver-Burk kinetics, Km for raw starch from jackfruit is 5.56 mg/ml
-
additional information
additional information
-
Lineweaver-Burk kinetics, Km for raw starch from jackfruit is 5.56 mg/ml
-
additional information
additional information
-
Lineweaver-Burk plot, kinetics and thermodynamics for recombinant chimeric acidic alpha-amylase Ba-Gt-amy, detailed overview. Adsorption kinetics of mutant Ba-Gt-amy and wild-type Ba?amy to 1% raw corn starch. Km and Vmax values of mutant Ba-Gt-amy for soluble starch are 0.8 mg/ml and 10.746 mmol*mg/min, whereas those for wild-type Ba-amy are 1.66 mg/ml and 0.0526 mmol*mg/min, respectively
-
additional information
additional information
Lineweaver-Burk plot, kinetics and thermodynamics for recombinant chimeric acidic alpha-amylase Ba-Gt-amy, detailed overview. Adsorption kinetics of mutant Ba-Gt-amy to 1% raw corn starch. Km and Vmax values of mutant Ba-Gt-amy for soluble starch are 0.8 mg/ml and 10.746 mmol * mg/min
-
additional information
additional information
-
Lineweaver-Burk plot, kinetics and thermodynamics for recombinant chimeric acidic alpha-amylase Ba-Gt-amy, detailed overview. Adsorption kinetics of mutant Ba-Gt-amy to 1% raw corn starch. Km and Vmax values of mutant Ba-Gt-amy for soluble starch are 0.8 mg/ml and 10.746 mmol * mg/min
-
additional information
additional information
-
Lineweaver-Burk plot, Michaelis-Menten kinetics
-
additional information
additional information
Lineweaver-Burke double reciprocal plot
-
additional information
additional information
Michaelis-Menten kinetic analysis, Km values for amylose and amylopectin of the recombinant His6-tagged enzyme are 9.2 mg/ml and 3.8 mg/ml, respectively, pH 5.0, 20°C
-
additional information
additional information
Michaelis-Menten kinetics, Km and Vmax of AmyD-1 in 2.0 M NaCl are 2.8 mg/ml and 21.8 mg*ml/ml, respectively, at 20°C and pH 6.0
-
additional information
additional information
-
Michaelis-Menten kinetics, Km and Vmax of AmyD-1 in 2.0 M NaCl are 2.8 mg/ml and 21.8 mg*ml/ml, respectively, at 20°C and pH 6.0
-
additional information
additional information
-
Michaelis-Menten kinetics, Km is 5.45 mg/ml and Vmax is 24.15 mg/ml/min
-
additional information
additional information
-
Michaelis-Menten kinetics, the purified alpha-amylase reveals Km and Vmax values of 0.5% and 1000 U/mg protein for soluble starch
-
additional information
additional information
thermodynamic and kinetic analysis, overview
-
additional information
additional information
-
Vmax value of purified native enzyme is 0.836 mg/ml
-
additional information
additional information
with substrate potato starch the enzyme shows a Km of 6.94 mg/ml and Vmax of 0.27 mg/ml * min
-
additional information
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
0.0001 mg/ml, intestine alpha-amylase
additional information
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
0.0003 mg/ml, muscle alpha-amylase
additional information
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
0.22 mg/ml, 37°C, pH 5.3
additional information
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
0.37 mg/ml, 37°C, pH 5.3
additional information
potato starch
-
free enzyme, Km: 0.4 mg/ml, Vmax: 25 mg starch degraded/ml/min/mg protein, immobilized enzyme, first use, Km: 0.98 mg/ml, Vmax: 23.3 mg starch degraded/ml/min/mg protein, first reuse, Km: 1.75 mg/ml, Vmax: 10.4 mg starch degraded/ml/min/mg protein. The higher Km value and the lower affinity for the substrate caused by diffiusional limitations and steric effects leading to a decrease in the accessibility of substrate to the enzyme active site
-
additional information
pullulan
-
Km-value: 15.4 mg/ml, 45°C, pH 5.0
additional information
pullulan
Km-value: 15.4 mg/ml, 45°C, pH 5.0
additional information
rabbit glycogen
-
0.00054 mg/ml, muscle alpha-amylase
-
additional information
rabbit glycogen
-
0.0015 mg/ml, intestine alpha-amylase
-
additional information
soluble starch
-
3.0 mg/ml, 63°C, pH 5.0
-
additional information
soluble starch
-
Km: 1.66 mg/ml, Vmax: 0.0001 mmol/min/ml
-
additional information
soluble starch
-
Km: 45 mg/ml, Vmax 9 mg/ml/min
-
additional information
soluble starch
-
Km: 3.8 mg/ml, pH 8.5, 70°C
-
additional information
soluble starch
-
apparent Km value of 7.1 mg/ml, pH 6, 35°C
-
additional information
starch
-
0.0005 mg/ml, intestine alpha-amylase
additional information
starch
-
0.003 mg/ml, muscle alpha-amylase
additional information
starch
-
0.056 mg/ml, 50°C, pH 5.5
additional information
starch
-
0.5 mg/ml, 50°C, pH 5.0
additional information
starch
-
0.53%, ragi starch, 45°C, pH 5.0
additional information
starch
-
0.59%, ragi starch, 45°C, pH 5.0
additional information
starch
-
1.1%, ragi starch, 45°C, pH 5.0
additional information
starch
-
1.28 mg/ml, 30°C, pH 6.0
additional information
starch
-
2.9 mg/ml
additional information
starch
-
3.44 mg/ml, 55°C
additional information
starch
0.60 mg/ml, double mutant, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
-
0.60 mg/ml, double mutant, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
0.61 mg/ml, mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.61 mg/ml, mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
0.64 mg/ml, mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.64 mg/ml, mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
0.86 mg/ml, wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.86 mg/ml, wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
starch
soluble starch: Km 4.57 mg/ml
additional information
starch
-
the KM-value for soluble starch (pH 8.5, 70°C) is 3.8 mg/ml
additional information
starch
KM value is 1.31 g/l at 5°C, 1.36 g/l at 25°C, and 1.42 g/l at 35°C respectively, and pH 9.0
additional information
starch
Km value is 1.79 ml/ml at 5°C, pH 8.3 and ,328 mg/ml at 15°C, pH 8.3
additional information
starch
KM value is 3 g/l at 5°C, 3.3g/l at 25°C, and 4.4 g/l at 35°C respectively, and pH 9.0
additional information
starch
-
Km-value: 16.0 mg/ml, 45°C, pH 5.0
additional information
starch
Km-value: 16.0 mg/ml, 45°C, pH 5.0
additional information
starch
-
Km-value: 2.9 mg/ml, pH 7.0, 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
132
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.8, 30°C, recombinant AMY1-SBD fusion enzyme
2.98
2-chloro-4-nitrophenyl alpha-D-maltotrioside
pH 7.0, 30°C
1.9 - 15.8
2-chloro-4-nitrophenyl alpha-maltotrioside
3 - 35
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
10 - 203
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
7.86 - 266
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
141 - 697
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
34
4-nitrophenyl alpha-D-maltohexaoside
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
0.0494 - 0.0497
4-nitrophenyl-alpha-D-maltoside
228
acarbose
-
pH 4.5, 90°C, recombinant enzyme
0.399 - 241
alpha-cyclodextrin
443
alpha-maltosyl fluoride
-
30°C, pH 7.0
283 - 285
alpha-maltotriosyl fluoride
29.4 - 485
beta-cyclodextrin
1940
Dextrin
at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2
64.6 - 186
gamma-cyclodextrin
150
maltosyl fluoride
pH 7.0, 30°C
750
oyster glycogen
at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2
-
8.5 - 175
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
1920
rabbit glycogen
at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2
-
5.9 - 3420
soluble potato starch
-
0.02 - 1055
soluble starch
-
additional information
maltotetraose
1.9
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM Br-
2
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.2 mM ClO3-
2.1
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM I-
2.2
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.1 mM NO3-
2.4
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 0.01 mM Cl-
3.5
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM NO2-
4.4
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM N3-
15.8
2-chloro-4-nitrophenyl alpha-maltotrioside
in presence of 1 mM N3-
3 - 6
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
wild-type enzyme, pH 5.5, 30°C, kcat/Km: 48 1/s/mg/ml
10
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y105A mutant, kcat below 10 1/s, pH 5.5, 30°C
10
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y105A/Y380A mutant, kcat below 10 1/s, pH 5.5, 30°C
10
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y105A/Y380M mutant, kcat below 10 1/s, pH 5.5, 30°C
19
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y380A mutant, pH 5.5, 30°C, kcat/Km: 28 1/s/mg/ml
21
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
H395A mutant, pH 5.5, 30°C, kcat/Km: 23 1/s/mg/ml
34
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y380M mutant, pH 5.5, 30°C, kcat/Km: 39 1/s/mg/ml
35
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Y380A/H395A mutant, pH 5.5, 30°C, kcat/Km: 25 1/s/mg/ml
10
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
below, pH 5.5, 37°C, mutant Y105A
19
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380A
24
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105A/T212W
31
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105A/T212Y
34
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380M
40.4
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
-
malt enzyme
48
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme S378T
52
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
alpha-amylase 1
56
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme Y380F
59
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
mutant enzyme S378P
61
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212W
63.1
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
-
recombinant enzyme
119
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, wild-type enzyme
127
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212Y
132
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105W
140
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant T212P
203
2-chloro-4-nitrophenyl beta-D-maltoheptaoside
pH 5.5, 37°C, mutant Y105F
7.86
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 25°C, pH 6.0
8.14
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 710000 1/s/M, 25°C, pH 6.0
8.32
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 740000 1/s/M, 25°C, pH 6.0
8.73
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 770000 1/s/M, 25°C, pH 6.0
34
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 140000 1/s/M, 37°C, pH 4.5
120
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
-
37°C, pH 6.0
175
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 880000 1/s/M, 37°C, pH 6.5
175
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 870000 1/s/M, 37°C, pH 5.5
186
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 920000 1/s/M, 37°C, pH 6.5
187
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1230000 1/s/M, 37°C, pH 5.5
201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1070000 1/s/M, 37°C, pH 5.5
205
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 1420000 1/s/M, 37°C, pH 6.5
209
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1100000 1/s/M, 37°C, pH 6.5
219
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1210000 1/s/M, 37°C, pH 4.5
233
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 37°C, pH 5.5
234
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1350000 1/s/M, 37°C, pH 4.5
266
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1910000 1/s/M, 37°C, pH 4.5
141
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
153
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
291
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
291
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
364
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
392
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
15°C, pH 7.2
675
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
697
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
0.0494
4-nitrophenyl-alpha-D-maltoside
-
isozyme PPA-I, at pH 6.9 and 30°C
0.0497
4-nitrophenyl-alpha-D-maltoside
-
isozyme PPA-II, at pH 6.9 and 30°C
0.399
alpha-cyclodextrin
-
pH 5.6, 40°C
10.7
alpha-cyclodextrin
-
calculated as low molecular weight products
241
alpha-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
283
alpha-maltotriosyl fluoride
-
30°C, pH 7.0
285
alpha-maltotriosyl fluoride
pH 7.0, 30°C
0.042
amylopectin
5°C, pH 8.3
0.13
amylopectin
isozyme HaAmy2, pH 7.0, 37°C
0.15
amylopectin
15°C, pH 8.3
0.29
amylopectin
isozyme HaAmy1, pH 7.0, 37°C
1.1
amylopectin
pH 5.0, 37°C, recombinant enzyme
1.4
amylopectin
pH 5.0, 37°C, recombinant enzyme
3.4
amylopectin
recombinant His6-tagged enzyme, pH 5.0, 20°C
137
amylopectin
45°C, pH 5.0
137
amylopectin
recombinant His-tagged enzyme, pH 5.0, 45°C
171
amylopectin
-
calculated as low molecular weight products
2274.8
amylopectin
-
pH 7.0, 50°C
4180
amylopectin
pH 6.5, 90°C
9.21
amylose
pH 6.5, 40°C, recombinant enzyme
55.5
amylose
-
37°C, pH 5.3
56
amylose
Y105A/Y380M mutant, pH 5.5, 30°C, kcat/Km: 56 1/s/mg/ml, kcat/Km decreases 10-25fold for all Y105 mutants
61
amylose
Y105A/Y380A mutant, pH 5.5, 30°C, kcat/Km: 51 1/s/mg/ml, kcat/Km decreases 10-25fold for all Y105 mutants
71.8
amylose
-
37°C, pH 5.3
75
amylose
H395A mutant, pH 5.5, 30°C, kcat/Km: 394 1/s/mg/ml
95
amylose
Y380A mutant, pH 5.5, 30°C, kcat/Km: 264 1/s/mg/ml
116.1
amylose
recombinant His6-tagged enzyme, pH 5.0, 20°C
144
amylose
-
DP 17, malt enzyme, calculated as low molecular weight products
149
amylose
Y380M mutant, pH 5.5, 30°C, kcat/Km: 425 1/s/mg/ml
163
amylose
Y380A/H395A mutant, pH 5.5, 30°C, kcat/Km: 543 1/s/mg/ml
169
amylose
wild-type enzyme, pH 5.5, 30°C, kcat/Km: 1300 1/s/mg/ml
178
amylose
Y105A mutant, pH 5.5, 30°C, kcat/Km: 132 1/s/mg/ml, kcat/Km decreases 10-25fold for all Y105 mutants
185
amylose
-
DP 17, recombinant enzyme, calculated as low molecular weight products
202
amylose
-
30°C, pH 5.5
206
amylose
-
30°C, pH 5.5
230
amylose
-
short chain amylose, calculated as low molecular weight products
1014
amylose
45°C, pH 5.0
1014
amylose
recombinant His-tagged enzyme, pH 5.0, 45°C
2280
amylose
pH 6.5, 90°C
78
amylose DP17
pH 5.5, 37°C, mutant Y105A/T212Y
-
105
amylose DP17
pH 5.5, 37°C, mutant Y105A/T212W
-
127
amylose DP17
pH 5.5, 37°C, mutant T212Y
-
146
amylose DP17
below, pH 5.5, 37°C, mutant Y105A
-
154
amylose DP17
pH 5.5, 37°C, mutant T212W
-
158
amylose DP17
pH 5.5, 37°C, mutant Y105F
-
165
amylose DP17
pH 5.5, 37°C, wild-type enzyme
-
200
amylose DP17
pH 5.5, 37°C, mutant Y105W
-
225
amylose DP17
-
pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme
-
264
amylose DP17
pH 5.5, 37°C, mutant T212P
-
95
amylose DP440
mutant enzyme Y380A
-
144
amylose DP440
mutant enzyme S378T
-
149
amylose DP440
mutant enzyme Y380M
-
162
amylose DP440
mutant enzyme Y380F
-
163
amylose DP440
mutant enzyme S378P
-
185
amylose DP440
alpha-amylase 1
-
209
amylose DP440
-
pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme
-
29.4
beta-cyclodextrin
-
calculated as low molecular weight products
31.1
beta-cyclodextrin
-
pH 5.6, 40°C
196
beta-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
283.3
beta-cyclodextrin
-
-
485
beta-cyclodextrin
-
-
64.6
gamma-cyclodextrin
-
pH 5.6, 40°C
173
gamma-cyclodextrin
-
pH 4.5, 90°C, recombinant enzyme
186
gamma-cyclodextrin
-
calculated as low molecular weight products
130
glycogen
-
from rat liver, calculated as low molecular weight products
166
glycogen
-
from oyster, calculated as low molecular weight products
2300
glycogen
pH 6.5, 90°C
125
maltodextrin
-
30°C, pH 5.5
129
maltodextrin
-
30°C, pH 5.5
2
maltoheptaose
-
30°C, pH 5.5
5.6
maltoheptaose
-
30°C, pH 5.5
25
maltoheptaose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
