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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase
for references in articles please use BRENDA:EC3.2.1.3
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.3 glucan 1,4-alpha-glucosidase
IUBMB Comments
Most forms of the enzyme can also rapidly hydrolyse (1→6)-α-D-glucosidic bonds when the next bond in the sequence is (1→4), and some preparations of this enzyme hydrolyse both (1→6)- and (1→3)-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes with configuration-inverting activity that act on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions but prefers oligosaccharides and retains the anomeric configuration of the release glucosyl units.
The enzyme appears in viruses and cellular organisms
- 3.2.1.3
- aspergillus
- niger
- glycogen
- alpha-amylase
- maltose
- corn
- awamori
-
amylolytic
- pompe
- sucrase
- myopathy
-
saccharification
- rhizopus
- lactase
-
brush
- sucrase-isomaltase
- acarbose
- dextrin
- glycogenosis
- maltotriose
- amylopectin
- flour
- amylases
-
starch-binding
- isomaltase
-
infantile
- maltodextrins
- occidentalis
- bran
- disaccharidase
- food industry
- pullulanase
-
liquefaction
- beta-cyclodextrins
-
debranching
- beta-amylase
-
carbohydrases
-
3.2.1.20
- cassava
- maltooligosaccharides
- trehalase
-
saccharify
-
bioethanol
- medicine
- industry
- energy production
- paper production
-
glucanotransferase
- nutrition
- maltoheptaose
- analysis
- maltotetraose
- biotechnology
- cgtase
- biofuel production
- isoamylase
-
liquefied
- 1-deoxynojirimycin
-
starchy
- synthesis
Reaction Schemes
showSynonyms
glucoamylase, amyloglucosidase, acid maltase, maltase-glucoamylase, lysosomal alpha-glucosidase, maltase glucoamylase, gamma-amylase, glucose amylase, gam-1, glucoamylase p, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucohydrolase
acid maltase
-
-
-
-
alpha-1,4-D-glucan glucohydrolase
alpha-1,4-glucan glucohydrolase
AmyC
AmyD
amyloglucosidase
APGA1
AtriGA15A
exo-1,4-alpha-glucosidase
GA
GA1
GA2
GAI
-
-
-
-
GAII
GAM
gamma-amylase
GHF15 glucoamylase
Gla1
GlaA
GLL1
Glu-1.1
Glu-A
Glu1
GlucaM
Glucan 1,4-alpha-glucosidase
glucoamylase
glucoamylase G1
glucose amylase
-
-
-
-
lysosomal alpha-glucosidase
-
-
-
-
maltase-glucoamylase
maltooligosaccharide-metabolizing enzyme
Meiotic expression upregulated protein 17
-
-
-
-
MGAM
PDE_05527
PoGA
PoGA15A
PoxGA15A
raw starch-degrading enzyme
raw starch-degrading glucoamylase
RSDE
RSDG
SBD
Sde_0600
sdgA
Sta1
starch-digesting glucoamylase
tGA
TmGLA
TmGlu1
additional information
1,4-alpha-D-glucan glucohydrolase
-
-
-
-
alpha-1,4-glucan glucohydrolase
-
-
-
-
amyloglucosidase
-
-
-
-
exo-1,4-alpha-glucosidase
-
-
-
-
GAII
-
-
-
-
gamma-amylase
-
-
-
-
Glucan 1,4-alpha-glucosidase
-
-
-
-
glucoamylase
-
-
-
-
glucoamylase
-
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 15
additional information
the enzyme belongs to the glycosyl hydrolase family 31
additional information
-
the enzyme belongs to the family 15 glycoside hydrolase
additional information
-
the enzyme belongs to the glycohydrolase family 21
additional information
the enzyme belongs to the carbohydrate-binding module family 21
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
-
-
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
reaction mechanism depends on the substrate, i.e. hydrolysis or transglycosylation, overview
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
Mucor rouxians
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
structure-function relationship, ligand binding
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
mode of action
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
mode of action
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
Aspergillus neotritici CGMCC 3.15694.3.2
-
-
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
exohydrolysis
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
glycogen degradation II
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucohydrolase
Most forms of the enzyme can also rapidly hydrolyse (1->6)-alpha-D-glucosidic bonds when the next bond in the sequence is (1->4), and some preparations of this enzyme hydrolyse both (1->6)- and (1->3)-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes with configuration-inverting activity that act on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions but prefers oligosaccharides and retains the anomeric configuration of the release glucosyl units.
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CAS REGISTRY NUMBER
COMMENTARY
9032-08-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-glucoside + H2O
?
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
D-glucose + 4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-alpha-trehalose + H2O
alpha-D-glucose
-
Substrates: -
Products: -
Products: -
?
amylose DP 18 + H2O
beta-D-glucose + amylose DP 17
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
beta-cyclodextrin + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
corn starch + H2O
beta-D-glucose + ?