573.8
maltoheptaose
pH 6.5, 40°C, recombinant enzyme
44.2
maltohexaose
-
pH 5.6, 40°C
37.2
maltopentaose
-
pH 5.6, 40°C
283
maltopentaose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
567.01
maltopentaose
pH 6.5, 40°C, recombinant enzyme
0.0258
maltose
-
pH 5.6, 40°C
428.98
maltose
pH 6.5, 40°C, recombinant enzyme
5.87
maltotetraose
-
pH 5.6, 40°C
117 - 144
maltotetraose
-
value depends on assay method
0.24
maltotriose
-
pH 5.6, 40°C
268
maltotriose
-
pH 4.5, 90°C, recombinant enzyme
538.95
maltotriose
pH 6.5, 40°C, recombinant enzyme
809
maltotriose
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
8.5
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 8.0, F256W mutant
62.4
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 5.3
85.3
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 5.3
175
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
37°C, pH 8.0, wild-type
0.085
pullulan
-
pH 5.6, 40°C
4.8
pullulan
-
mutant Y374A
140
pullulan
-
wild-type enzyme
297
pullulan
45°C, pH 5.0
297
pullulan
recombinant His-tagged enzyme, pH 5.0, 45°C
40000
raw starch
pH 4.0, 60°C, recombinant chimeric acidic alpha-amylase Ba-Gt-amy
-
40000
raw starch
-
pH 4.0, 60°C, recombinant chimeric acidic alpha-amylase Ba-Gt-amy
-
5.9
soluble potato starch
pH 8.0, 80°C
-
3420
soluble potato starch
at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2
-
0.02
soluble starch
in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
-
0.025
soluble starch
-
-
-
0.72
soluble starch
pH 6.5, 40°C, recombinant enzyme
-
98.3
soluble starch
-
-
-
139.1
soluble starch
-
mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C
-
141.3
soluble starch
-
mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C
-
147.5
soluble starch
-
mutant BACDELTANC/M231L, pH 8.0, 60°C
-
156.8
soluble starch
-
mutant BACDELTANC/DELTARS, pH 8.0, 60°C
-
168.5
soluble starch
-
mutant BACDELTANC, pH 8.0, 60°C
-
561.7
soluble starch
-
-
-
933.5
soluble starch
recombinant enzyme, 20°C, pH 6.0
-
1055
soluble starch
recombinant His-tagged enzyme, pH 5.0, 45°C
-
0.017
starch
pH 7.2, 42°C
0.022
starch
presence of 0.4 mM neohesperidin dihydrochalcone, pH 7.2, 42°C
0.035
starch
presence of 2.4 mM neohesperidin dihydrochalcone, pH 7.2, 42°C
0.04
starch
presence of 4.8 mM neohesperidin dihydrochalcone, pH 7.2, 42°C
0.156
starch
15°C, pH 8.3
0.19
starch
isozyme HaAmy2, pH 7.0, 37°C
0.67
starch
isozyme HaAmy1, pH 7.0, 37°C
0.92
starch
pH 5.0, 37°C, recombinant enzyme
1.13
starch
pH 5.0, 37°C, recombinant enzyme
9.4
starch
-
mutant Y374A
9.8
starch
mutant enzyme A53S, in the presence of 5 mM Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
19.9
starch
wild type enzyme, in the presence of 5 mM Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
20.7
starch
mutant enzyme H58I, in the presence of 5 mM Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
22.4
starch
mutant enzyme A53S, in the absence of Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
25.7
starch
wild type enzyme, in the absence of Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
27.4
starch
mutant enzyme H58I, in the absence of Ca2+, in 20 mM Tris-HCl buffer (pH 7.2), at 30°C
67
starch
-
pH 4.5, 90°C, recombinant enzyme
91.4
starch
-
pH 5.6, 40°C
120
starch
-
wild-type enzyme
179
starch
pH not specified in the publication, 5°C
206
starch
-
soluble starch of Zulkowsky type, calculated as low molecular weight products
237
starch
-
soluble starch from Merck, calculated as low molecular weight products
280
starch
pH not specified in the publication, 20°C
518
starch
pH not specified in the publication, 37°C
1449.43
starch
-
pH and temperature not specified in the publication
1457
starch
pH not specified in the publication, 55°C
3000
starch
-
calculated as low molecular weight products
3021.2
starch
-
pH 7.0, 50°C
additional information
maltotetraose
-
pH 5.6, 40°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
additional information
additional information
-
503 per s for soluble starch, variant enzyme M77
-
additional information
additional information
-
586 per s for soluble starch, wild-type enzyme
-
additional information
additional information
-
656 per s for soluble starch, variant enzyme M111
-
additional information
additional information
-
722 per s for soluble starch, variant enzyme 21B
-
additional information
starch
double mutant, L134R/S320A, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
-
double mutant, L134R/S320A, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
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0.000575
crude extract, at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2, using 4-nitrophenyl maltoheptaoside as substrate
0.0063
using amylopectin as substrate, in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
0.0109
using amylose as substrate, in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
0.0145
-
crude extract, at 80°C
0.0188
using soluble starch as substrate, in 50 mM sodium phosphate buffer (pH 6.5) at 75°C
0.1
0.1% starch as substrate
0.54
after 939fold purification, at 30°C in 10 mM MOPS buffer (pH 7.0) with 5 mM CaCl2, using 4-nitrophenyl maltoheptaoside as substrate
0.94
-
muscle alpha-amylase
0.956
-
crude extract, at 40°C
1.2
-
after 82fold purification, at 80°C
10000
-
purified enzyme, pH and temperature not specified in the publication
1022.36
purified native mutant enzyme, pH 5.0, 4°C
1026.7
-
pH 6.5, 60°C, substrate gamma-cyclodextrin
104.9
-
glycosylated alpha-amylase
11.2
-
enzyme immobilized on polyacrylamide
110.94
P04745
commercial enzyme preparation, solution, pH 6.9, 37°C
1145.4
-
pH 6.5, 60°C, substrate amylopectin
12
-
crude extract, at 42°C
120
-
pullulan hydrolyzing activity
121.3
-
substrate: amylopectin, pH 7.0, 50°C
122.04
purified recombinant enzyme, pH 6.5, 40°C, substrate amylose
1275
purified native extracellular enzyme, substrate soluble starch, pH 8.0, 80°C
13.3
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate potato starch
13.6
-
after 13.6fold purification, at 65°C
130
Halalkalibacterium halodurans
-
alpha-amylase I
1314.5
-
pH 6.5, 60°C, substrate potato starch
1343
purified recombinant enzyme, pH 5.0, 60°C
135
-
purified enzyme, pH and temperature not specified in the publication
14.6
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate pea starch
141.5
purified enzyme with 5 mM Ca2+, pH 8.0, 20°C
142.2
-
purified recombinant mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C
1421
-
purified enzyme, substrate soluble starch
145.4
-
purified recombinant mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C
146
Wangia sp. C52
-
purified enzyme, pH and temperature not specified in the publication
148.6
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate raw rice starch
158.9
-
purified recombinant mutant BACDELTANC/DELTARS, pH 8.0, 60°C
16.4
purified recombinant His-tagged enzyme, pH 6.0, 20°C, substrate soluble starch
1633
-
purified enzyme, pH and temperature not specified in the publication
1641
-
purified enzyme, pH and temperature not specified in the publication
175.8
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate maize starch
176.4
-
purified recombinant enzyme, substrate beta-cyclodextrin
179.6
-
purified recombinant mutant BACDELTANC/M231L, pH 8.0, 60°C
18
Halalkalibacterium halodurans
-
alpha-amylase II
18.5
-
purified isozyme BAA
1900
-
recombinant Amy1, hydrolysis of soluble starch at 37°C and pH 6.0
193.3
-
purified recombinant mutant BACDELTANC, pH 8.0, 60°C
200.76
-
purified native enzyme, pH 8.0, 55°C, substrate soluble starch
2162.42
-
purified native enzyme, pH 7.0, 60°C
229
-
non-glycosylated alpha-amylase
2339
-
pH 6.5, 60°C, substrate rice starch
2416.6
-
pH 6.5, 60°C, substrate wheat starch
246.5
-
after 131.52fold purification
25.6
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate potato starch
254
purified recombinant His-tagged enzyme, pH 5.0, 45°C, substrate soluble starch
2551
-
purified native enzyme, soluble starch, pH 4.5, 35°C
26493
-
purified native enzyme, pH 6.0, 80°C, substrate soluble starch
267
-
after 23fold purification, at 42°C
27.96
purified recombinant enzyme, pH 7.0, 25°C, substrate soluble starch
270.59
-
immobilized enzyme, pH 6.0, 55°C
27065
-
the purified enzyme, one unit of amylase activity is defined as the amount of enzyme that released 1 micromol of maltose per minute per ml under the assay conditions, pH 7.0, 60°C
2709.1
-
pH 6.5, 60°C, substrate corn starch
2814.3
-
pH 6.5, 60°C, substrate soluble starch
2868.6
-
pH 6.5, 60°C, substrate sweet potato starch
29.4
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate mung bean starch
2902.26
-
purified enzyme, pH 5.0, 100°C, substrate starch
3.1
-
enzyme immobilized on aminoalkylsilane-alumina
3101.9
-
pH 6.5, 60°C, substrate amylose
33.2
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate wheat starch
36.7
purified enzyme without Ca2+, pH 8.0, 20°C
384
purified recombinant His-tagged enzyme, pH 5.0, 45°C, substrate amylose
384.6
-
purified enzyme, pH 5.5, temperature not specified in the publication
39.6
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate maize starch
4.16
-
purified recombinant enzyme, pH 5.5, 60°C
402.02
-
partially purified enzyme, pH 6.0, 55°C
4076
-
hydrolysis of starch
42
-
purified enzyme form I
4215.91
-
purified enzyme, pH 7.0, 50°C
44
-
purified enzyme, pH and temperature not specified in the publication
4410
-
purified enzyme from honey
46.1
purified recombinant His-tagged enzyme, pH 5.0, 45°C, substrate amylopectin
48.1
purified native enzyme, pH 7.0, 50°C
5.1
-
enzyme immobilized on DEAE-cellulose
5.33
-
pH 7.0, temperature not specified in the publication
513.4
-
pH 6.5, 60°C, substrate pullulan
55.77
P04745
commercial enzyme preparation, solution, pH 6.9, 37°C, in presence of 4 mg/ml Sorghum procyanidin tetramer
59
-
crude extract, at 65°C
595.5
purified native wild-type enzyme, pH 5.0, 20°C
60
purified recombinant enzyme, pH 3.0, 25°C, substrate soluble starch
61.65
purified recombinant enzyme, pH 7.0, 60°C
627.5
-
purified enzyme, pH 5.5, 50°C
7.4
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate wheat starch
7.7
-
intestine alpha-amylase
7.986
-
after 8.4fold purification, at 40°C
700
purified native mutant enzyme, pH 5.0, 20°C
72
-
purified to near homogeneity, pH 5.0, 50°C
79.8
purified enzyme, pH 8.5, 55°C
8
-
purified enzyme form II
8.3
-
enzyme immobilized on chitin
8.9
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate pea starch
804.88
purified native wild-type enzyme, pH 8.0, 20°C
8600
-
purified recombinant mutant enzyme Gs4j-amyA, pH 5.5, 60°C
9.7
purified recombinant His6-tagged enzyme, pH 5.0, 20°C
98.4
-
purified alpha-amylase I
980
-
substrate: starch, pH 7.0, 50°C
1190
-
enzyme from shoots
1190
-
enzyme from cotyledons
17.9
-
-
17.9
purified recombinant His-tagged wild-type enzyme AmyP, pH 7.5, 40°C, substrate mung bean starch
1755
-
purified enzyme, pH and temperature not specified in the publication
1755
purified enzyme, pH and temperature not specified in the publication
327
-
purified enzyme
327
-
purified enzyme, pH 6.5, 60°C
426.7
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C
426.7
purified recombinant His-tagged chimeric mutant enzyme AmyP-Cr, pH 7.5, 40°C, substrate raw rice starch
487.5
-
pH 8.5, 70°C
487.5
-
pH 8.5, 70°C, reducing sugar produced
5.6
-
-
5.6
-
substrate starch, pH 5.5, 60°C
648.2
-
purified enzyme
648.2
-
after 15.3fold purification
72.5
45°C, pH 5.0
72.5
purified recombinant His-tagged enzyme, pH 5.0, 45°C, substrate pullulan
additional information
-
purified isozyme AoA1 and isozyme AoA2
additional information
-
highest production activity of 1874.8 U/ml obtained at 24 h of incubation
additional information
-
-
additional information
alpha-amylase activity of crude enzyme is 2.87 U/ml after 5 days of incubation in medium containing raw sago starch
additional information
-
enzyme activity in cultures grown on wheat bran with coconut oil cake
additional information
-
enzyme activity in solid fermentation cultures grown on spent-brewing grains
additional information
-
activities with soluble starch of wild-type native enzyme, and recombinant wild-type enzyme from different expressing Escherichia coli strains, overview
additional information
-
adsorption to and hydrolysis of raw starch from corn and potato, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
adsorption to and hydrolysis of raw starch from corn and potato, overview
additional information
amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml
additional information
-
amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml
additional information
-
-
additional information
-
-
additional information
-
4200 units/mg, one unit is defined as the amount of alpha-amylase that gives an increase of 0.001 in A620/ml for 15 min in a total volume of 5 ml
additional information
-
607 U/mg. One unit of alpha-amylase activity is defined as the amount of enzyme which causes 1% blue value reduction of 1% potato starch solution at 40°C for one minute
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
adsorption to and hydrolysis of raw starch from corn and potato, overview
additional information
kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method
additional information
the recombinant enzyme shows a specific activity of 21.3 units/mg in the extract supernatant and of 35.8 units/mg after 1.7fold purification, one unit is defined as the amount of enzyme required to liquefy 1 g soluble starch completely for 1 h at 60°C and pH 6.0
additional information
-
the recombinant enzyme shows a specific activity of 21.3 units/mg in the extract supernatant and of 35.8 units/mg after 1.7fold purification, one unit is defined as the amount of enzyme required to liquefy 1 g soluble starch completely for 1 h at 60°C and pH 6.0
additional information
-
-
additional information
-
assay method: measurement of the iodine-starch-complex
additional information
-
-
additional information
-
-
additional information
-
18.7 U/mg, purified Amy II
additional information
-
6.05 U/mg, purifed Amy II
additional information
-
-
additional information
-
-
additional information
-
-
additional information
decreased from 1000 to 845 U/mg for AmyUS100DELTAIG to the mutant M197A, assay at 80°C and pH 5.6
additional information
-
decreased from 1000 to 845 U/mg for AmyUS100DELTAIG to the mutant M197A, assay at 80°C and pH 5.6
additional information
-
450 U/mg. One saccharogenic alpha-amylase unit is defined as the amount of enzyme required for the liberation of 0.001 mM of reducing sugars as maltose per milliliter per minute
additional information
-
28 U/ml, pH 8.0, 100°C
additional information
-
0.07 mg of starch/min*mg
additional information
one enzyme unit is defined as the amount of enzyme that hydrolyses 1 mg of starch in 1 min
additional information
-
one enzyme unit is defined as the amount of enzyme that hydrolyses 1 mg of starch in 1 min
additional information
-
assay
additional information
-
assay: UV-method with maltotetraose
additional information
-
assay: UV-method with maltoheptaose
additional information
-
colorimetric method
additional information
-
assay method: measurement of the iodine-starch-complex
additional information
-
assay method: measurement of the iodine-starch-complex
additional information
-
measurement of alpha-amylase activity in serum and urine by determination of the products maltose and glucose
additional information
-
determination with coloured insoluble substrates
additional information
-
determination of isoenzymes by measurment of the iodine-starch-complex after electroporetic separation.
additional information
-
assay: measurement of reducing groups
additional information
-
assay method: measurement with coloured unsoluble substrates
additional information
-
F256W mutant, 900 units, 1 unit is definded as the amount of alpha-amylase able to decrease 1% of absorbance at 620 nm in 1 min
additional information
-
wild-type, 66400 units, 1 unit is definded as the amount of alpha-amylase able to decrease 1% of absorbance at 620 nm in 1 min
additional information
P04745
the specific activity of the mutant HSAmy-ar decreases by 87% (a 10fold reduction) compared to the wild-type HSAmy, indicating that the absence of saccharide-binding ability at the secondary binding sites in HSAmy-ar has resulted in a significant reduction in enzyme activity. The activity is also affected by about 2fold when the aromatic residue at position 203 is mutated. Among the single or douible mutants studied, W203A exhibit the least activity against starch hydrolsis. The mutation at position W284 do not alter the specific activity to any significant extent. Double mutations at the residues W316 and E388 also do not affect activity
additional information
-
the specific activity of the mutant HSAmy-ar decreases by 87% (a 10fold reduction) compared to the wild-type HSAmy, indicating that the absence of saccharide-binding ability at the secondary binding sites in HSAmy-ar has resulted in a significant reduction in enzyme activity. The activity is also affected by about 2fold when the aromatic residue at position 203 is mutated. Among the single or douible mutants studied, W203A exhibit the least activity against starch hydrolsis. The mutation at position W284 do not alter the specific activity to any significant extent. Double mutations at the residues W316 and E388 also do not affect activity
additional information
-
-
additional information
-
activity of recombinant AMY1-SBD fusion enzyme towards different starch substrates
additional information
-
AMY1 with various substrates: 25.74 U/mg with insoluble blue starch, 132.64 U/mg with corn starch, 189.31 U/mg with potato starch, 153.28 U/mg with soluble starch (Showa Chemical Co.), and 296.6 U/mg with soluble starch (Sigma-Aldrich). AMY2 with various substrates: 17.64 U/mg with insoluble blue starch, 131.71 U/mg with corn starch, 222.34 U/mg with potato starch, 272.68 U/mg with soluble starch (Showa Chemical Co.), and 210.24 U/mg with soluble starch (Sigma-Aldrich)
additional information
substrate insoluble Blue Starch, pH 6.8, 37°C, wild-type: 2800 U/mg, mutants Y105A/Y380A: 2300 U/ml, Y105A/Y380M: 1800 U/ml, H395A: 2300 U/ml, Y380A/H395A: 3200 U/ml, Y380A: 1400 U/ml, Y380M: 2000 U/ml, and Y105A: 4000 U/ml. Units defined as 1 Unit gives DELTA optical density at 620 nm: 1. Y105A/Y380A and Y105A/Y380M mutant lose 18-36% activity relative to wild-type. 29-50% decrease in acitivity of the single mutants Y380M and Y380A.
additional information
-
substrate insoluble Blue Starch, pH 6.8, 37°C, wild-type: 2800 U/mg, mutants Y105A/Y380A: 2300 U/ml, Y105A/Y380M: 1800 U/ml, H395A: 2300 U/ml, Y380A/H395A: 3200 U/ml, Y380A: 1400 U/ml, Y380M: 2000 U/ml, and Y105A: 4000 U/ml. Units defined as 1 Unit gives DELTA optical density at 620 nm: 1. Y105A/Y380A and Y105A/Y380M mutant lose 18-36% activity relative to wild-type. 29-50% decrease in acitivity of the single mutants Y380M and Y380A.
additional information
-
-
additional information
-
210 mg starch/min
additional information
-
-
additional information
-
-
additional information
one unit of enzyme activity is defined as the quantity of enzyme that causes a 0.01% reduction of absorbance at 690 nm of starch-iodine solution at 20°C in one min per ml
additional information
-
-
additional information
-
assay method: measurement of the iodine-starch-complex
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown
additional information
-
-
additional information
-
assay method: measurement of the iodine-starch-complex
additional information
-
842.9 units, one unit is defined as the amount of alpha-amylase necessary to hydrolyze 0.1 mg starch per min
additional information
-
values about 5.8 U/ml for different transformants
additional information
-
25000 U/mg, pH 7.0, 27°C
additional information
-
value is 0.48 U/g-wet-cell, strain NBRC1440SS
additional information
-
value is 0.93 U/g-wet-cell, strain MT8-1SS
additional information
-
value is 1.86 U/g-wet-cell, strain MN8140SS
additional information
-
microplate-reader based kinetic assay
additional information
-
-
additional information
-
-
additional information
-
8.3 U/mg purified enzyme, pH 5.0, 95°C
additional information
-
-
additional information
-
-
additional information
1000 U/mg for the wild-type enzyme and the mutants W177V, Y178V, and F179V
additional information
-
1000 U/mg for the wild-type enzyme and the mutants W177V, Y178V, and F179V
additional information
-
-
additional information
-
-
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?
-
x * 55000-65000, SDS-PAGE
?
-
x * 52000, SDS-PAGE
-
?
-
x * 66000, SDS-PAGE
-
?
x * 61160, calculated from sequence
?
-
x * 65000, about, SDS-PAGE
?
x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 80000, recombinant His6-tagged enzyme, SDS-PAGE, x * 79610, sequence calculation
?
-
x * 80000, recombinant His6-tagged enzyme, SDS-PAGE, x * 79610, sequence calculation
-
?
-
x * 53000, SDS-PAGE, intestine alpha-amylase
?
-
x * 74000, SDS-PAGE, isoenzyme alpha-I1
?
-
x * 83000, SDS-PAGE, isoenzyme alpha-I2
?
x * 54000, SDS-PAGE, x * 52500, sequence calculation, mature enzyme
?
-
x * 54000, SDS-PAGE, x * 52500, sequence calculation, mature enzyme
-
?
-
x * 48000, SDS-PAGE
-
?
-
x * 51300, SDS-PAGE
-
?
-
x * 58000, SDS-PAGE
-
?
-
x * 67500, SDS-PAGE
-
?
-
x * 55000, about, SDS-PAGE
?
x * 55000, about, SDS-PAGE
?
-
x * 28000, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 62650, SDS-PAGE
-
?
-
x * 55000, about, SDS-PAGE
-
?
-
x * 53000, extracellular enzyme, SDS-PAGE
?
-
x * 53000, recombinant enzyme, SDS-PAGE
?
-
x * 55391, extracellular enzyme, SDS-PAGE
?
-
x * 54000, SDS-PAGE, recombinant alpha-amylase
?
-
x * 55331, deduced from nucleotide sequence, native ABA
?
-
x * 57000, SDS-PAGE, native ABA
?
-
x * 74000, SDS-PAGE, recombinant ABA, due to glycosylation by Pichia pastoris
?
-
x * 51000, isozyme BAA, SDS-PAGE
?
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 94500, SDS-PAGE
-
?
-
x * 69200, SDS-PAGE
-
?
-
x * 53000, recombinant enzyme, SDS-PAGE
-
?
-
x * 53000, extracellular enzyme, SDS-PAGE
-
?
-
x * 55391, extracellular enzyme, SDS-PAGE
-
?
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE, recombinant alpha-amylase
-
?
-
x * 75000, about, SDS-PAGE
?
x * 50100, about, SDS-PAGE and sequence calculation
?
-
x * 55000, about, SDS-PAGE
?
x * 58000, about, SDS-PAGE
?
-
x * 68000, about, SDS-PAGE
?
x * 58000, about, SDS-PAGE
?
-
x * 64000, isozyme RBSA-1, SDS-PAGE, x * 47000, isozyme BSA-2, SDS-PAGE, x * 46000, isozyme RBLA, SDS-PAGE
?
-
x * 80000, about, SDS-PAGE
?
-
x * 43000, about, SDS-PAGE
?
-
x * 68000, SDS-PAGE
-
?
-
x * 80000, about, SDS-PAGE
-
?
-
x * 43000, about, SDS-PAGE
-
?
-
x * 80000, about, SDS-PAGE
-
?
-
x * 43000, about, SDS-PAGE
-
?
-
x * 42800, SDS-PAGE
-
?
-
x * 53000, SDS-PAGE
-
?
-
x * 53000, SDS-PAGE
-
?
-
x * 87000, SDS-PAGE in absence of 2-mercaptoethanol
?
-
x * 87000, SDS-PAGE in absence of SDS
?
Bacteria SS71
-
x * 87000, SDS-PAGE in absence of 2-mercaptoethanol
-
?
Bacteria SS71
-
x * 87000, SDS-PAGE in absence of SDS
-
?
x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 89000, SDS-PAGE
-
?
-
x * 66000, SDS-PAGE
-
?
x * 66000, about, recombinant His-tagged chimeric mutant enzyme AmyP-Cr, sequence calculation
?
-
x * 55000, about, SDS-PAGE
?
-
x * 50000, SDS-PAGE
-
?
-
x * 62000, recombinant His6-tagged mutant Gs4j-amyA N-terminally fused to OmpA signal peptide, SDS-PAGE, x * 58770, sequence calculation
?
x * 58000, recombinant wild-type enzyme, SDS-PAGE
?
-
x * 58000, SDS-PAGE
-
?
x * 54000, SDS-PAGE, as fusion protein 965000 Da, combined with the maltose binding protein with 42500 Da
?
x * 72026, calculated from sequence
?
x * 83000, C-terminally 6*His-tagged recombinant enzyme
?
-
x * 55000, non-glycosylated alpha-amylase
?
-
x * 56091, deduced from nucloeotide sequence
?
-
x * 56095, mass spectrometry
?
-
x * 62000, glycosylated alpha-amylase
?
-
x * 62000, glycosylated HSA, SDS-PAGE, x * 56000, deglycosylated HSA, SDS-PAGE
?
-
x * 68900, recombinant AMY1-SBD fusion enzyme, amino acid sequence calculation, x * 75000, recombinant glycosylated AMY1-SBD fusion enzyme, SDS-PAGE
?
-
x * 45000, AMY1 or AMY2, SDS-PAGE
?
-
x * 51750, calculated from sequence
?
-
x * 51750, calculated from sequence
-
?
-
x * 67000, recombinant enzyme, SDS-PAGE
?
-
x * 135000, SDS-PAGE
-
?
-
x * 119560, SDS-PAGE
-
?
-
x * 68709, amino acid sequence calculation, x * 73000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 49600, isozyme AI-1, SDS-PAGE, x * 56700, isozyme AI-2, SDS-PAGE, x * 100000, isozyme AII, SDS-PAGE
?
x * 66000, wild-type and mutant enzymes, SDS-PAGE
?
-
x * 66000, wild-type and mutant enzymes, SDS-PAGE
-
?
-
x * 56269, MARDI-TOF mass spectrometry, non-glycosylated alpha-amylase
?
-
x * 56286, deduced from nucleotide sequence
?
x * 45100, calculated from sequence
?
-
x * 55000, SDS-PAGE
-
?
-
x * 45000, about, SDS-PAGE
?
x * 71700, recombinant His-tagged enzyme, SDS-PAGE
?
x * 68800, recombinant enzyme, SDS-PAGE
?
-
x * 60000, about, SDS-PAGE
?
-
x * 96000, SDS-PAGE
-
?
x * 52875, extracellular enzyme, calculation from nucleotide sequence
?
-
x * 76084, amino acid sequence calculation
?
x * 49456, calculated from sequence
?
-
x * 42000, SDS-PAGE
-
?
-
x * 49456, calculated from sequence
-
?
-
x * 92000, SDS-PAGE
-
?
x * 60000, recombinant His6-tagged enzyme, SDS-PAGE, x * 58500, about, sequence calculation
?
-
x * 60000, recombinant His6-tagged enzyme, SDS-PAGE, x * 58500, about, sequence calculation
-
?
x * 53000, recombinant enzyme, SDS-PAGE
?
-
x * 53000, recombinant enzyme, SDS-PAGE
-
?
-
x * 70000, about, SDS-PAGE
?
-
x * 70000, about, SDS-PAGE
?
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 65000, recombinant enzyme, SDS-PAGE
-
?
x * 51544, calculated from sequence
?
-
x * 51544, calculated from sequence
-
?
-
x * 53600, SDS-PAGE
-
?
x * 51948, calculated from sequence
?
-
x * 51400, SDS-PAGE
-
?
-
x * 62000, about, SDS-PAGE
?
-
x * 58000, about, SDS-PAGE
?
x * 66000, about, recombinant His-tagged chimeric mutant enzyme AmyP-Cr, sequence calculation
?
-
x * 55000, about, SDS-PAGE
?
-
x * 46000, MALDI-TOF analysis
?