-
Substrates: 12% of the activity with maltose
Products: -
Products: -
?
curcumin + beta-D-glucose
curcuminyl bis-alpha-D-glucoside + 6-O-curcuminyl bis-D-glucose + curcuminyl bis-beta-D-glucoside
-
Substrates: i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
Products: -
Products: -
?
curcumin + D-mannitol
1-O-curcuminyl bis-D-mannitol
-
Substrates: i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
Products: -
Products: -
?
curcumin + D-mannose
curcuminyl bis-alpha-D-mannoside + curcuminyl bis-maltoside + 6-O-curcuminyl bis-maltose + 6''-O-curcuminyl bis-maltose
-
Substrates: i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
Products: -
Products: -
?
curcumin + sucrose
1-O-curcuminyl bis-sucrose + 6''-O-curcuminyl bis-sucrose + 6-O-curcuminyl bis-sucrose
-
Substrates: i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
Products: -
Products: -
?
curcumin-bis-alpha-D-glucoside + H2O
curcumin + beta-D-glucose
-
Substrates: the enzyme also performs glucosylation of curcumin-bis-alpha-D-glucoside in the reverse reaction
Products: -
Products: -
r
D-malto-oligosaccharides + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
eugenol + beta-D-glucose
eugenyl alpha-D-glucoside + 6-O-eugenyl D-glucose + eugenyl beta-D-glucoside
-
Substrates: i.e. 4-allyl-2-methoxy phenol
Products: -
Products: -
?
eugenol + D-mannitol
1-O-eugenyl mannitol
-
Substrates: i.e. 4-allyl-2-methoxy phenol
Products: -
Products: -
?
eugenol + D-mannose
eugenyl alpha-D-mannoside
-
Substrates: i.e. 4-allyl-2-methoxy phenol
Products: -
Products: -
?
eugenol + maltose
eugenyl maltoside + 6-O-eugenyl maltose + 6''-O-eugenyl maltose
-
Substrates: -
Products: -
Products: -
?
eugenol + sucrose
1-O-eugenyl sucrose + 6-O-eugenyl sucrose + 6''-O-eugenyl sucrose
-
Substrates: i.e. 4-allyl-2-methoxy phenol
Products: -
Products: -
?
gamma-cyclodextrin + H2O
gamma-cyclodextrin + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
guaiacol-alpha-D-glucoside + H2O
guaiacol + beta-D-glucose
-
Substrates: the enzyme also performs glucosylation of guaiacol-alpha-D-glucoside in the reverse reaction
Products: -
Products: -
r
isomaltose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltodextrin + H2O
beta-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltodextrin + H2O
D-glucose + ?
-
Substrates: from corn mash
Products: -
Products: -
?
maltodextrin + H2O
maltodextrin + beta-D-glucose
-
Substrates: during incubation 5-(hydroxymethyl)-2-furfuraldehyde is released, resulting in a glycated enzyme
Products: -
Products: -
?
maltoheptaose + 6 H2O
7 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
maltohexaose + 5 H2O
6 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
maltononaose + H2O
maltooctaose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltooctaose + H2O
maltoheptaose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltooligomers + H2O
? + beta-D-glucose
Substrates: substrate specificity
Products: -
Products: -
r
maltopentadecaose + H2O
maltotetradecaose + beta-D-glucose
-
Substrates: low activity
Products: -
Products: -
?
maltopentaose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
maltotetraose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + D-glucose
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
pullulan + H2O
beta-D-glucose + ?
-
Substrates: 182% of activity with soluble starch
Products: -
Products: -
?
pullulan + H2O
pullulan + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
short-chain amylose + H2O
beta-D-glucose + short-chain amylose
-
Substrates: -
Products: -
Products: -
?
4 glucose
glucooligosaccharide + 3 H2O
-
Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
Products: -
Products: -
r
4 glucose
glucooligosaccharide + 3 H2O
-
Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
Products: -
Products: -
r
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 12% of activity with starch
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 6% of the activity with maltose
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Aspergillus japonicus Saito
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
alpha-cyclodextrin + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
alpha-cyclodextrin + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
glucose + ?
-
Substrates: no activity
Products: -
Products: -
?
alpha-cyclodextrin + H2O
glucose + ?
-
Substrates: 6% of the activity with maltose
Products: -
Products: -
?
amylopectin + H2O
?
Substrates: from potato
Products: -
Products: -
?
amylopectin + H2O
?
Substrates: from potato
Products: -
Products: -
?
amylopectin + H2O
?
-
Substrates: best substrate, from potatoes or corn
Products: -
Products: -
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
Substrates: preferred substrate
Products: -
Products: -
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose, best substrate
Products: -
Products: -
?
amylopectin + H2O
amylopectin + beta-D-glucose
Substrates: 94% of activity with amylose
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: 933% of activity with soluble starch
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: 104% of activity with soluble starch from potato
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: 100% of activity with soluble starch from potato
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: 18% of the activity with maltose
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
beta-D-glucose + ?
-
Substrates: 104% of activity with soluble starch from potato
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: 84% of the activity with starch
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: 85% of activity with starch
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: best substrate
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
Aspergillus japonicus Saito
-
Substrates: best substrate
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: high activity
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
Substrates: potato amylopectin
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
D-glucose + ?
-
Substrates: -
Products: beta-glucose
Products: beta-glucose
?
amylose + H2O
?
Substrates: from potato
Products: -
Products: -
?
amylose + H2O
amylose + beta-D-glucose
-
Substrates: low activity
Products: -
Products: -
?
amylose + H2O
amylose + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
amylose + H2O
amylose + beta-D-glucose
Substrates: preferred substrate
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: 187% of activity with soluble starch
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: 74% of activity with soluble starch from potato
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: 60% of activity with soluble starch from potato
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: 13% of activity with starch
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylose + H2O
beta-D-glucose + ?
-
Substrates: 63% of activity with soluble starch from potato
Products: -
Products: -
?
amylose + H2O
D-glucose + ?
Substrates: potato amylose type III
Products: -
Products: -
?
amylose + H2O
glucose + ?
-
Substrates: 61% of the activity with starch
Products: -
Products: -
?
amylose + H2O
glucose + ?
-
Substrates: 93% of the activity with starch
Products: -
Products: -
?
amylose + H2O
glucose + ?
-
Substrates: 31% of the activity with starch
Products: -
Products: -
?
amylose + H2O
glucose + ?
-
Substrates: -
Products: -
Products: -
?
amylose + H2O
glucose + ?
-
Substrates: short-chain
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
-
Substrates: 6% of the activity with maltose
Products: -
Products: -
?
dextrin + 6 H2O
7 beta-D-glucose
-
Substrates: 91% of activity with soluble starch from potato
Products: -
Products: -
?
dextrin + 6 H2O
7 beta-D-glucose
-
Substrates: 89% of activity with soluble starch from potato
Products: -
Products: -
?
dextrin + 6 H2O
7 beta-D-glucose
-
Substrates: 84% of activity with soluble starch from potato
Products: -
Products: -
?
dextrin + 6 H2O
7 D-glucose
-
Substrates: the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
Products: -
Products: -
?
dextrin + 6 H2O
7 D-glucose
-
Substrates: potato dextrin, the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
Products: -
Products: -
?
dextrin + 6 H2O
7 D-glucose
Substrates: a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose
Products: -
Products: -
?
dextrin + H2O
?
-
Substrates: beta-limit dextrin
Products: -
Products: -
?
glycogen + 3 H2O
4 beta-D-glucose
-
Substrates: 103% of activity with soluble starch from potato
Products: -
Products: -
?
glycogen + 3 H2O
4 beta-D-glucose
-
Substrates: 90% of activity with soluble starch from potato
Products: -
Products: -
?
glycogen + 3 H2O
4 beta-D-glucose
-
Substrates: 150% of activity with starch
Products: -
Products: -
?
glycogen + 3 H2O
4 beta-D-glucose
-
Substrates: 96% of activity with soluble starch from potato
Products: -
Products: -
?
glycogen + H2O
glucose + ?
-
Substrates: 82% of the activity with starch
Products: -
Products: -
?
glycogen + H2O
glucose + ?
-
Substrates: shellfish glycogen, sweet-corn phytoglycogen, skate liver glycogen, human muscle glycogen, rabbit muscle glycogen, cat liver glycogen, cat liver glycogen. Incomplete conversion to glucose in absence of alpha-amylase
Products: -
Products: -
?
glycogen + H2O
glucose + ?
-
Substrates: amylose A, n = 25 and amylose B, n = 130
Products: -
Products: -
?
glycogen + H2O
glucose + ?
-
Substrates: shellfish glycogen, sweet-corn phytoglycogen, skate liver glycogen, human muscle glycogen, rabbit muscle glycogen, cat liver glycogen, cat liver glycogen. Incomplete conversion to glucose in absence of alpha-amylase
Products: -
Products: -
?
glycogen + H2O
glucose + ?
-
Substrates: -
Products: beta-glucose
Products: beta-glucose
?
glycogen + H2O
glycogen + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
glycogen + H2O
glycogen + beta-D-glucose
Substrates: 87% of activity with amylose
Products: -
Products: -
?
isomaltose
isomaltooligosaccharide
-
Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
Products: -
Products: -
r
isomaltose
isomaltooligosaccharide
-
Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
Products: -
Products: -
r
isomaltose + H2O
glucose
-
Substrates: -
Products: -
Products: -
?
isomaltose + H2O
glucose
-
Substrates: 10% of the activity with starch
Products: -
Products: -
?
maltodextrin + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
maltohexaose + D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
?
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharide + H2O
beta-D-glucose
-
Substrates: 49% of activity with soluble starch from potato
Products: -
Products: -
?
maltooligosaccharide + H2O
beta-D-glucose
-
Substrates: 55% of activity with soluble starch from potato
Products: -
Products: -
?
maltooligosaccharide + H2O
beta-D-glucose
-
Substrates: 54% of activity with soluble starch from potato
Products: -
Products: -
?
maltooligosaccharides + H2O
maltooligosaccharides + beta-D-glucose
-
Substrates: high activity
Products: -
Products: -
?
maltooligosaccharides + H2O
maltooligosaccharides + beta-D-glucose
-
Substrates: high activity
Products: -
Products: -
?
maltopentaose + 4 H2O
5 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltopentaose + 4 H2O
5 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
?
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: low activity
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
Rhizopus arrhizus 99-880
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 glucose
-
Substrates: 19% of the activity with starch
Products: -
Products: -
?
maltose + H2O
2 glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 glucose
-
Substrates: 40% of the activity with starch
Products: -
Products: -
?
maltose + H2O
2 glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
2 glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: product analysis
Products: product analysis
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: product analysis
Products: product analysis
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: substrate of isozyme GA-II, no activity with isozyme GA-I
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: 17% of activity with soluble starch from potato
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: 2% of activity with soluble starch from potato
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
Substrates: -
Products: -
Products: -
r
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
Substrates: 14% of activity with amylose
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: 24% of activity with soluble starch from potato
Products: -
Products: -
?
maltose + H2O
beta-D-glucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltose + H2O
D-glucose + ?
-
Substrates: assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
Products: -
Products: -
?
maltotetraose + 3 H2O
4 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltotetraose + 3 H2O
4 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
?
-
Substrates: 60% of the activity with maltose
Products: -
Products: -
?
maltotetraose + H2O
?