Wangia sp. C52
-
x * 60000, about, SDS-PAGE
dimer
-
2 * 79000, SDS-PAGE
dimer
-
2 * 79000, SDS-PAGE
-
dimer
-
2 * 59000, SDS-PAGE
dimer
-
2 * 66000, intracellular enzyme, electrophoresis in presence of 8 M urea
homodimer
2 * 66000, SDS-PAGE
homodimer
-
2 * 120000, SDS-PAGE
homodimer
-
2 * 120000, SDS-PAGE
-
monomer
-
1 * 30000, isozyme AoA1, SDS-PAGE, 1 * 45000, isozyme AoA2, SDS-PAGE
monomer
1 * 56700, MALDI-TOF mass spectrometry
monomer
-
1 * 59000, enzyme form Amyl II, SDS-PAGE
monomer
-
1 * 120000, enzyme form Amyl III, SDS-PAGE
monomer
-
1 * 46000, enzyme form Amyl I, SDS-PAGE
monomer
-
1 * 59000, enzyme form Amyl II, SDS-PAGE
-
monomer
-
1 * 120000, enzyme form Amyl III, SDS-PAGE
-
monomer
-
1 * 46000, enzyme form Amyl I, SDS-PAGE
-
monomer
-
1 * 54000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
1 * 55300, recombinant enzyme, SDS-PAGE
monomer
-
1 * 55300, recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
-
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
-
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 67000, extracellular enzyme, SDS-PAGE
monomer
-
1 * 205000, SDS-PAGE
monomer
-
1 * 67000, extracellular enzyme, SDS-PAGE
-
monomer
-
1 * 205000, SDS-PAGE
-
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 22500, SDS-PAGE
monomer
-
1 * 22500, SDS-PAGE
-
monomer
1 * 53000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 100000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
-
monomer
Halalkalibacterium halodurans
-
1 * 100000, alpha-amylase I, SDS-PAGE
monomer
Halalkalibacterium halodurans
-
1 * 75000, alpha-amylase II, SDS-PAGE
monomer
Halalkalibacterium halodurans 38C-2-1
-
1 * 100000, alpha-amylase I, SDS-PAGE
-
monomer
Halalkalibacterium halodurans 38C-2-1
-
1 * 75000, alpha-amylase II, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE
-
monomer
-
1 * 46000, alpha-amylase I, SDS-PAGE
monomer
-
1 * 61856, isoenzymes of family A, SDS-PAGE
monomer
-
1 * 56133, isoenzymes of family B, SDS-PAGE
monomer
-
1 * 62000, parotid enzyme of enzyme family A, SDS-PAGE
monomer
-
x * 54000, pancreatic enzyme, SDS-PAGE
monomer
-
1 * 56000, parotid enzyme of enzyme family B, SDS-PAGE
monomer
-
1 * 31000, SDS-PAGE
monomer
-
1 * 31000, SDS-PAGE
-
monomer
-
1 * 22500, SDS-PAGE
monomer
-
1 * 22500, SDS-PAGE
-
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 51000, SDS-PAGE
monomer
-
1 * 51000, SDS-PAGE
-
monomer
-
1 * 33000, SDS-PAGE
monomer
-
x * 66000, enzyme form II, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
-
monomer
-
x * 97000, SDS-PAGE
monomer
-
x * 97000, SDS-PAGE
-
monomer
1 * 48138, mass spectrometry, 1 * 48000, SDS-PAGE, 1 * 50414, sequence calculation
monomer
-
1 * 48138, mass spectrometry, 1 * 48000, SDS-PAGE, 1 * 50414, sequence calculation
-
monomer
-
1 * 61200, recombinant enzyme, SDS-PAGE
monomer
-
1 * 61200, recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
1 * 48000, gel filtration
monomer
-
1 * 48000, gel filtration
-
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 51000, SDS-PAGE
tetramer
4 * 100000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
-
tetramer
-
4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE
tetramer
-
4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE
-
additional information
the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902)
additional information
-
the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902)
-
additional information
-
loosly packed enzyme interior, secondary enzyme structure does not protect against aqueous environment, overview
additional information
-
three-dimensional structure analysis of intact and unfolded enzyme
additional information
-
loosly packed enzyme interior, secondary enzyme structure does not protect against aqueous environment, overview
-
additional information
three-dimensional structure analysis of intact and unfolded enzyme
additional information
-
comparison of primary and secondary enzyme structure
additional information
-
comparison of primary and secondary enzyme structure
-
additional information
SusG is composed of A, B, and C domains that share structural features with other amylases. The A domain, residues 43-152 and 364-607, has an eight-stranded alpha/beta barrel that contains the catalytic site, with the B domain, residues 153-215 and 336-363, inserted between beta3 and alpha3 of the A domain. The B domain consists of two two-stranded antiparallel beta sheets, two alpha helices, and three 310 helices that pack against the A domain and contribute to the size and accessibility of the active site. The C domain, residues 608-692, folds into an eight-stranded beta sandwich, structure model, overview
additional information
three-dimensional enzyme structure modelling
additional information
-
three-dimensional enzyme structure modelling
additional information
-
presence of random coil conformation
additional information
-
peptide mapping, overview
additional information
-
AmyA forms unique reversiblepoly-dispersed oligomers that show high thermal stability, sedimentation velocity and circular dichroism structure analysis
additional information
P04745
enzyme structural organization, identification of several isozymes with molecular weights of 18-59 kDa in salivary gland by two-dimensional gel electrophoresis and MALDI-TOF mass spectrometry analysis, detailed overview
additional information
-
enzyme structural organization, identification of several isozymes with molecular weights of 18-59 kDa in salivary gland by two-dimensional gel electrophoresis and MALDI-TOF mass spectrometry analysis, detailed overview
additional information
-
HSA consists of three domains, dimer structure, packing, and interface, overview
additional information
-
the native enzyme contains 4.49% alpha-helices and 43.69% beta-sheets, while the denatured enzyme contains 11.53% alpha-helices and 28.35% beta-sheets
additional information
-
the native enzyme contains 4.49% alpha-helices and 43.69% beta-sheets, while the denatured enzyme contains 11.53% alpha-helices and 28.35% beta-sheets
-
additional information
-
the enzyme occurs in two forms, an aggregated form I and a monomeric form II, the latter is more abundant, but unstable
additional information
-
primary structure scheme
additional information
enzyme three-dimensional structure homology modelling, overview
additional information
-
enzyme three-dimensional structure homology modelling, overview
additional information
-
enzyme three-dimensional structure homology modelling, overview
-
additional information
three-dimensional enzyme structure modelling
additional information
-
three-dimensional enzyme structure modelling
additional information
-
the overall structure of amylase AMY121 is composed by three distinct domains (A-C), which are typical in liquefying-type bacterial alpha-amylases, overview
additional information
-
three-dimensional structure modelling
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D231N
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
D233N
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively
D438G
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
I34H
-
mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity
P407H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type
Q67H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type
V289D
-
the mutation results in complete loss of the alpha-amylase activity
V289E
-
the mutation results in complete loss of the alpha-amylase activity
V289F
-
the mutant shows 48.9% activity compared to the wild type enzyme
V289G
-
the mutant shows 14.5% activity compared to the wild type enzyme
V289I
-
the mutant shows 20% more hydrolytic activity than the wild type enzyme
V289L
-
the mutant shows 36.4% activity compared to the wild type enzyme
V289P
-
the mutant shows 2.2% activity compared to the wild type enzyme
V289R
-
the mutation results in complete loss of the alpha-amylase activity
V289S
-
the mutant shows 5% activity compared to the wild type enzyme
V289Y
-
the mutant shows 9.2% activity compared to the wild type enzyme, the mutant has acquired a transglycosylation activity, which results in the change of product profile of the reaction, giving a longer oligosaccharide
I34H
-
mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity
-
P407H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type
-
Q67H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type
-
D231N
-
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
-
D233N
-
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively
-
D438G
-
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
-
V289F
-
the mutant shows 48.9% activity compared to the wild type enzyme
-
V289G
-
the mutant shows 14.5% activity compared to the wild type enzyme
-
V289I
-
the mutant shows 20% more hydrolytic activity than the wild type enzyme
-
V289L
-
the mutant shows 36.4% activity compared to the wild type enzyme
-
V289Y
-
the mutant shows 9.2% activity compared to the wild type enzyme, the mutant has acquired a transglycosylation activity, which results in the change of product profile of the reaction, giving a longer oligosaccharide
-
A209V
more thermostable than wild type enzyme
H133Y
more thermostable than wild type enzyme
I157S/W193R
-
random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme
L134R
amyl, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
L134R/S320A
amyd, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. The highest kcat/Km with pH 4.5 approximately 14times that of the wild-type is observed in the double mutant. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
M15T/H133Y/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 4fold longer half-life than wild-type enzyme
M15T/H133Y/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 23fold longer half-life than wild-type enzyme
M15T/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 1.5fold longer half-life than wild-type enzyme
M15T/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 4.5fold longer half-life than wild-type enzyme
N172R/H156Y/A181T
-
the mutations increase the thermostability of alpha-amylase by 5fold
S320A
amy2, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
L134R
-
amyl, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
L134R/S320A
-
amyd, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. The highest kcat/Km with pH 4.5 approximately 14times that of the wild-type is observed in the double mutant. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
S320A
-
amy2, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
I157S/W193R
-
random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme
-
E151A
-
mutant of N- and C-terminally truncated alpha-amylase, specific activity for E151A is decreased by more than 30%
E219
-
mutant of N- and C-terminally truncated alpha-amylase, decreased half-life at 70°C
E295A
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
E295D
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
H191L
-
similar activity as wild-type
H239L
-
similar activity as wild-type
H305L
-
similar activity as wild-type
H323L
-
approx. 50% of wild-type activity
H436L
-
approx. 40% of wild-type activity, reduced thermostability
H475L
-
similar activity as wild-type
M231L
-
construction of a thermostable variant BACDELTANC/DELTARS derived from the truncated alpha-amylase BACDELTANC, introduction of mutation M231L for enhancing the resistance towards chemical oxidation, and site-directed mutagenesis of the 483th codon in the gene to stop codon, resulting in the mutants BACDELTANC/DELTARS/M231L/DELTAC31. Mutants BACDELTANC/DELTARS/M231L and BACDELTANC/DELTARS/M231L/DELTAC31 are very similar to BACDELTANC in terms of specific activity, kinetic parameters, pH-activity profile, and the hydrolysis of raw starch, but the engineered enzymes show an increased half-life at 70°C
E151A
-
mutant of N- and C-terminally truncated alpha-amylase, specific activity for E151A is decreased by more than 30%
-
E219
-
mutant of N- and C-terminally truncated alpha-amylase, decreased half-life at 70°C
-
E295A
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
-
E295D
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
-
H191L
-
similar activity as wild-type
-
H239L
-
similar activity as wild-type
-
H305L
-
similar activity as wild-type
-
H323L
-
approx. 50% of wild-type activity
-
M231L
-
construction of a thermostable variant BACDELTANC/DELTARS derived from the truncated alpha-amylase BACDELTANC, introduction of mutation M231L for enhancing the resistance towards chemical oxidation, and site-directed mutagenesis of the 483th codon in the gene to stop codon, resulting in the mutants BACDELTANC/DELTARS/M231L/DELTAC31. Mutants BACDELTANC/DELTARS/M231L and BACDELTANC/DELTARS/M231L/DELTAC31 are very similar to BACDELTANC in terms of specific activity, kinetic parameters, pH-activity profile, and the hydrolysis of raw starch, but the engineered enzymes show an increased half-life at 70°C
-
H100I
increase in half-inactivation temperature, kcat value similar to wild-type
H100M/D144R
increase in half-inactivation temperature, 70% decrease in kcat value
L134R/S320A
-
the mutagenised protein is more acid resistant than the native protein. The optimum pH and stable range of pH with the mutagenised protein is 4.5 and 4.0 to 6.5, respectively, compared with pH 6.5 and 5.5 to 7.0 as the favorite pH and pH stability range of the native protein
N197C
decrease in half-inactivation temperature, kcat value similar to wild-type
T147P
increase in half-inactivation temperature, 25% decrease in kcat value
H100I
-
increase in half-inactivation temperature, kcat value similar to wild-type
-
H100M/D144R
-
increase in half-inactivation temperature, 70% decrease in kcat value
-
N197C
-
decrease in half-inactivation temperature, kcat value similar to wild-type
-
T147P
-
increase in half-inactivation temperature, 25% decrease in kcat value
-
L134R/S320A
-
the mutagenised protein is more acid resistant than the native protein. The optimum pH and stable range of pH with the mutagenised protein is 4.5 and 4.0 to 6.5, respectively, compared with pH 6.5 and 5.5 to 7.0 as the favorite pH and pH stability range of the native protein
-
D498N
site-directed mutagenesis, a catalytically inactive mutant, crystal structure determination and analysis
M197A
site-directed mutagenesis. Studies of its catalytic properties show no effect on the thermostability, pH activity/stability, calcium demand and chelator resistance. Specific activity is decreased from 1000 to 845 U/mg. The profile of starch hydrolysis is affected. As a result hereof AmyUS100DELTAIG/M197A produces in majority maltose and maltotriose as major products compared to maltohexaose and maltopentaose produced by the wild-type and the AmyUS100DELTAIG variant. The mutant retains 85% of its original activity. 70% of the mutantM197A activity is retained after 60 min of treatment at 60°C in the presence of 1.8 M H2O2, whereas AmyUS100DELTAIG is totally inactivated. These results confirm the importance of Met197 in the oxidative sensibility, situated in the cavity of the active site
DELTAAmyB
-
lacking the N-domain, with no significant difference between the rates of soluble starch degradation, indicating that the N-domain does not play a direct role in catalysis with this substrate. For insoluble starch AmyB shows increase binding compared with DELTAAmyB, suggesting that the N-domain enhances the ability of AmyB to bind this substrate. The temperature stability of AmyB and DELTAAmyB, lacking the N-domain are strongly influenced by NaCl concentration, shown by an increasing melting temperature with increased NaCl concentrations up to 4-4.5 M
D300A
-
0.0005% of wild-type starch hydrolyzing activity
D300N
-
0.0005% of wild-type starch hydrolyzing activity
E233A
-
0.005% of wild-type starch hydrolyzing activity
E233A/D300A
-
0.001% of wild-type starch hydrolyzing activity
E233Q
-
0.0005% of wild-type starch hydrolyzing activity
N298S
variant of the enzyme has an approximate 200fold reduction in affinity for chloride ion
W134A/W203A/Y276A/W284A/W316A/W388A
P04745
HSAmy-ar, multiple mutant, 10fold reduction of activity compared with wild-type enzyme and also sigificant reductaion of starch binding activity
W203A
P04745
2fold reduction of activity compared to the wild-type enzyme, similar starch-binding activity like the wild-type enzyme
W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
W316A/W388A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
W58L
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
Y151M
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
Y276/W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
Y276A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
H395A
located in the C-domain, the sugar tong, may be involved in the allosteric activation of the enzyme
S378P
kcat/KM for amylose is 1.2fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is nearly identical to wild-type value
S378T
kcat/KM for amylose is 1.4fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is nearly identical to wild-type value
T212P
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
T212W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
T212Y
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A/T212W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A/T212Y
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A/Y380A
loss of 18-36% activity relative to wild-type
Y105A/Y380M
loss of 18-36% activity relative to wild-type
Y105F
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y380A/H395A
located in the C-domain, the sugar tong, may be involved in the allosteric activation of the enzyme
Y380F
kcat/KM for amylose is fold lowerthan wild-type value. kcat/KM for is 2.6fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is 1.1fold higher than wild-type value
N240Q
-
mutant of isoenzyme Amy1A
A53S
in comparison to the wild type, calcium ion has more effect on the catalytic efficiency, kcat/Km, and half-life (at 60°C) of A53S mutant, although the overall activity (kcat/Km) has not improved, about 80% of activity is maintained in the case of A53S mutant
H58I
calcium-independent mutant possessing high thermostability, in the absence of CaCl2, the H58I mutant is much more stable than the wild type and there is a 7fold increase in the residual activity of H58I mutant after 30 min of incubation as compared to the wild type
A53S
-
in comparison to the wild type, calcium ion has more effect on the catalytic efficiency, kcat/Km, and half-life (at 60°C) of A53S mutant, although the overall activity (kcat/Km) has not improved, about 80% of activity is maintained in the case of A53S mutant
-
H58I
-
calcium-independent mutant possessing high thermostability, in the absence of CaCl2, the H58I mutant is much more stable than the wild type and there is a 7fold increase in the residual activity of H58I mutant after 30 min of incubation as compared to the wild type
-
K300R
-
47% of wild-type kcat
K300R/N150D/V196F/Q164I/T232V
-
44% of wild-type kcat, increase in temperature stability
N150D
-
98% of wild-type kcat
Q164I
-
73% of wild-type kcat
T232V
-
105% of wild-type kcat
V196F
-
108% of wild-type kcat
H286A
site-directed mutagenesis, altered activity compared to wild-type
H286C
site-directed mutagenesis, altered activity compared to wild-type
H286D
site-directed mutagenesis, the mutant shows a decreased optimum pH compared to wild-type, altered activity compared to wild-type
H286E
site-directed mutagenesis, the mutant shows a 6.43fold increase in half-life at pH 4.5 and an decreased pH optimum compared to wild-type, altered activity compared to wild-type
H286F
site-directed mutagenesis, altered activity compared to wild-type
H286G
site-directed mutagenesis, altered activity compared to wild-type
H286I
site-directed mutagenesis, mutant H286I shows a 1.5fold increase in half-life at 55°C compared to wild-type, and the mutant shows an increased optimum temperature and a decreased pH optimum compared to wild-type, altered activity compared to wild-type
H286K
site-directed mutagenesis, altered activity compared to wild-type
H286L
site-directed mutagenesis, the mutant shows an increased optimum temperature and a decreased pH optimum compared to wild-type, the ability to form maltose from soluble starch is significantly improved, altered activity compared to wild-type
H286M
site-directed mutagenesis, the mutant shows an inproved ability to form maltose from soluble starch compared to wild-type, altered activity compared to wild-type
H286N
site-directed mutagenesis, altered activity compared to wild-type
H286P
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286Q
site-directed mutagenesis, altered activity compared to wild-type
H286R
site-directed mutagenesis, altered activity compared to wild-type
H286S
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286T
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286V
site-directed mutagenesis, altered activity compared to wild-type
H286W
site-directed mutagenesis, altered activity compared to wild-type
H286Y
site-directed mutagenesis, altered activity compared to wild-type
D325N
-
site-directed mutagenesis, inactive mutant
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
D325N
-
site-directed mutagenesis, inactive mutant
-
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
-
F179V
yield a similar product profile to that of the wild-type enzyme
H222D
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol and butanol are used as nucleophil instead of H2O, the mutant produces more methylglucoside and butylglucoside than wild-type, respectively
H222E
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol is used as nucleophil instead of H2O, more methylglucoside is produced than with wild-type enzyme. Butanol produces almost equal amount in both wild-type and H222E mutant
H222Q
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol and butanol are used as nucleophil instead of H2O, the mutant produces more methylglucoside and butylglucoside than wild-type, respectively
V259W
in addition to alpha-D-glucose and maltose the product profile is broadened with small amounts of maltotriose
W177V
yield a similar product profile to that of the wild-type enzyme
Y178V
yield a similar product profile to that of the wild-type enzyme
K205L
-
site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
K209A
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209C
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209D
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209E
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209F
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209G
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209H
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209I
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209L
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209M
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209N
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209P
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209Q
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209R
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209S
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209T
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209V
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209W
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209Y
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
Y187E
-
site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
Y187E/K205L
-
site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
Y105A
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A
43% of the activity compared to wild-type
Y380A
mutant fails to bind to beta-cyclodextrin-Sepharose, a starch-mimic resin used for alpha-amylase affinity purification. The Kd for beta-cyclodextrin binding to Y380A is 1.4 mm compared to 0.20-0.25 mM for the wild-type, S378P and S378T enzymes. Crystal structures of both wild-type and S378P enzymes, but not the Y380A enzyme, shows binding of the pseudotetrasaccharide acarbose at the sugar tongs site. beta-Cyclodextrin both inhibits binding to and suppresses activity on starch granules for wild-type and S378P enzymes, but does not affect these properties of Y380A. Y380A enzyme hydrolyzes amylose with reduced multiple attack. kcat/KM for amylose is 3.7fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is 2.4fold lower than wild-type value
Y380A
29-50% decrease in activity compared to wild-type enzyme
Y380M
mutant fails to bind to beta-cyclodextrin-Sepharose, a starch-mimic resin used for alpha-amylase affinity purification. The Kd for beta-cyclodextrin binding to Y380M is 1.4 mm compared to 0.20-0.25 mM for the wild-type, S378P and S378T enzymes. kcat/KM for amylose is 2.3fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is 1.8fold lower than wild-type value
Y380M
29-50% decrease in activity compared to wild-type enzyme
additional information
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construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans
additional information
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construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans. Generation of multi-copy integrants that can secrete high levels of heterologous protein using multiple transformation approach followed by post-transformational vector amplification (PTVA). Method evaluation and optimization
additional information
-
hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase, expression in Escherichia coli and Bacillus subtilis. The letters A and L in the hybrid names stand for the Bacillus amyloliquefaciens and the Bacillus licheniformis portion, respectively, and the numbers for the amino acid residues at the cross-over sites of the hybrid enzymes: Al76, Al108, AL112, AL142, AL147, AL149, AL151, LAL19-153, AL163, AL174
additional information
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hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase, expression in Escherichia coli and Bacillus subtilis. The letters A and L in the hybrid names stand for the Bacillus amyloliquefaciens and the Bacillus licheniformis portion, respectively, and the numbers for the amino acid residues at the cross-over sites of the hybrid enzymes: Al76, Al108, AL112, AL142, AL147, AL149, AL151, LAL19-153, AL163, AL174
additional information
engineering of the enzyme for improved industrial performance
additional information
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engineering of the enzyme for improved industrial performance
additional information
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repeated cycles of random mutagenesis of a region comprising residues from the position 34-281, mutant library construction. Mutant TP8H5 shows an altered pH profile as compared to the wild-type. The sequencing of variant TP8H5 indicated 2 amino acid changes, Ile157Ser and Trp193Arg, which are located in the solvent accessible flexible loop region in domain B
additional information
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repeated cycles of random mutagenesis of a region comprising residues from the position 34-281, mutant library construction. Mutant TP8H5 shows an altered pH profile as compared to the wild-type. The sequencing of variant TP8H5 indicated 2 amino acid changes, Ile157Ser and Trp193Arg, which are located in the solvent accessible flexible loop region in domain B
-
additional information
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enzyme immobilization, best at 4% alginate as compared to agar agar and other concentrations of alginate, overview
additional information
improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C
additional information
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improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C
-
additional information
enzyme silencing, evaluation in pairings of BGTG-1 RNAi or control males with virgin females, overview. Attenuation of BGTG-1 gene and protein expression has no impact on precopulatory behaviours exhibited by paired adult males and females
additional information
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enzyme silencing, evaluation in pairings of BGTG-1 RNAi or control males with virgin females, overview. Attenuation of BGTG-1 gene and protein expression has no impact on precopulatory behaviours exhibited by paired adult males and females
additional information
construction of a recombinant chimeric alpha-amylase (AmyP-Cr) by a catalytic core of alpha-amylase (AmyP) from a marine metagenomic library and a starch-binding domain (SBDCr) of alpha-amylase from Cryptococcus sp. S-2. The molecular fusion does not alter optimum pH, optimum temperature, hydrolysis products, and an ability of preferential and rapid degradation towards raw rice starch, but catalytic efficiency and thermostability are remarkably improved compared with those of the wild-type AmyP. The chimeric AmyP-Cr achieves the final hydrolysis degree of 61.7% for 10% raw rice starch and 47.3% for 15% raw rice starch after 4 h at 40°C with 1.0 U per mg of raw starch, the catalytic efficiency is 3.6-4.0 times higher than that of wild-type AmyP
additional information
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an N-terminally truncated form of Geobacillus sp. 4j alpha-amylase (Gs4j-amyA) is fused at its N-terminal end with the signal peptide of outer membrane protein A (OmpA) of Escherichia coli
additional information
construction of a dexadletion mutant AmySDELTAR179-G180 by deleting Arg179 and Gly180 through site-directed mutagenesis. The thermostability of mutant AmySDELTAR179-G180 is enhanced and the half-life at 100°C significantly increased from 24 to 33 min. In addition, AmySDELTAR179-G180 exhibits greatxader acid resistance and lower calcium requirements to maintain alpha-amylase activity compared to the wild-type enzyme AmyS. The sexadcretory capacity of the recombinant strain is evaluated by fed-batch fermentation in a 7.5-litre fermenter in which high alpha-amylase activity is obtained. The highest activity reaches 3300 U/ml with a high productivity of 45.8 U/(ml*h). Structural comparison of the AmyS model with that of the AmySDELTAR179-G180 mutant model shows that the deletion of R179-G180 causes a slight structural rearrangement and a decrease in AmySDELTAR179-G180 calcium requirements
additional information
construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans
additional information
-
construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans
additional information
construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans. Generation of multi-copy integrants that can secrete high levels of heterologous protein using multiple transformation approach followed by post-transformational vector amplification (PTVA). Method evaluation and optimization
additional information
-
construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans
-
additional information
-
construction of the chimeric amylase Ba-Gt-amy having catalytic domain from acidic amylase of Bacillus acidicola and N- and C-terminal additional amino acids from thermophilic alpha-amylase of Geobacillus thermoleovorans
-
additional information
-
construction of a mutant alpha-amylase, containing its signal peptide, which is fused to the starch binding domain, SBD, of the glucoamylase GA-I of Aspergillus niger via a 37 amino acid GA-I linker segment, the activity of the fusion protein is 2fold enhanced with amylose, and with starch at low concentration, not at high concentration, compared to the wild-type enzyme
additional information
immobilization of the alpha-amylase from Laceyella sacchari TSI-2 via entrapment, ionic binding and surface adsorption using 6 different matrices (Agar Agar, hydroxyapatite, Seralite SRA and SRC, silica + glutaraldehyde, and DEAE cellulose + glutaraldehyde), method evaluation, overview. The DEAE anion exchange cellulose with glutaraldehyde crosslinking method appears most effective for the immobilization with high operational stability. While the temperature optima and thermal stability of the immobilized alpha-amylase shift from 60°C to 70°C with increased half-life, the pH optimum remains unaltered while pH stability is shifted from pH 6.0 to pH 7.0. The stability of the immobilized enzyme improves in solvents. The enzyme catalysis in surfactants enhances, while the Km and Vmax are reduced after immobilization. Role of aliphatic amines, esters and alkenes in immobilization, structure analysis. Starch hydrolysis efficiency of the immobilized enzyme is 15.55%
additional information
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immobilization of the alpha-amylase from Laceyella sacchari TSI-2 via entrapment, ionic binding and surface adsorption using 6 different matrices (Agar Agar, hydroxyapatite, Seralite SRA and SRC, silica + glutaraldehyde, and DEAE cellulose + glutaraldehyde), method evaluation, overview. The DEAE anion exchange cellulose with glutaraldehyde crosslinking method appears most effective for the immobilization with high operational stability. While the temperature optima and thermal stability of the immobilized alpha-amylase shift from 60°C to 70°C with increased half-life, the pH optimum remains unaltered while pH stability is shifted from pH 6.0 to pH 7.0. The stability of the immobilized enzyme improves in solvents. The enzyme catalysis in surfactants enhances, while the Km and Vmax are reduced after immobilization. Role of aliphatic amines, esters and alkenes in immobilization, structure analysis. Starch hydrolysis efficiency of the immobilized enzyme is 15.55%
-
additional information
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deletion of C-terminus, does not bind and hydrolyse raw starch
additional information
random chemical mutagenesis by the treatment of cells with sodium azide, alkali-tolerant Microbacterium foliorum strain GA2 is randomly mutated using UV radiation and sodium azide to obtain a mutant with higher cold-active extracellular amylolytic activity, designated as MFSD20, which is selected owing to its higher amylase activity at 20°C. Under optimized conditions, amylase production is achieved best with raw banana peels (5000 units) in solid-state fermentation (SSF)
additional information
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random chemical mutagenesis by the treatment of cells with sodium azide, alkali-tolerant Microbacterium foliorum strain GA2 is randomly mutated using UV radiation and sodium azide to obtain a mutant with higher cold-active extracellular amylolytic activity, designated as MFSD20, which is selected owing to its higher amylase activity at 20°C. Under optimized conditions, amylase production is achieved best with raw banana peels (5000 units) in solid-state fermentation (SSF)
-
additional information
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chimeric enzyme engineered from two rice alpha-amylases isoenzymes, Amy1A and Amy3D. Amy1 shows high activity in soluble-starch hydrolysis and low activity in oligosaccharide degradation, while Amy3D shows low activity in soluble-starch hydrolysis and high activity in oligosaccharide degradation. The chimeric enzyme shows high activities in both soluble-starch hydrolysis and oligosaccharide degradation
additional information