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: low activity
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
Rhizopus arrhizus 99-880
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + 2 H2O
3 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltotriose + 2 H2O
3 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltotriose + 2 H2O
3 beta-D-glucose
Substrates: -
Products: -
Products: -
?
maltotriose + 2 H2O
3 beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose
Products: -
Products: -
?
maltotriose + H2O
maltose + beta-D-glucose
Substrates: exoglycosidic hydrolysis of terminal glucose in forward reaction, preferred substrate, synthesis of isomaltose from beta-D-glucose in the reverse reaction with low activity
Products: anomeric product configuration analysis at 80°C
Products: anomeric product configuration analysis at 80°C
r
maltotriose + H2O
maltose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + beta-D-glucose
Substrates: 40% of activity with amylose
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: 47% of the activity with starch
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: 46% of the activity with starch
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: 68% of the activity with starch
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
maltose + glucose
-
Substrates: hydrolysis by a multi-chain mechanism
Products: -
Products: -
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
Substrates: -
Products: -
Products: -
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
Substrates: no activity
Products: -
Products: -
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
Substrates: 5% of the activity with maltose
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Cephalosporium eichhorniae
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Endomycopsis fibuligera
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Schwanniomyces castellii
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
Substrates: -
Products: -
Products: -
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
Substrates: -
Products: -
Products: -
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
Substrates: -
Products: -
Products: -
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
Substrates: -
Products: -
Products: -
?
potato starch + H2O
beta-D-glucose + ?
-
Substrates: 20% of the activity with maltose
Products: -
Products: -
?
pullulan + H2O
?
-
Substrates: 52% of the activity with starch
Products: -
Products: -
?
pullulan + H2O
?
Substrates: low activity
Products: -
Products: -
?
pullulan + H2O
?
-
Substrates: 1.46% of the activity with starch
Products: -
Products: -
?
raw potato starch + H2O
?
Substrates: -
Products: -
Products: -
?
raw starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
Substrates: -
Products: -
Products: -
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
Substrates: -
Products: -
Products: -
?
starch + H2O
?
-
Substrates: soluble starch, which is the best substrate, and raw starch from cassava, potato, and corn
Products: -
Products: -
?
starch + H2O
?
Substrates: best substrate, soluble starch and gelatinized raw sago starch
Products: -
Products: -
?
starch + H2O
?
Aspergillus flavus NSH9
Substrates: best substrate, soluble starch and gelatinized raw sago starch
Products: -
Products: -
?
starch + H2O
?
-
Substrates: corn starch, potato starch, hydrolyzed potato starch, and rice starch
Products: -
Products: -
?
starch + H2O
?
Aspergillus japonicus Saito
-
Substrates: corn starch, potato starch, hydrolyzed potato starch, and rice starch
Products: -
Products: -
?
starch + H2O
?
Substrates: standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
Products: -
Products: -
?
starch + H2O
?
Aspergillus neotritici CGMCC 3.15694.3.2
Substrates: standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
Products: -
Products: -
?
starch + H2O
?
Substrates: standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
Products: -
Products: -
?
starch + H2O
?
Substrates: soluble starch and raw starch from sweet potato and corn
Products: -
Products: -
?
starch + H2O
?
Corallococcus coralloides CCTCC M2012528
Substrates: soluble starch and raw starch from sweet potato and corn
Products: -
Products: -
?
starch + H2O
?
Substrates: soluble starch and raw starch from sweet potato and corn
Products: -
Products: -
?
starch + H2O
?
-
Substrates: recombinant N-terminal subunit of human small intestinal maltase-glucoamylase is used to explore digestion of native starches from different botanical sources, e.g. normal and waxy maize, wheat, potato, pea, banana, and tapioca starches, and high-amylose maize starch with 50-70% amylose, substrate specificity, overview
Products: -
Products: -
?
starch + H2O
?
Substrates: starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview
Products: -
Products: -
?
starch + H2O
?
Substrates: raw starch, different raw starch flours, e.g. raw cassava starch or raw potato starch, the enzyme also hydrolyzes soluble starch
Products: -
Products: -
?
starch + H2O
?
Penicillium oxalicum CGMCC 3.15650
Substrates: raw starch, different raw starch flours, e.g. raw cassava starch or raw potato starch, the enzyme also hydrolyzes soluble starch
Products: -
Products: -
?
starch + H2O
?
Penicillium oxalicum GXU20
Substrates: starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview
Products: -
Products: -
?
starch + H2O
?
-
Substrates: starch granules from various botanical sources: rice, wheat, potato, sweet potato, cassava, and maize
Products: -
Products: -
?
starch + H2O
?
-
Substrates: Paselli starch or soluble starch
Products: -
Products: -
?
starch + H2O
?
Substrates: soluble starch, and low activity with raw corn starch
Products: -
Products: -
?
starch + H2O
?
Tricholoma matsutake NBRC 30605
Substrates: soluble starch, and low activity with raw corn starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: activities with starch in descending order, wheat starch, rice starch, sago starch, potato starch, soluble starch, tapioca starch and corn starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Mucor rouxians
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Mucor rouxians
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: rice starch, 95% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: maize starch, 83% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: native starch from potato, 92% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: rice starch, 110% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: maize starch, 105% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: native starch from potato, 105% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: glucoamylase is an exo-amylolytic enzyme that cleaves alpha-1,4-linked and alpha-1,6-linked glucose from starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: -
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: soluble starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
Substrates: soluble starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: strongest activity with soluble starch
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: rice starch, 123% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: maize starch, 109% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: native starch from potato, 105% of activity with soluble starch from potato
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
Products: -
Products: -
?
starch + H2O
beta-D-glucose + ?