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creation of a chimeric enzyme Amy1A/3D, which has 158 amino acid residues of the N-terminus of isoenzyme Amy1A and 252 amino acid residues of the C-terminus of isoenzyme Amy3D
additional information
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immobilization of the enzyme on Celite by an adsoption method with a yield of 87.6% adsorbed enzyme, evaluation of enzyme parameters, which shows improved operational stability, storage stability, and thermal stability, overview
additional information
activities and half-lives of mutant enzymes compared to wild-type enzyme at different pH values, and molecular docking of maltotriose to wild-type and mutant enzymes, overview
additional information
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gene for alpha-amylase from Debaryomyces occidentalis was integrated into genom of Saccharomyces cerevisiae
additional information
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recombinant strain with integration of the alpha-amylase gene from Streptococcus bovis
additional information
development of genetic lines engineered to overexpress TaAMY3 (A3OE) targeted to the amyloplasts in the endosperm of the grain demonstrate an increase of total alpha-amylase activity in harvested grains from 2 to 2000fold compared to negative segregant controls. Increased activity does not have a significant impact on starch content but leads to an increase of soluble carbohydrate (mainly sucrose and glucose) and trialcylglycerol (TAG) in the endosperm of dry grain, overview
additional information
-
development of genetic lines engineered to overexpress TaAMY3 (A3OE) targeted to the amyloplasts in the endosperm of the grain demonstrate an increase of total alpha-amylase activity in harvested grains from 2 to 2000fold compared to negative segregant controls. Increased activity does not have a significant impact on starch content but leads to an increase of soluble carbohydrate (mainly sucrose and glucose) and trialcylglycerol (TAG) in the endosperm of dry grain, overview
additional information
construction of a recombinant chimeric alpha-amylase (AmyP-Cr) by a catalytic core of alpha-amylase (AmyP) from a marine metagenomic library and a starch-binding domain (SBDCr) of alpha-amylase from Cryptococcus sp. S-2. The molecular fusion does not alter optimum pH, optimum temperature, hydrolysis products, and an ability of preferential and rapid degradation towards raw rice starch, but catalytic efficiency and thermostability are remarkably improved compared with those of the wild-type AmyP. The chimeric AmyP-Cr achieves the final hydrolysis degree of 61.7% for 10% raw rice starch and 47.3% for 15% raw rice starch after 4 h at 40°C with 1.0 U per mg of raw starch, the catalytic efficiency is 3.6-4.0 times higher than that of wild-type AmyP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1 - 2
-
65°C, 15 min, stable
393406, 393411
10 - 12
-
stable at
750825
10.5
-
45% loss of activity after 15 h at 37°C
657151
11 - 12
-
50% remaining activity after 24 h at 25°C
752016
2
-
70°C, 30 min, more than 70% of the activity remains
393388
2 - 12
-
purified enzyme, 50% activity remaining at pH 5.0 and pH 9.0, inactiuvation at pH 2.0 and pH 12.0, profile, overview
701769
2.2
-
37°C, 30 min, 13% loss of activity
393439
3 - 11
purified recombinant isozyme HaAmy1 is completely stable at, isozymes HaAmy1 and HaAmy2 show 10% and 5% increase in the amylase activity at pH 9.0 and pH 5.0, respectively
749947
3.4 - 6.4
-
optimal stability
393406
3.5 - 6.5
-
stable
393393
3.5 - 7.5
-
remains stable from pH 3.5-7.0, the enzyme activity keeps above 75% after treatment at pH values ranging from 3.5 to 6.0, for pH values beyond 7.5 or less than 3.5 the enzyme activity decreases drastically
704059
3.6
-
1 h, complete loss of activity
681158
3.9 - 11.9
-
20% loss of activity after 24 h at 4°C
655034
4 - 4.5
-
24 h, no loss of activity
678788
4 - 6.5
-
70°C, 1 h, stable pH-range for mutant enzyme L134R/S320A
677791
4 - 7
-
ScAmy43 is stable over a narrow range, pH 4.0: below 60% residual activity, pH 7: below 80% residual activity, after incubation at various pH at 4°C for 24 h, assay at pH 4.0 and 55°C for 30 min
693602
4.2
-
at 3 M NaCl, half-life: 5.7 h
727458
4.5 - 10
-
purified recombinant enzyme, 30 min, over 80% activity remaining
750813
4.5 - 7.2
-
purified enzyme, 4°C, 24 h, stable at
749783
4.5 - 8
-
enzymes from strain SB, N, P, and T are stable
393441
4.6
-
at 3 M NaCl, half-life: 138 h
727458
4.6 - 10.4
-
20% loss of activity after 24 h at 4°C
655034
4.8 - 8
-
over 90% of the secondary and tertiary structural elements are retained, indicating unfolding of the enzyme under both acidic and basic pH conditions. The enzyme retains its native conformation. The enzyme is found to be unfolded with loss of both structure and activity at pH below 3.0 and above 10.0
691135
5 - 11
-
the relative activities at pH5.0 and 9.0 are about 84% and 63%, respectively, of that measured at optimum pH 6.5, the activity decreases rapidly to 11% at pH 10.0
701769
5.5 - 7
-
70°C, 1 h, stable pH-range for wild-type enzyme
677791
5.5 - 8.5
-
stable
393446
5.8 - 7.5
-
25°C, 0.067 M phosphate buffer, enzyme retains over 93% of its activity
393421
5.9
-
optimal stability of the enzyme from strain F
393441
6 - 12
recombinant enzyme, stable at
750980
6 - 13
-
stable at
750825
6 - 7.5
-
4°C, 24 h, purified enzyme, stable
664782
6 - 9.5
purified recombinant His-tagged enzyme, 30 min, over 70% activity remaining
752126
6.3 - 7.9
-
stable
393387
7 - 9
-
30°C, 18 h, stable
393404
7.5
-
purified enzyme, 90% activity remaining after 200 min
750793
7.5 - 8.5
-
AmyB and the variant DELTAAmyB, lacking the N-domain depend only weakly on pH. At 7.5-8.5 they show almost identical Tm values
693640
8 - 12
-
purified enzyme, stable at
750825
8.5 - 11
40°C, 60 min, enzyme retains almost 80% of its initial activity
678857
10
-
30 min, whole cells, 55% amylase activity is remaining
750079
10
30 min, whole cells, 95% amylase activity is remaining
750079
10
-
30 min, whole cells, 90% amylase activity is remaining
750079
10
-
30 min, whole cells, 70% amylase activity is remaining
750079
10
-
at 3 M NaCl, half-life: 240 d
727458
10
purified enzyme, completely stable for 6 h, loss of 50% activity after 9 h, inactivation after 11 h
750816
11
-
relatively stable in alkaline condition with at least 70% of the activity at pH 9.0
693478
11
purified enzyme, completely stable for 3 h, loss of 50% activity after 6 h, inactivation after 8 h
750816
11
-
purified recombinant enzyme, 30 min, 40% activity remaining
750813
3
purified enzyme, 25°C, 24 h, 40% activity remaining
749443
3
-
30°C, 18 h, 50% loss of activity
393404
3
-
10°C, 24 h, 95% loss of activity
393380
3
Thermomonospora vulgaris
-
few min, complete inactivation
393425
3 - 6
-
loses its activity in acidic buffers (pH 36)
727441
3 - 6
-
over 80% acivity remaining within this range
717552
3 - 9
stable at
750825
3.5
-
AMY1 is more stable at low pH than AMY2. The activity of AMY2 rapidly decreases to 51% after 3 min incubation at pH 3.5
693604
3.5
-
24 h, complete loss of activity
678788
3.8
-
1 h, 90% loss of activity
681158
3.8
Thermomonospora vulgaris
-
5 min, complete inactivation
393406
4
-
1 h, 78% loss of activity
681158
4
-
30°C, 18 h, 34% loss of activity
393404
4
-
65°C, 15 min, about 20% loss of activity
393411
4
-
30°C, 30 min, inactivation below
393472
4
-
37°C, 1 h, about 60% loss of activity
393383
4
-
purified recombinant enzyme, 30 min, 40% activity remaining
750813
4 - 10
-
purified native enzyme, highly stable at
750781
4 - 10
-
30°C, 30 min, stable
393365
4 - 10
-
the enzyme activity is increased gradually from 4.0 to 9.0 and 4.0 to 10.0 in case of midgut and salivary enzymes, respectively and decreases thereafter with increasing pH
702990
4 - 5
-
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, 12 h, 90% activity remaining
751255
4 - 5
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, 12 h, 90% activity remaining
751255
4 - 5
-
purified enzyme, stable
718308
4 - 5.5
-
80°C, 15 min, stable
393388
4 - 5.5
-
purified enzyme, stable
717982
4 - 8
-
30 min, stable
393459
4 - 8
-
no loss of activity after 24 h at pH 5.0 to pH 6.0, approx. 90% loss of activity after 24 h at pH 4.0, approx. 80% loss of activity after 24 h at pH 8.0
655358
4 - 9
recombinant enzyme, retains over 60% of its activity between pH 4.0 and pH 9.0 after incubation for 24 h
749624
4 - 9
-
most stable in the pH range 4.0-9.0
393448
4 - 9
purified recombinant His-tagged enzyme, over 50% activity remaining, completely stable at pH 6.0, over 80% activity remaining at pH 5.0-8.0
750501
4 - 9
incubation at different pH conditions from pH 4.5 to pH 9 for 24h in 4°C followed by activity measurement, retention of more than 98% of initial activity
681349
4 - 9
-
room temperature, 24 h, stable
393408
4.5
-
90°C, 30 min, in absence of substrate, more than 90% of the activity remains
393388
4.5
the mutant L134R/S320A shows a stronger activity in acidic conditions, In contrast, the wild-type is sensitive to acidic pH. The double mutant is more effective in increasing enzyme stability against acidic pH than L134R and S320A
690586
4.5
-
more than 80% of the maximum activity remains at pH 4.5 and 95°C
690582
4.5 - 11
-
stable
678760
4.5 - 11
purified enzyme, stable at
750825
5
-
30 min, whole cells, 40% amylase activity is remaining
750079
5
-
30°C, 18 h, 25% loss of activity
393404
5
-
90°C, 1 h, complete inactivation, alpha-amylase PA
680540
5
30 min, whole cells, 90% amylase activity is remaining
750079
5
-
30 min, whole cells, 80% amylase activity is remaining
750079
5
-
30 min, whole cells, 55% amylase activity is remaining
750079
5
-
50°C, 1 h, about 40% loss of activity
678799
5
-
at 3 M NaCl, half-life: 15000 h
727458
5
-
AmyB and the variant DELTAAmyB, lacking the N-domain depend only weakly on pH. At pH 5.0 both proteins are destabilized
693640
5
-
24 h, about 10% loss of activity
678788
5
purified recombinant His-tagged enzyme, 30% activity remaining
752105
5 - 10
-
purified enzyme, stable at
750825
5 - 10
-
isozyme RBLA, stable for 24 h at 4°C
664790
5 - 10
-
Amy I, 24 h at 4°C, pH 5, ca. 22% residual activity, pH 10: ca. 10% residual activity, maximal stability between pH 7 and 9
691902
5 - 10
-
19% and 36% of maximum activity at pH 4.5 and 9.5, respectively
701874
5 - 10
-
30°C, 3 h, stable
171741
5 - 10
-
4°C, 24 h, stable
681739
5 - 10
-
purified enzyme, stable at
750825
5 - 6
-
stable
666693
5 - 6
-
stable at 100°C for 1 h
690582
5 - 7
-
purified native enzyme, 90% initial activity is retained after 48 h
750802
5 - 7
-
stable at 80°C and 90°C for 1 h
690582
5 - 8
-
stable for 1 h
666785
5 - 8
-
16 h, purified recombinant His-tagged enzyme, 90% stable
664980
5 - 8
-
12 h, isozymes AI-1 and AI-2, and AII, most stable at pH 7.0, about 50% of maximal activity at pH 3.5-4.5 and at pH 8.0-8.5, dependent on the isozyme, overview
665013
5 - 9
-
stable at
750825
5 - 9
-
purified enzyme, stable, 24 h at 4°C
666829
5 - 9
-
4°C, 24 h, enzyme retains more than 50% activity
749668
5 - 9
-
Amy II, 24 h at 4°C, pH 5, ca. 42% residual activity, pH 9: ca. 75% residual activity, maximal stability between pH 7 and 9
691902
5 - 9
-
purified native enzyme, 100% activity remaining when pre-incubated at pH 6.0 and pH 7.0 for 24 h
749440
5.5
-
purified enzyme, 20% activity remaining after 200 min
750793
5.5
-
90°C, 1 h, 50% loss of activity, alpha-amylase PA
680540
5.5 - 7.5
-
37°C, 1 h, stable
393383
5.5 - 7.5
purified recombinant His-tagged enzyme, 80% activity remaining
752105
5.5 - 9
-
purified enzyme, stable at
750825
5.5 - 9
-
isozymes RBSA-1 and BSA-2, stable for 24 h at 4°C
664790
6
-
purified enzyme, 80% activity remaining after 200 min
750793
6
-
30°C, 18 h, 15% loss of activity
393404
6
-
24 h, about 20% loss of activity
678788
6
the free enzyme shows maximum stability at pH 6.0 with the residual activity at 68% after 12 h, while the immobilized enzyme at pH 7.0 retaining 80% of activity after 12 h. Overall, a 10% enhancement in the residual activities is evident for the immobilized alpha-amylase compared to the free enzyme
750828
6
purified enzyme, completely stable for 16 h, loss of 50% activity after 21 h, inactivation after 24 h
750816
6
-
purified enzyme, stable at
750825
6 - 10
-
40°C, 30 min, 50 mM Tris-HCl buffer, stable
393431
6 - 10
-
55°C, 24 h, less than 20% loss of activity
393394
6 - 10
purified recombinant enzyme, 4°C, 24 h, stable
717948
6 - 10
20°C, stable for at least 14 h
729090
6 - 10
-
purified enzyme, stable at
750825
6 - 11
-
25°C, 24 h, stable
393406
6 - 11
-
20% loss of activity after 30 min at 40°C
654254
6 - 11
-
hig activity is retained, activity remains after 24 h incubation at alkaline pH
717451
6 - 11
-
26°C, 30 min, stable
393438
6 - 11
Halalkalibacterium halodurans
-
4°C, 24 h, stable, alpha-amylase I
678804
6 - 11
-
stable at
750825
6 - 7
purified enzyme, 25°C, 24 h, completely stable at
749443
6 - 7
-
30 min, whole cells, the amylase activity is completely stable
750079
6 - 7
-
30 min, whole cells, the amylase activity is completely stable
750079
6 - 8
-
25°C, 5 h, stable
393391
6 - 8
-
25°C, 30 min, stable
727461
6 - 8
-
at 3 M NaCl, half-life: 100 d
727458
6 - 9
30 min, whole cells, the amylase activity is completely stable
750079
6 - 9
-
4°C, 24 h, stable
393379
6 - 9
-
30 min, whole cells, the amylase activity is completely stable
750079
6 - 9
-
purified enzyme, 12 h, loss of 40% activity. The enzyme is relatively less stable at pH 6.0, pH 8.0 and pH 9.0 and is completely denatured at pH 4.0 and pH 5.0
752072
6 - 9
-
30°C, 3 h, stable
393403
6.5
-
purified enzyme, 90% activity remaining after 200 min
750793
6.5
-
purified enzyme, completely stable
701769
6.5 - 7.5
-
purified enzyme, stable at
750825
6.5 - 7.5
-
purified enzyme, stable at
750825
7
-
purified enzyme, stable at
750825
7
-
1 h, optimum stability
681158
7
-
purified enzyme, 95% activity remaining after 200 min
750793
7
-
AmyB and the variant DELTAAmyB, lacking the N-domain depend only weakly on pH. At pH 7.0 both proteins are equally stabilized
693640
7
-
24 h, about 50% loss of activity
678788
7
-
maximal stability for structure as well as activity at pH 7.0
691135
7
purified enzyme, completely stable for 12.5 h, loss of 50% activity after 18 h, inactivation after 21 h
750816
7
Thermomonospora vulgaris
-
60 min, stable
393406
7 - 10
-
stable
393412
7 - 10
-
purified enzyme, stable at
750825
7 - 10
-
stable at
750825
7 - 11
-
purified enzyme, stable at
750825
7 - 11
-
stable at
750825
7 - 8
-
10°C, 30 min, stable
393472
7 - 8
-
50°C, 1 h, no loss of activity
678799
8
-
1 h, 10% loss of activity
681158
8
-
purified enzyme, 80% activity remaining after 200 min
750793
8
-
56% remaining activity after 24 h at 25°C
752016
8
-
37°C, 1 h, about 75% loss of activity
393383
8
-
24 h, about 80% loss of activity
678788
8
purified enzyme, completely stable for 9 h, loss of 50% activity after 15 h, inactivation after 18 h
750816
8
-
55°C, 24 h, stable
393394
8.5
-
1 h, 29% loss of activity
681158
8.5
-
purified enzyme, 50% activity remaining after 200 min
750793
8.5
purified enzyme, 2 M NaCl, 55°C, 84% residual activity after 1 h
750835
9
-
1 h, 31% loss of activity
681158
9
purified enzyme, 25°C, 24 h, 40% activity remaining
749443
9
-
purified enzyme, 40% activity remaining after 200 min
750793
9
-
42% loss of activity after 15 h at 37°C
657151
9
-
at pH values higher than 9.0 enzymatic activity drops sharply to 50% of maximal activity
702987
9
-
50°C, 1 h, about 60% loss of activity
678799
9
-
at 3 M NaCl, half-life: 280 d
727458
9
purified recombinant His-tagged enzyme, 30% activity remaining
752105
9
purified enzyme, stable at
750825
9
purified enzyme, completely stable for 8 h, loss of 50% activity after 11 h, inactivation after 13 h
750816
9
Thermomonospora vulgaris
-
30 min, 25% loss of activity
393406
additional information
-
purified honey amylase is less pH-stable than in its natural environment
681158
additional information
-
Ca2+ is required for stability at high pH
393406
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0 - 40
purified recombinant His-tagged enzyme, over 80% activity remaining
0 - 60
purified recombinant His-tagged enzyme, stable up to 30°C, the enzyme activity drops to 82%, 39%, and 16% after5 min at 40°C, 50°C, and 60°C, and to 41%, 15%, and 4% after 30 min, respectively
10 - 45
purified recombinant His-tagged enzyme, over 50% activity remaining, completely stable at 20°C, over 80% activity remaining at 15-35°C
105
-
2 h, about 80% loss of activity
106
-
denaturation of the enzyme is irreversible above a Tm of approximately 106°C and can be described by a one-step irreversible model
115
3 h, 65% loss of activity
121
-
t1/2: 6.1 min, activation energy at 121°C is 316kJ/mol. Under an isothermal holding temperature of 121°C, the structure of the enzyme changes during denaturation from an alpha-helical structure, through a beta-sheet structure to an aggregated protein
20 - 70
-
purified native enzyme, 10 min, completely stable at
25 - 55
-
purified recombinant enzyme, 30 min, over 90% activity remaining
25 - 85
-
alpha-amylase do not unfold at pH 7.0 in the temperature range of 25-85°C, it unfolds at pH 4.8. Guanidine HCl is more effective than urea. Thermal unfolding is irreversible for Sorghum alpha-amylase
26
-
1 h, with 25% w/v raw corn starch, 11% loss of activity
30 - 75
-
the amylase is very stable at temperatures between 30 and 70°C after 150 min of incubation. It becomes completely inactivated at temperatures higher than 85°C for this period. The enzyme remains active to more than 75% up to 75°C for 45 min, the relative activities at 55 and 65°C are approximately 79% and 90% of the activity at 70°C, respectively. The enzyme displays a half-life of 48 min at 80°C