-
Substrates: the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: soluble and raw starch
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme hydrolyzes glucosidic bonds in amylase, amylopectin, and maltoligosaccharides
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: raw and cooked soluble starch from potato, no activity with corn starch and sweet potato starch
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: gelatinized and ungelatinized substrates: soluble, potato, sweet potato, and corn starch granules, determination of optimal substrate concentration, substrate specificity, overview
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: important industrial enzyme that removes the glucose units from the non-reducing chain-ends of starch and glycogen by hydrolyzing alpha-1,4 linkages consecutively
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: -
Products: sole end-product
Products: sole end-product
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose
Products: -
Products: -
?
starch + H2O
D-glucose + ?
Substrates: one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: soluble corn and wheat starch granules
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme preferentially hydrolyzes all the starch substrates, soluble and raw. High substrate specificity is demonstrated towards soluble starch
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme preferentially hydrolyzes all the starch substrates, soluble and raw. High substrate specificity is demonstrated towards soluble starch
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: soluble starch
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: raw starch and gelatinized starch
Products: -
Products: -
?
starch + H2O
glucose + ?
Agroathelia rolfsii AHU 9627
-
Substrates: raw starch and gelatinized starch
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: 300fold preference for the alpha-1,4-glucosidic linkage over the alpha-1,6-glucosidic linkage
Products: -
Products: -
?
starch + H2O
glucose + ?
Substrates: catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: with concentrated solutions of D-glucose, 10% w/v and 30% w/v, small amounts of isomaltose are produced as the sole reversion product
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: waxy-maize starch, waxy-sorghum starch, floridean starch. Incomplete conversion to glucose in absence of alpha-amylase
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: beta-glucose and maltooligosaccharides
Products: beta-glucose and maltooligosaccharides
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: wheat starch, potato starch, corn starch
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: wheat starch, potato starch, corn starch
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: -
Products: -
?
starch + H2O
glucose + ?
-
Substrates: soluble
Products: beta-glucose
Products: beta-glucose
?
starch + H2O
glucose + ?
Paecilomyces variotii AHU 9417
-
Substrates: soluble
Products: beta-glucose
Products: beta-glucose
?
starch + H2O
glucose + ?
-
Substrates: waxy-maize starch, waxy-sorghum starch, floridean starch. Incomplete conversion to glucose in absence of alpha-amylase
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme contains 7 subsites for substrate binding, subsite affinities
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble starch, raw rice starch, and raw wheat starch, the latter is the preferred substrate
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble starch, raw rice starch, and raw wheat starch, the latter is the preferred substrate
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the starch chain, substrates corn cobs, maize starch, soluble starch, and wheat bran
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: hydrolysis of solid-state starch from raw chestnut homogenate, composition, 30% of the raw chestnut is starch, overview
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme contains 7 subsites for substrate binding, subsite affinities
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble potato starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble potato starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme contains 7 subsites for substrate binding, subsite affinities
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme contains 7 subsites for substrate binding, subsite affinities
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme contains 7 subsites for substrate binding, subsite affinities
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: product analysis
Products: product analysis
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: product analysis
Products: product analysis
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble potato starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: 16times and 29times higher activity with soluble starch compared to wheat or corn starch granules, respectively
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: exoglycosidic hydrolysis of terminal glucose, high activity
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
Mucor rouxians
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: cooked corn starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: raw corn starch granules of different size, exoglycosidic hydrolysis of terminal glucose, determination of relation of granule surface area to adsorbed enzyme and activity including product liberation
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
Substrates: soluble starch
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the native enzyme shows low activity with raw starch due to a lack in starch binding domain
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble starch, very low activity
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: soluble starch, very low activity
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
starch + beta-D-glucose
-
Substrates: the enzyme is required for degradation of raw starch
Products: -
Products: -
?
sucrose + H2O
D-glucose + D-fructose
-
Substrates: 3.3% of carbohydrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high affinity for the branched polysaccharides. It can digest raw starch
Products: -
Products: -
?
additional information
?
-
Substrates: catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose
Products: -
Products: -
?
additional information
?
-
Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose
Products: -
Products: -
?
additional information
?
-
Aspergillus flavus NSH9
Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulation mechanisms of enzyme expression, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: immobilization of the enzyme on polyaniline polymer results in improved catalytic performance with decreased temperature optimum, and increased thermal stability and catalytic efficiency, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: modelling of potato starch saccharification by Aspergillus niger, influences of assay conditions on activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: modelling of potato starch saccharification by Aspergillus niger, influences of assay conditions on activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulation mechanisms of enzyme expression, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
Products: -
Products: -
?
additional information
?
-
Substrates: poor substrate: cyclodextrin
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has debranching activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: pullulan is a poor substrate, substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: poor activity with pullulan and laminarin
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glucoamylase also shows steroidal saponin-rhamnosidase activity, EC 3.2.1.40, being able to hydrolyze the terminal rhamnosyl of steroidal saponins and the sugar chain at the C-3 position of spirostanosides, the enzyme also hydrolyzed the terminal rhamnosyl residues of the sugar chain at the C-3 position while retaining the glucosyl residues at the C-26 position of furostanosides, substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
endophytic fungus EF6
-
Substrates: soluble starch is the best substrate, various raw starches, i.e. soluble starch, corn, tapioca, wheat, rice, sticky rice starch, are used as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme shows broad substrate specificity and raw starch hydrolyzing activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the key intestinal enzyme involved in the breakdown of glucose oligosaccharides in the small intestine
Products: -
Products: -
?
additional information
?