34
or below, 60 min, no loss of activity
37
-
1 h, with 25% w/v raw corn starch, 3% loss of activity
4 - 30
-
purified enzyme, 7 days, completely stable
4 - 47
the enzyme is relatively stable at 4°C for at least 4 h but is gradually inactivated at high temperatures, at 47°C the activity level remaining after 200 min is 25%
40 - 45
-
purified enzyme, stable at
40 - 60
-
purified enzyme, stable at
41
-
T50-value at pH 4.5, without CaCl2, alpha-amylase PA
43
purified recombinant His-tagged enzyme retaining 50% of its activity after 10 min incubation
45 - 50
-
more than 40% of the activity is lost
48
-
transition temperature T1/2 in the presence of 10 mM EDTA, thermal unfolding observed by circular dichroism spectrum measurements
50 - 55
purified enzyme, 2 M NaCl, pH 8.5, 84% residual activity after 1 h, highly stable also in presence of 3 M NaCl. The enzyme retains 65% activity after 24 h at 50°C, and its half-life is 5 h and 25 min at 55°C, and 12 min at 60°C
53
-
t1/2 inact of the native enzyme TAAUM is 6 min, of the modified enzyme TAAMOD 140 min
55 - 60
-
increasing the temperature above 55°C leads to irreversible thermal inactivation of the enzyme, there is complete loss of alpha-amylase activity after 30 min of incubation at 60°C
55 - 75
purified recombinant His-tagged enzyme, T50 value of AGXA with calcium ions is 73.8°C, T50 value of AGXA without calcium ions is 63.5°C
56
-
midpoint of thermal inactivation, soluble enzyme
58.3
mutant N197C, half inactivation
62.3
wild-type, half inactivation
66
-
melting temperature in absence of Ca2+
66.8
mutant H100I, half inactivation
68
-
recombinant ABA, 50-60% loss of activity after 1 h, complete loss of activity after 100 min, native ABA, 20% loss of activity after 1 h, approx. 50% loss of activity after 100 min
69.3
mutant T147P, half inactivation
70 - 100
-
the enzyme loses 50% of its activity after 10 min incubation at 70°C and is completely denatured at 100°C
70 - 80
-
activity is rapidly lost at 70°C and 80°C, no activity after a 30 min incubation
70.3
mutant H100M/D144R, half inactivation
73
-
melting temperature in presence of Ca2+
75 - 85
-
purified enzyme, stable at
84
-
T50-value at pH 6.0, 5 mM CaCl2, alpha-amylase PA
85 - 90
-
29% activity is seen after 10 min at 85 and 90°C, respectively
87
-
transition temperature T1/2 in the presence of 5 mM CaCl2, thermal unfolding observed by circular dichroism spectrum measurements
90 - 100
the enzyme retains its full activity after 7 h of incubation at 90°C, the half-life of AmyB is determined to be 50.2 and 28 h at 95°C and 100°C, respectively, thermostability is slightly enhanced by Ca2+
94
-
irreversible inactivation by conversion into an inactive 72 kDa trimer
10 - 60
recombinant enzyme, highly stable at
10 - 60
-
Amy I and Amy II, pH 8.0, 30 min, 10°C: ca. 90% relative activity for both Amy I and Amy II, 60°C: ca. 10% and ca. 90% relative activity for Amy I and Amy II, respectively, maximal stability between 50 and 60°C
100
-
larvaeal alpha-amylase loses 70% of activity after about 2 min, and after over 5 min, the enzyme is completely inactivated
100
-
4 h, in presence of starch, completely stable
100
-
remains active to 2 h in presence of substrate
100
around 60% of the enzyme activity is still detectable in wild-type and mutant enzymes after incubating in a boiling bath for 60 min
100
-
purified native enzyme, 10 min, no activity remaining
100
-
15% loss of activity after 15 min
100
-
10 min, pH 9.0, purified enzyme, inactivation
100
purified recombinant wild-type enzyme AmyS, half-life is 24 min, for the purified recombinant mutant AmySxadDELTAR179-G180 half-life is 33 min
100
-
t1/2 increases from 3.6 h to 5.6 h in presence of cholic acid
100
-
purified enzyme, half-life is 120 min
100
-
50% loss of activity after 50 h
100
6 h, 20% loss of activity
100
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 65% activity within 60 min
100
60 min, in presence of 2 mM Ca2+, about 60% loss of activity
100
-
85% of its initial activity after 4 h incubation, recombinant protein in Xanthomonas campestris
100
purified enzyme, 5 mM Ca2+, completely stable for 1 h, loss of 50% activity after 3 h, inactivation after 4 h
100
purified enzyme, without Ca2+, loss of 50% activity after 2 h, inactivation after 3h
100
-
30 min, 26% loss of activity
100
-
over 40% and 30% of the enzyme activity remains after incubation at 100°C for 2 and 3 h, respectively. At pH 5.0-6.0 stable for 1 h
110
-
1 h, 50-60% loss of activity
110
-
partially purified recombinant enzyme, half-life is 3.5 h, at pH 5.6 in 0.05 M acetate buffer
110
-
more than 50% of its initial activity after 4 h incubation, recombinant protein in Xanthomonas campestris
120
-
purified enzyme, 30 min, 45% activity remaining
120
1 h, 40% loss of activity
120
-
partially purified recombinant enzyme, 2 h, at pH 5.6 in 0.05 M acetate buffer, 24% remaining activity
120
-
more than 50% of its initial activity after 0.75 h incubation, recombinant protein in Xanthomonas campestris
20
purified wild-type enzyme shows 64% activity remaining after 2 h, the mutant enzyme from strain MFSD20 shows 70% remaining activity after 2 h
20
-
approx. 20% loss of activity after 30 min, approx. 10% loss of activity in the presence of 5 mM CaCl2
25
-
4 h, stable
25
-
56% remaining activity after 24 h at pH 8.0, 50% after 24 h at pH 11.0-12.0
25
-
24 h, completely stable
30
-
no loss of activity after 60 min
30
up to more than 60% relative activity, incubated for 30 min, is stable, even for 1 h
30
-
purified enzyme, 45 min, completely stable
30
-
20 min, stable, in absence of substrate
30
-
15 min, in presence of 3 mM Ca2+, 9% loss of activity of the enzyme from shoot, 14% loss of activity of the enzyme from cotyledons. 15 min, without Ca2+, 63% loss of activity of the enzyme from shoot, 81% loss of activity of the enzyme from cotyledons
30
-
approx. 30% loss of activity after 30 min, approx. 15% loss of activity in the presence of 5 mM CaCl2
35
-
10 min, stable
35
-
1 h, enzyme from strain P loses 6% of its activity, enzyme from strain SB loses 9% of its activity, enzyme from strain N loses 12% of its activity, enzyme from strain T loses 15% of its activity, enzyme from strain F is stable
35
-
1 h, purified isozyme BAA, 84.3% remaining activity
35
-
1 h, in absence of Ca2+, stable below
35
-
purified enzyme, 60 min, stable
35
140 min, no loss of activity
35
purified recombinant enzyme, completely stable for 140 min
37 - 100
-
purified enzyme, stable at
37 - 100
-
there is no detectable activity of plant-made AmyN26 below 37°C when compared to the wild type. The plant-made enzyme retains 85% of its initial activity after 3 h incubation at 100°C, the recombinant enzyme is completely inactivated after 30 min under the same conditions
4
-
1 h, purified isozyme BAA, completely stable
4
-
24 h, 50% loss of activity
4
-
1 h, with 25% w/v raw corn starch, 24% loss of activity
40
-
pH 7.4, half-life: 23.4 min
40
-
10 min, about 15% loss of activity
40
-
pH 5, 30 min, stable below
40
-
4 h, 69% remaining activity
40
-
stable at over 60 min
40
-
purified enzyme, 30 min, 50% activity remaining
40
-
30 min, 23% loss of activity
40
-
1 h, stable below in presence of 1 mM Ca2+
40
-
almost all of the enzyme activity remains after the enzyme is incubated for 60 min at temperatures of below 40°C
40
half-life of chimeric mutant AmyP-Cr at 40°C is prolonged by almost 2.6fold when compared with wild-type AmyP from the uncultured bacterium
40
up to more than 60% relative activity, incubated for 30 min, is stable, even for 1 h
40
-
pH 7.0, half-life: 2100 h
40
-
purified alpha-amylase I, stable up to, unstable above
40
-
no loss of activity after 10 min, 50% loss of activity after 100 min
40
-
30 min, stable up to
40
-
20 min, 92% remaining activity, in absence of substrate
40
purified recombinant His-tagged enzyme retaining 63% of its activity after 10 min incubation
40
120 min, about 45% loss of activity
40
purified recombinant enzyme, loss of 50% activity after 140 min
40
-
stable in the absence of substrate during 30 min pre-incubation, assay at pH 4.0 and 55°C, above 40°C rapid inactivation
40
-
the deglycosylated enzymes are slightly less thermo-stable than the glycosylated forms. PPA, PPA-I, and PPA-II retain more than 95% activities up to 40°C and the activities decrease with the increase in temperature. The difference is marginal in the mid-point of thermal transition shifting by 1-2°C
40
-
approx. 50% loss of activity after 30 min, approx. 25% loss of activity in the presence of 5 mM CaCl2
40
half-life of chimeric mutant AmyP-Cr at 40°C is 12 h, half-life of wild-type AmyP is 4.5 h
40
-
half-life after 4 h incubation
40 - 70
-
the enzyme is thermally stable up to 40°C and inactivated at 70°C, the enzyme has lost 80% of its activity at 60°C
40 - 70
-
purified native enzyme, 83% activity remains at 40°C after 180 min, 72% at 80°C, and 100% at 50°C
40 - 80
-
the enzyme retains more than 80% activity after 1 h incubation at 40°C, at 50°C, the enzyme retaines 80% of its initial activity, the activity is rapidly lost at 70 and 80°C and no activity is detected after a 30 min incubation. The enzyme shows a half-life value of 48 min at 70°C, while in the absence of calcium the half-life of the enzyme is only 5 min
40 - 80
after incubation at 40, 60 and 80°C for 1 h, the recombinant enzyme retains nearly 90, 80 and 50% of its initial activity, respectively. 83% of its initial activity is lost after being treated at 100°C for 20 min
45
30 min, stable up to
45
-
1 h, retains more than 80% of the activity
45
-
10 min, about 80% loss of activity
45
-
all five enzymes are rapidly inactivated above
45
-
20 min, recombinant enzyme, stable up to
45
-
pH 8.5, 20 mM Tris-HCl buffer, in absence of CaCl2, stable for 60 min
45
-
90 min, about 15% loss of activity of isoenzymes of family A and B
45
-
no loss of activity after 120 min
45
-
pH 5.0, 10 min, stable up to
45
-
wild-type, approx. 70% loss of activity after 45 min in the absence of starch, approx. 95% loss of activity after 45 min in the presence of 2% starch, K300R/N150D/V196F/Q164I/T232V mutant, approx. 50% loss of activity in the absence of starch
45
20 min, about 70% loss of activity
45
purified recombinant enzyme, inactivation within about 27 min
45
20 min, complete loss of activity
50
30 min, 29% loss of activity
50
-
pH 7.4, half-life: 6.16 min
50
purified enzyme, pH 5.0, 87% activity remaining after 60 min
50
-
10 min, complete loss of activity
50
-
partially purified enzyme, rapid loss of activity, Ca2+ protects
50
-
at a temperature approximating the optimal temperature of 50°C, the modified enzyme TAAMOD has a 28fold higher t1/2-inact of 340 min compared with native enzyme TAAUM with 12 min
50
-
purified enzyme, 10 mM Ca2+, 8 h 61.9% activity remaining. Without Ca2+, the enzyme loses 50% and 100% activity within 40 min and 120 min, respectively
50
-
purified enzyme, 70% activity remaining after 42 h
50
-
loss of 20%activity after 60 min
50
-
pH 8.5, 20 mM Tris-HCl buffer, in absence of CaCl2, 68% loss of activity, stable in presence of 0.2 mM CaCl2
50
-
no loss of activity after 15 min
50
-
80% loss of activity after 30 min
50
-
half-life is less than 3 min
50
-
30 min, purified enzyme, stable
50
moderate thermostability, half-life of 94 min at 50°C, rapid deactivation with a half-life of 7 min at 70°C, analyzed at pH 6 and temperatures between 30°C to 70°C, residual activity measured in intervals of 10 min
50
-
30 min, not stable above 50°C
50
-
1 h, less than 5% loss of activity
50
Halalkalibacterium halodurans
-
30 min, 58% loss of activity, alpha-amylase II
50
Halalkalibacterium halodurans
-
30 min, less than 5% loss of activity, alpha-amylase I
50
up to more than 60% relative activity, incubated for 30 min
50
-
pH 7.0, half-life: 10.1 h
50
-
30 min, loss of 62% activity of purified alpha-amylase I
50
-
pH 5.0, 30 min, about 20% loss of activity
50
half-life of free enzyme is 23 h, of immobilized enzyme 28 h
50
-
purified enzyme, half-life is 300 min
50
-
30% loss of activity after 1 h
50
-
30 min, inactivation
50
-
no loss of activity after 1 h
50
-
in absence of substrate stable for 1 h, in presence of substrate fully stable
50
-
pH 7.0, 10 min, stable
50
-
pH 8.0, 10 min, stable below
50
purified recombinant His-tagged enzyme, 60% activity remaining
50
purified recombinant His-tagged enzyme, inactivation after 10 min incubation
50
-
stable for 10 min in absence of Ca2+
50
-
10% loss of activity after 1 h
50
-
60 min, purified enzyme, 90% remaining activity
50
-
in the presence of 1% (w/v) potato starch the thermostability is enhanced above 50°C
50
-
at pH 6.0-7.5 stable for at least 20 h without substrate and Ca2+, incubation at pH 8.0 under the same conditions results in 40% decrease in activity
50
-
stable for more than 7 h
50
-
32% and 94% loss of activity after 2 h and 18 h, respectively
50
-
purified enzyme, 1 h, completely stable up to
50
-
almost complete loss of activity after 30 min, approx. 30% loss of activity in the presence of 5 mM CaCl2
50
-
30 min, purified enzyme, stable
50
-
purified enzyme, stable up to
50
-
half-life after 2 h incubation
50 - 70
activity of purified recombinant HaAmy1 when carried out under standard assay conditions is retained at 50°C incubation while decreased by 70% when incubated at 70°C
50 - 70
activity of purified recombinant HaAmy2 when carried out under standard assay conditions is reduced by 15% at 50°C incubation while decreased by 70% when incubated at 70°C
55
30 min, unstable above
55
-
t1/2 inact of the native enzyme TAAUM is 4 min, of the modified enzyme TAAMOD 30 min
55
-
1 h, purified isozyme BAA, inactivation in presence of Ca2+, 1.6% residual activity in absence of Ca2+
55
-
10 min, isozymes RBSA-1 and BSA-2, stable up to
55
-
30 min, about 80% loss of the activity of isoenzymes A and B, complete inactivation after 90 min
55
-
pH 5.0, 30 min, about 60% loss of activity
55
-
almost complete loss of activity after 1 h
55
-
approx. 50% loss of activity after 15 min, approx. 75% loss of activity after 120 min
55
-
20 min, 67% loss of activity, 20% loss of activity in presence of 2 mM CaCl2 or 0.5 mg bovine serum albumin
55
-
50% loss of activity after 25 min
55
-
30 min, 82% loss of activity
55
-
purified recombinant enzyme, 1 h, 90% activity remaining
55
-
20% of maximal activity after 30 min pre-incubation in the absence of a substrate, but the enzyme is stable during short time assay for 30 min
55
5 min, complete loss of activity
60
-
half-life: 5 days
60
-
larvaeal alpha-amylase maintains 34.6% activity after 5 min, and 23% after 60 min
60
-
purified enzyme, 30% glycerol, 85% activity remaining at 60°C after 2 h, 93% after 1 h. Without glycerol, the enzyme loses about 30% activity after 2 h
60
-
10 min, 96% loss of activity in absence of Ca2+, 10% loss of activity in presence of 0.01 M CaCl2
60
purified enzyme, pH 5.0, over 70% activity remaining after 30 min
60
-
15 min, retains about 90% of its original activity
60
-
18% loss of activity after 10 min, 64% loss of activity after 60 min
60
-
t1/2 inact of the native enzyme TAAUM is 1 min, of the modified enzyme TAAMOD 6 min
60
-
purified enzyme, without Ca2+, 50% activity remaining after 10 min, inactivation after 30 min
60
-
half-life: 164.2 min for enzyme immobilized in calcium alginate gel beads, 26.2 min for soluble enzyme
60
-
in the absence of CaCl2, the enzyme is stable up to 25 min retaining 65% of the activity. In the presence of 5 mM CaCl2 90% of the activity retained after 25 min incubation at 60°C
60
AmyQ remains stable at 60°C for 30 min
60
-
purified enzyme, 95% activity remaining after 42 h
60
-
30 min, whole cells, the amylase activity is completely stable
60
-
3 h, in absence of substrate, 9% loss of activity
60
-
20 min, recombinant enzyme, complete loss of activity, Ca2+, 0.5 mM, and Na+, 12.5 mM, completely protect from thermoinactivation
60
-
pH 8.5, 20 mM Tris-HCl buffer, in absence of CaCl2, 97% loss of activity, 35% loss of activity in presence of 0.1 mM CaCl2
60
-
3% loss of activity after 15 min
60
-
purified enzyme, 30 min, completely stable
60
-
60 min, soluble enzyme loses 73% of its activity, enzyme immobilized on aminoalkylsilane-alumina loses 29% of its activity, enzyme immobilized on DEAE-cellulose loses 23% of its activity, enzyme immobilized on chitin loses 2% of its activity, enzyme immobilized on polyacrylamide loses 12% of its activity
60
-
5 min, unstable above
60
-
10 min, isozyme RBLA, stable up to
60
-
30 min, complete inactivation
60
-
30 min, whole cells, the amylase activity is completely stable
60
-
1 h, complete inactivation in absence of substrate, less than 10% inactivation in presence of soluble starch. In presence of Ca2+ and Sr2+, Amy-FC1 retains full activity after 1 h and more than 80% activity after 5 h
60
-
pH 7.0, half-life: 0.88 h
60
-
1 h, 25% loss of activity
60
-
fully active after preincubation at 60°C in the presence of soluble starch. In the absence of starch AmyB is inactivated rapidly after 15 min of preincubation
60
-
30 min, loss of 78% activity of purified alpha-amylase I
60
-
pH 5.0, 30 min, complete loss of activity
60
-
10 min, 40% loss of activity
60
half-life of free enzyme is 27 h, of immobilized enzyme 31 h
60
-
purified enzyme, half-life is 720 min
60
-
50% loss of activity after 10 min
60
-
50% loss of activity after 12 min, no loss of activity after 1 h in the presence of 1% starch
60
-
half-life 12 min in absence of substrate
60
purified recombinant His-tagged enzyme, 10% activity remaining
60
-
30 min, complete loss of activity
60
-
10% loss of activity in presence of 0.00125 M Ca2+, 86% loss of activity without Ca2+
60
-
40% loss of activity after 1 h
60
-
purified recombinant enzyme, 1 h, 50% activity remaining