-
-
Substrates: key intestinal enzymes involved in the breakdown of glucose
Products: -
Products: -
?
additional information
?
-
Substrates: structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the basic catalytic properties of the N-terminal subunit of MGAM (ntMGAM) on the hydrolysis of glucan substrates and compared it with those of human native MGAM
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cyclodextrins and laminarin
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ripening and production of good taste in fermented tofu production, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificities of isozymes GA-I and GA-II, cyclodextrins are poor substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with sucrose, 4-nitrophenyl-beta-D-maltoside, methyl-beta-D-glucopyranoside, pullulan, alpha-cyclodextrin, beta-cyclodextrin, and trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows a broad substrate specificity
Products: -
Products: -
?
additional information
?
-
Penicillium oxalicum GXU20
Substrates: the enzyme shows a broad substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: the intracellular enzyme shows a unique substrate specificity compared to already known glucoamylases, in addition to the hydrolysis of branched and linear alpha-glucans, the purified enzyme preferentially attacks maltotriose, overview, oligossaccharides Dp2, Dp4, Dp5, Dp6, and Dp7 as well as isomaltose, panose, and isopanose are poor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for much of the isomaltase and maltase activities in the intestine of the frog
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme contains a carbohydrate-binding module, which functions independently to assist the carbohydrate-active enzyme, structure of a family 21 CBM from the starch-binding domain of Rhizopus oryzae glucoamylase, RoCBM21, determined by NMR spectroscopy
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme consists of at least two domains, one for adsorption to the starch molecule in the N-terminal portion, and the other for catalyzing starch degradation in the C-terminal portion
Products: -
Products: -
?
additional information
?
-
-
Substrates: reaction of the amyloglucosidase in concert with sweet almond beta-glucosidase, EC 3.2.1.21, to hydrolyze curcumin and eugenol in acetate buffer, method optimization, NMR product determinations, overview
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of alpha-1,6 linkages
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of alpha-1,6 linkages
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme binds poorly to insoluble starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds poorly to insoluble starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of alpha-1,6 linkages
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme does not show significant activity in the presence of starch
Products: -
Products: -
-
additional information
?
-
Substrates: enzyme does not show significant activity in the presence of starch
Products: -
Products: -
-
additional information
?
-
Substrates: no substrate: 4-nitrophenyl alpha-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 4-nitrophenyl alpha-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with pullulan, dextran, and isomaltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: raw starch, amylose, glycogen. Poor substrate: wheat starch
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme can attack alpha-1,4-glycosidic linkages and alpha-1,6-glycosidic linkages. The velocity of oligosaccharide hydrolysis decreases with a decrease in size of substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: displays broad substrate specificity by cleaving alpha-1,4- and alpha-1,6-glycosidic linkages in starch, amylopectin, amylose and pullulan. No activity is observed on alpha-cyclodextrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: displays broad substrate specificity by cleaving alpha-1,4- and alpha-1,6-glycosidic linkages in starch, amylopectin, amylose and pullulan. No activity is observed on alpha-cyclodextrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of alpha-1,6 linkages
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of alpha-1,6 linkages
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an exo-hydrolase that attacks the substrate from the non-reducing end, producing glucose with beta-anomeric configuration, substrate specificity with substrates from different sources in descending activity order: Paselli starch, soluble starch, corn-amylopectin, glycogen, and amylose, no activity with pullulan, alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin, TaGA is not able to catalyze the formation of oligosaccharides, e.g., by transglycosylation with glucose as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenyl alpha-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 4-nitrophenyl alpha-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
Substrates: no substrate: 4-nitrophenyl alpha-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
Substrates: branched glucooligosaccharides with a DP between five and twelve are produced from potato amylopectin digestion by alpha-amylase from Bacillus licheniformis and used as substrates for comparing their degradation by the glucoamylase GA2 from Hypocrea jecorina, analysis of the mode of action of the glucoamylase, substrate specificity, overview. The majority of branched gluco-oligosaccharides larger than DP7 have multiple branching points. The enzyme is active versus alpha-1,4- and alpha-1,6-linkages
Products: -
Products: -
?
additional information
?
-
Trichoderma reesei ATCC 56765
Substrates: branched glucooligosaccharides with a DP between five and twelve are produced from potato amylopectin digestion by alpha-amylase from Bacillus licheniformis and used as substrates for comparing their degradation by the glucoamylase GA2 from Hypocrea jecorina, analysis of the mode of action of the glucoamylase, substrate specificity, overview. The majority of branched gluco-oligosaccharides larger than DP7 have multiple branching points. The enzyme is active versus alpha-1,4- and alpha-1,6-linkages
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
Products: -
Products: -
?
additional information
?
-
Tricholoma matsutake NBRC 30605
Substrates: the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 glucose
glucooligosaccharide + 3 H2O
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Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
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r
isomaltose
isomaltooligosaccharide
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Substrates: reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
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r
maltodextrin + H2O
beta-D-glucose + ?
-
Substrates: -
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maltotriose + 2 H2O
3 beta-D-glucose
-
Substrates: -
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amylopectin + H2O
beta-D-glucose + ?
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Substrates: 104% of activity with soluble starch from potato
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amylopectin + H2O
beta-D-glucose + ?
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Substrates: 100% of activity with soluble starch from potato
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amylopectin + H2O
beta-D-glucose + ?
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Substrates: 104% of activity with soluble starch from potato
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amylose + H2O
beta-D-glucose + ?
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Substrates: 74% of activity with soluble starch from potato
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amylose + H2O
beta-D-glucose + ?
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Substrates: 60% of activity with soluble starch from potato
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amylose + H2O
beta-D-glucose + ?
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Substrates: 13% of activity with starch
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amylose + H2O
beta-D-glucose + ?
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Substrates: 63% of activity with soluble starch from potato
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dextrin + 6 H2O
7 beta-D-glucose
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Substrates: 91% of activity with soluble starch from potato
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dextrin + 6 H2O
7 beta-D-glucose
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Substrates: 89% of activity with soluble starch from potato
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dextrin + 6 H2O
7 beta-D-glucose
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Substrates: 84% of activity with soluble starch from potato
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dextrin + 6 H2O
7 D-glucose
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Substrates: the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
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glycogen + 3 H2O
4 beta-D-glucose
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Substrates: 103% of activity with soluble starch from potato
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glycogen + 3 H2O
4 beta-D-glucose
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Substrates: 90% of activity with soluble starch from potato
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glycogen + 3 H2O
4 beta-D-glucose
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Substrates: 150% of activity with starch
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glycogen + 3 H2O
4 beta-D-glucose
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Substrates: 96% of activity with soluble starch from potato
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maltooligosaccharide + H2O
beta-D-glucose
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Substrates: 49% of activity with soluble starch from potato
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maltooligosaccharide + H2O
beta-D-glucose
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Substrates: 55% of activity with soluble starch from potato
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maltooligosaccharide + H2O
beta-D-glucose
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Substrates: 54% of activity with soluble starch from potato
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maltose + H2O
beta-D-glucose + D-glucose
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Substrates: -
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maltose + H2O
beta-D-glucose + D-glucose
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Substrates: 17% of activity with soluble starch from potato
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maltose + H2O
beta-D-glucose + D-glucose
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Substrates: 2% of activity with soluble starch from potato
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maltose + H2O
beta-D-glucose + D-glucose
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Substrates: 24% of activity with soluble starch from potato
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maltose + H2O
beta-D-glucose + D-glucose
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Substrates: -
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: -
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: -
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
Mucor rouxians
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: rice starch, 95% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: maize starch, 83% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: native starch from potato, 92% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: rice starch, 110% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: maize starch, 105% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: native starch from potato, 105% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: glucoamylase is an exo-amylolytic enzyme that cleaves alpha-1,4-linked and alpha-1,6-linked glucose from starch
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
beta-D-glucose + ?
Substrates: -
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starch + H2O
beta-D-glucose + ?
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Substrates: strongest activity with soluble starch
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starch + H2O
beta-D-glucose + ?
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Substrates: soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: rice starch, 123% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: maize starch, 109% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: native starch from potato, 105% of activity with soluble starch from potato
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starch + H2O
beta-D-glucose + ?
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Substrates: the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
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starch + H2O
D-glucose + ?
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Substrates: the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
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starch + H2O
D-glucose + ?
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Substrates: important industrial enzyme that removes the glucose units from the non-reducing chain-ends of starch and glycogen by hydrolyzing alpha-1,4 linkages consecutively
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starch + H2O
D-glucose + ?
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Substrates: the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose
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starch + H2O
D-glucose + ?
Substrates: one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
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starch + H2O
D-glucose + ?
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Substrates: one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
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starch + H2O
D-glucose + ?
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Substrates: the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the starch chain, substrates corn cobs, maize starch, soluble starch, and wheat bran
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starch + H2O
starch + beta-D-glucose
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Substrates: soluble starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
Mucor rouxians
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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starch + H2O
starch + beta-D-glucose
Substrates: soluble starch
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starch + H2O
starch + beta-D-glucose
Substrates: -
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starch + H2O
starch + beta-D-glucose
Substrates: -
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starch + H2O
starch + beta-D-glucose
Substrates: -
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starch + H2O
starch + beta-D-glucose
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Substrates: the enzyme is required for degradation of raw starch
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additional information
?
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Substrates: catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
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additional information
?
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Substrates: catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
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additional information
?
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Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
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additional information
?
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Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
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additional information
?
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Aspergillus flavus NSH9
Substrates: glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
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additional information
?
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Substrates: regulation mechanisms of enzyme expression, overview
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additional information
?
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Substrates: glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis
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additional information
?
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Substrates: regulation mechanisms of enzyme expression, overview
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additional information
?
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Substrates: different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
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additional information
?
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Substrates: the key intestinal enzyme involved in the breakdown of glucose oligosaccharides in the small intestine
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additional information
?
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Substrates: key intestinal enzymes involved in the breakdown of glucose
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additional information
?
-
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Substrates: analysis of the basic catalytic properties of the N-terminal subunit of MGAM (ntMGAM) on the hydrolysis of glucan substrates and compared it with those of human native MGAM
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additional information
?
-
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Substrates: key enzyme in ripening and production of good taste in fermented tofu production, overview
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additional information
?
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Substrates: glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
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additional information
?
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Substrates: glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
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additional information
?
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Substrates: the enzyme is responsible for much of the isomaltase and maltase activities in the intestine of the frog
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additional information
?