60
-
more than 75-85% if the activity is lost
60
-
approx. 50% loss of activity after 30 min in the presence of 2% starch, approx. 85% loss of activity after 30 min in the absence of starch
60
-
pH 5.0, 10 mM Ca2+, 120 min, stable. Inactivation without Ca2+
60
purified recombinant enzyme, 3 h, 70% activity remaining
60
purified recombinant enzyme, 3 h, 75% activity remaining
60
Thermomonospora vulgaris
-
60 min, 50% loss of activity
60
-
purified recombinant enzyme, 30 min, 70% activity remaining
60
-
purified enzyme, 1 h, about 80% activity remaining
60
-
approx. 65% loss of activity in the presence of 5 mM CaCl2
60 - 70
recombinant enzyme, stable up to in absence of Ca2+
60 - 70
-
30 min, no loss of activity
60 - 70
thermal inactivation occurs when the protein is incubated at 60-70°C for 30 min
63
-
pH 7.4, complete inactivation within 8 min, half-life: 165 min. The soluble starch increases the half-life of the purified amylase from 1.65 min to 8.98 min at 63°C
63
-
T50-value at pH 4.5, 5 mM CaCl2, alpha-amylase PA
63
-
Tm value, the maximum thermal stability for AmyB and DELTAAmyB, lacking the N-domain are obtained at pH above 6.0 and above 3.0 M NaCl
65
-
midpoint of thermal inactivation for enzyme immobilized in calcium alginate beads
65
-
purified enzyme, stable up to
65
-
15 min, 0.1 M sodium acetate-HCl buffer
65
-
5 min, 95% loss of activity
65
-
wild-type, 60% loss of activity after 120 min, AmyADelta mutant, complete loss of activity after 120 min
65
-
stable in absence of substrates and Ca2+ for at least 2 h
65
-
rapid inactivation below pH 7, stable in presence of bovine serum albumin
70
-
-
70
-
pH 2.0, 30 min, in absence of substrate, 73% of the activity remains
70
-
muscle alpha-amylase, 50% loss of activity, intestine alpha-amylase, 90% loss of activity
70
purified enzyme, pH 5.0, over 70% activity remaining after 15 min
70
-
15 min, 73% loss of activity
70
-
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 44 min, of recombinant wild-type Ba-amy 25 min
70
-
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, T1/2 is 40 min
70
-
wild-type, 75% of initial activity after 80 min, mutant Q67H after 185 min, and mutant P407H 125 min of incubation, respectively
70
-
purified enzyme, 80% activity remaining after 42 h
70
-
30 min, whole cells, 85% amylase activity is remaining
70
-
3 h, in absence of substrate, 21% loss of activity
70
30 min, whole cells, the amylase activity is completely stable
70
-
pH 2, 10 min, 40% loss of activity, 94% loss of activity after 30 min
70
-
8% loss of activity after 15 min
70
-
approx. 40% loss of activity after 30 min
70
-
t1/2 of N- and C-terminally truncated alpha-amylase is 14 min, t1/2 of the E219A mutant and the E219D mutant of N- and C-terminally truncated alpha-amylase is 5 min
70
-
30 min, whole cells, the amylase activity is completely stable
70
-
30 min, whole cells, 85% amylase activity is remaining
70
-
purified native enzyme, 40% activity is retained after 2 h, 20% after 5 h in absence of substrate, while in presence of 0.1% starch substrate, over 80% activity is retained for 8 h
70
-
1 h, in presence of Ca2+, 92% remaining activity
70
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 44 min, of recombinant wild-type Gt-amy 238 min
70
purified recombinant chimeric acidic alpha-amylase Ba-Gt-amy, T1/2 is 40 min
70
-
pH 7.0, half-life: 7.2 min
70
-
1 h, 31% loss of activity
70
-
10 min, 98% loss of activity
70
half-life of free enzyme is 24 h, of immobilized enzyme 38 h
70
-
purified enzyme, half-life is 1080 min
70
-
10 min, 70% loss of activity, complete inactivation after 40 min
70
-
complete inactivation
70
-
15 min, chimeric enzyme, 45% loss of activity
70
-
10 min, in absence of substrate, stable
70
-
15 min, in presence of 3 mM Ca2+, 36% loss of activity of the enzyme from shoot, 23% loss of activity of the enzyme from cotyledons. 15 min, without Ca2+, 98% loss of activity of the enzyme from shoot, 99% loss of activity of the enzyme from cotyledons
70
purified enzyme, 5 mM Ca2+, completely stable for 14 h, loss of 50% activity after 19 h, inactivation after 23 h
70
purified enzyme, without Ca2+, completely stable for 10 h, loss of 50% activity after 16 h, inactivation after 19 h
70
-
purified recombinant enzyme, 30 min, 50% activity remaining
70
-
almost complete loss of activity in the presence of 5 mM CaCl2
70
-
30 min, loss of 80% activity
70
-
more than 60% of the activity is lost within the first 30 min
70
-
1 h, 80% loss of activity
71
-
pH 7.4, complete inactivation within 2 min, half-life: 24 s
71
-
T50-value at pH 6.0, without CaCl2, alpha-amylase PA
75
-
pH 3.5, 30 min, 10% loss of activity
75
-
wild-type, half-life 125 min, mutant Q67H, 145 min, and mutant P407H, 185 min
75
-
30 min, 18% loss of activity
75
-
approx. 75% loss of activity after 15 min and 120 min, respectively
75
-
t1/2 values of wild-type AMY121, mutant Y187E, mutant K205L, and mutant Y187E/K205L are 7.04, 7.29, 31.08, and 26.16 min, respectively
78
-
half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min
78
-
half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min
78
-
5 min, chimeric enzyme, about 90% loss of activity
80
-
-
80
-
pH 5.0, 30 min, stable
80
-
larvaeal alpha-amylase maintains 14% activity after 5 min, and 6% after 60 min
80
-
20 min, 64% loss of activity
80
-
15 min, complete inactivation
80
-
about 70% of activity are kept after 70 min
80
-
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 30 min, of recombinant wild-type Ba-amy 15 min
80
-
96% loss of activity in the absence of additive, 93%, 80%, 86% and 91% loss of activity in the presence of 20% trehalose, sorbitol, mannitol and glycerol, respectively
80
-
approx. 50% loss of activity after 60 min, complete loss of activity after 100 min
80
-
purified enzyme, 75% activity remaining after 42 h
80
-
30 min, whole cells, 30% amylase activity is remaining
80
-
5 min, 55% loss of activity
80
-
90 min, in absence of substrate, 29% loss of activity
80
-
30% loss of activity in the absence of additive, 21%, 5%, 7% and 10% loss of activity in the presence of 20% trehalose, sorbitol, mannitol and glycerol, respectively
80
30 min, whole cells, 90% amylase activity is remaining
80
-
purified native enzyme, 10 min, 70% activity remaining
80
recombinant enzyme, stable up to in presence of Ca2+
80
-
complete inactivation after 60 min in presence of 0.1 mM Ca2+
80
-
11% loss of activity after 15 min
80
-
30 min, whole cells, 80% amylase activity is remaining
80
-
30 min, whole cells, 60% amylase activity is remaining
80
-
purified recombinant His6-tagged mutant Gs4j-amyA N-terminally fused to OmpA signal peptide, half-life (t1/2) is 4.25 h
80
-
purified native enzyme, 15% activity is retained after 1 h, 10% after 2 h in absence of substrate, while in presence of 0.1% starch substrate, about 30% activity is retained for 4-8 h, 20% remaining after 9 h
80
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 30 min
80
-
pH 7.0, half-life: 4.1 min
80
-
after preincubation in the presence of starch, activity falls off linearly with time to reach 10% after 2 h, with a half-life of above 1 h at 80°C. In the absence of starch AmyB is inactivated rapidly after 15 min of preincubation
80
half-life of free enzyme is 20 h, of immobilized enzyme 24 h
80
-
purified enzyme, half-life is 540 min
80
-
90% loss of activity after 10 min
80
purified enzyme, 5 mM Ca2+, completely stable for 8 h, loss of 50% activity after 13 h, inactivation after 16 h
80
purified enzyme, without Ca2+, completely stable for 6 h, loss of 50% activity after 10 h, inactivation after 13 h
80
pH 6, half-life: 30 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 7581 min
80
-
stable at pH 5.0-7.0 for 1 h
80
Thermomonospora vulgaris
-
5 min, complete inactivation
80
Thermomonospora vulgaris
-
complete inactivation after a few min
80
-
purified recombinant enzyme, 30 min, 35% activity remaining
80
-
5 min, complete inactivation
80
-
purified enzyme, 1 h, about 70% activity remaining
80
-
complete loss of activity after 30 min
80
-
50% loss of activity after 30 min
80
-
20 min, 84% loss of activity
85
-
purified enzyme, 25% activity remaining after 42 h
85
-
60 min, with the exception of the enzyme from strain NCIB 9668, more than 98% of the activity is retained
85
-
complete loss of activity after 5 min
85
-
thermal inactivation, first-order kinetics with rate constant equal to 0.0063/min
85
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, completely stable for 120 min
85
-
30% loss of activity after 10 min, complete inactivation after 40 min, about 40% loss of activity after 2 h in presence of 2 mM Ca2+
85
the wild-type AmyA and the mutants are stable for more thant 30 h at 85°C. No loss of activity is observed
90
-
-
90
-
pH 4.5, 30 min, in absence of substrate, more than 90% of the activity remains
90
-
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 15 min, of recombinant wild-type Ba-amy 5 min
90
-
30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263
90
-
half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34
90
-
no loss of activity in the presence of 50% toluene or n-octane
90
-
30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263
90
-
half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34
90
approx. 25% loss of activity after 150 min, approx. 60% loss of activity after 400 min
90
-
no loss of activity in the presence of 50% toluene or n-octane
90
-
pH 5.5, 1 h, 50% inactivation, alpha-amylase PA
90
-
purified native enzyme, 10 min, 10% activity remaining
90
-
14% loss of activity after 15 min
90
-
purified enzyme, 30 min, 50% activity remaining
90
-
pH 9.0, purified enzyme, loss of 35% activity after 10 min, and of 80% after 30 min
90
-
pH 8.0, in presence of 5 mM CaCl2, half-life: 20 min
90
-
pH 6.0, 17% loss of activity after 6 min, 80% loss of activity after 30 min
90
-
half-life in presence of 0.05 mM Ca2+ is 4.3 min. Half-life in presence of 5 mM Ca2+ is 44 min. Half-life in presence of 10% dextrose and 5 mM Ca2+ at pH 5.35 is 51 min. Half-life in presence of 10% maltose and 5 mM Ca2+ at pH 5.35 is 55 min. Half-life in presence of 10% maltotriose and 5 mM Ca2+ at pH 5.35 is 166 min. Half-life in presence of 10% Maltrin M-105 and 5 mM Ca2+ at pH 5.35 is 342 min
90
-
50% loss of activity after 50 min at pH 6.5
90
half-life of purified recombinant chimeric mutant Ba-Gt-amy is 15 min
90
-
1 h, more than 60% loss of activity
90
-
purified enzyme, half-life is 300 min
90
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 15-20% activity within 120 min
90
60 min, about 10% loss of activity, thermostability is enhanced in the presence of 2 mM Ca2+
90
-
partially purified recombinant enzyme, half-life is 11 h, at pH 5.6 in 0.05 M acetate buffer
90
-
stable for 4 h, recombinant protein in Xanthomonas campestris shows similar thermostability as the native Pyrococcus woesei enzyme
90
purified enzyme, 5 mM Ca2+, completely stable for 5 h, loss of 50% activity after 8 h, inactivation after 10 h
90
purified enzyme, without Ca2+, completely stable for 3 h, loss of 50% activity after 6 h, inactivation after 8 h
90
at pH 6, half-life: 10 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 153 min. The thermostability is not enhanced by the addition of Zn2+ or other divalent metals, irrespective of the concentration
90
-
half-life of the enzyme 5 h, at pH 5.0-7.0 stable for 1 h
90
-
5 min, 40% loss of activity, complete inactivation after 60 min
90
-
6 h, 80% remaining activity
90
-
purified enzyme, 1 h, about 20% activity remaining
90
-
60 min, 6% loss of activity
95
-
approx. 50% loss of activity after 2 min, complete loss of activity after 20 min
95
-
approx. 50% loss of activity after 15 min, approx. 80% loss of activity after 15 min
95
-
covalent binding of thermostable alpha-amylase on calcium alginate provides a 80% activity based on the immobilized protein for the first cycle and hydrolyzes a total of 51 mg starch/s/mg protein after seven cycles at 95°C
95
-
10 min, pH 9.0, purified enzyme, loss of 60% activity
95
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 25% activity within 120 min
98
half-life: 13 min
98
-
8 h, about 70% loss of activity
additional information
with calcium ions, the values of Topt, T50, t1/2, Tm and DELTAH in enzyme AGXA are significantly higher than those of enzyme AGXA without calcium ions, showing calcium ions have stabilizing effects on alpha-amylase structure with the increased temperature. AGXA undergoes thermal denaturation via a two-state irreversible unfolding process. AGXA without calcium ions exhibits two transition states upon unfolding, including alpha-helical contents increasing, and the transition from alpha-helices to beta-sheet structures, which is obviously different in AGXA with Ca2+ ions, and up to 4 Ca2+ ions are located on the interdomain or intradomain regions according to the modeling structure
additional information
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substrate is required for stability at high temperatures
additional information
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analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
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determination of thermal denaturation kinetics of the recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy, overview
additional information
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analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
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thermal unfolding kinetics and thermal stability, overview
additional information
-
-
additional information
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Ca2+ and Na+ stabilize at higher reaction temperatures
additional information
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analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
thermal unfolding kinetics and thermal stability, overview
additional information
Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C
additional information
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Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C
additional information
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profile, overview
additional information
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analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
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in the presence of substrate, thermostability of the alpha-amylase is increased
additional information
-
-
additional information
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the enzyme is protected from thermal denaturation above 55°C by Ca2+ and by protein
additional information
determination of thermal denaturation kinetics of the recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy, overview
additional information
-
determination of thermal denaturation kinetics of the recombinant His-tagged chimeric acidic alpha-amylase Ba-Gt-amy, overview
additional information
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AmyA forms unique reversiblepoly-dispersed oligomers that show high thermal stability
additional information
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the temperature stability of AmyB and DELTAAmyB, lacking the N-domain are strongly influenced by NaCl concentration, shown by an increasing melting temperature with increased NaCl concentrations up to 4-4.5 M
additional information
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isoenzyme Amy1A shows the highest thermostability, mutant enzyme N240Q of isoenzyme Amy1A shows almost identical thermostability to those of Amy3D and Amy1A/3D
additional information
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enzyme immobilization on Celite increases the thermal stability
additional information
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partial protection from heat inactivation by Ca2+, EGTA increases heat inactivation
additional information
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the process of heat denaturation is complex and includes at least three stages, indicating that the protein structure consists of three domains, heat denaturation is irreversible
additional information
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highly thermostable recombinant enzyme
additional information
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thermostable enzyme
additional information
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reversible unfolding even at high temperature
additional information
the purfied enzyme is moderately thermostable
additional information
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analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
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high thermostability is not substrate dependent
additional information
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stabilizes at 85°C, fails to protect against inactivation at 95°C
additional information
Thermomonospora vulgaris
-
-
additional information
Thermomonospora vulgaris
-
bovine serum albumin protects from thermal denaturation at 60°C, no protection at 80°C
additional information
-
-
additional information
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Ca2+ protects against inactivation at 60°C
additional information
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at 65°C the enzyme is nearly 8times more stable in presence of Ca2+
additional information
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addition of hydrophobic interactions and saltbridges can increase the thermostability of variants Y187E and K205L
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