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Substrates: glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
CaCl2
Co2+
Cu2+
Fe2+
Fe3+
K+
Mg2+
MgCl2
Mn2+
Na+
NaCl
Sn2+
Zn2+
ZnCl2
additional information
Ca2+
-
slight increase in enzyme activtiy
Mn2+
-
activates 51% and 65% at 5 mM and 10 mM, respectively, inhibitory at above 15 mM
Mn2+
-
slight increase in enzyme activity
NaCl
-
the glucoamylase exhibits a high degree of salt tolerance with residual activity above 65% after 24 h incubation in 2.0 M NaCl solution
additional information
-
Mg2+ and Mn2+ have negligible effect on the enzyme activity
additional information
-
no effects on enzyme activity by Li+ and K+, and by NaCl
additional information
metal ions, such as Na+, K+, Ca2+ and Cd2+, have no significant effect on the recombinant glucoamylase activity at concentration of 1 mM
additional information
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metal ions, such as Na+, K+, Ca2+ and Cd2+, have no significant effect on the recombinant glucoamylase activity at concentration of 1 mM
additional information
-
neither inhibitory nor activating: ions Mg2+, NH4+, Co2+, and Ca2+
additional information
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no effect on the recombinant enzyme by Li+, Zn2+, Mg2+, Cu+, Ca2+, and EDTA
additional information
-
no requirement for Ca2+, the enzyme is not affected by K+, and Mg2+
additional information
-
only slight effects by Co2+, Ca2+, Ba2+, Mg2+ and Hg2+, and oby other reagents, such as NaCl, NaBr, EDTA, KH2PO4, NaH2PO4, NH4F, NH4Cl, and KCl, overview
additional information
calcium ions has no obvious influence on enzyme activity. Most of the metal ions and chemical reagents do not have an obvious influence on PoGA15A activity
additional information
-
the enzyme does not depend on Ca2+ for its hydrolytic activity
additional information
-
no effects by guanidine chloride, Ca2+, Na+, and Mg2+ at 1 mM
additional information
Ba2+, K+, Al3+, Mg2+, Fe3+, Na+, Ni+, Li+, Co2+, and EDTA have poor effects on activity
additional information
-
Ba2+, K+, Al3+, Mg2+, Fe3+, Na+, Ni+, Li+, Co2+, and EDTA have poor effects on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-selenophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
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a structure analogue of salacinol, synthesis, overview
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-thiophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
a structure analogue of salacinol, synthesis, overview
(2S,3S,4S)-1-[(2S,3S,4S)-4-carboxy-2,3,4-trihydroxybutyl]-3,4-dihydroxy-2-methoxytetrahydrothiophenium
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a salacinol derivative, salacinol is a sulfonium ion with an internal sulfate counterion, synthesis of a compound with the D-arabinitol configuration in the heterocyclic ring displayed by salacinol, overview
1,4-dideoxy-1,4-[(1-octadecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol triflate
-
-
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-sulfoniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(S)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[1-(3-methyl)-butyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(6-ethoxy)-hexyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(9-methoxy)-nonyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
5-(1,4-dideoxy-1,4-episulfoniumylidene-D-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
5-(1,4-dideoxy-1,4-episulfoniumylidene-L-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
acarviosine
the inhibitor occupies the active-site pocket with the cyclohexitol moiety of acarviosine populating the -1 subsite
acarviostatin 103
-
component isolated from Streptomyces sp. strain PW638, also inhibitory to alpha-amylase, EC 3.2.1.1
DTT
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
miglitol
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
myricetin
potent inhibitor with high binding affinity for both N- and C-terminals of the enzyme. Molecular dynamics reveal that myricetin interacts in its stretched conformation through water-mediated interactions with the C-terminus and by normal hydrogen bonding with the N-terminus. Residue W1369 of the extended 21 amino acid residue helical loop of C-terminal plays a major role in myricetin binding
Periodate
-
27% inhibition at 5 mM, 30% at 10 mM, 35% at 15 mM. 34% Glycosyl content of the enzyme is lost at 2.1 mM of periodate
pyridoxal 5'-phosphate
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
tosylphenylalanylchloromethyl ketone
-
10% inhibition at 1 mM, 20% at 10 mM
Triton-X100
-
inhibits enzyme activity for 25% and 26% at concentrations of 1 mM and 2.5 mM, respectively, complete inhibition at 5 mM
4-chloromercuribenzoate
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
4-chloromercuribenzoate
-
complete inhibition at 10 mM, 72% inhibition at 1 mM
acarbose
binding structure, overview. Found in the active sites of both independent monomers. In both monomers an acarbose molecule is fitted and refined, assuming full occupancy
acarbose
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
acarbose
bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview
acarbose
-
inhibitory effect is 2 orders of magnitude higher for ntMGAM than for native MGAM
Ag+
-
38% inhibition of isozyme GA-I, 14% inhibition of isozyme GA-II at 1 mM
beta-cyclodextrins
-
above 5 mM, slight inhibition
-
blintol
-
a selenium analogue of salacinol, is very effective in controlling blood glucose levels in rats after a carbohydrate meal, thus providing a lead candidate for the treatment of type 2 diabetes, synthesis, overview
Cr3+
62% inhibition at 1 mM, complete inhibition at 5 mM
Cu2+
22% inhibition at 1 mM, complete inhibition at 5 mM
Cu2+
-
10 mM, 71% residual activity with substrate starch, 31% with substrate maltose
EDTA
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
Fe2+
27% inhibition at 1 mM, complete inhibition at 5 mM
Fe3+
62% inhibition at 1 mM, complete inhibition at 5 mM
Hg2+
-
34% inhibition of isozyme GA-II, 49% inhibition of isozyme GA-I at 1 mM
kotalanol
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
kotalanol
-
natural inhibitor isolated from the roots and stems of the plant Salacia reticulata
kotalanol
-
isolated from the roots and stems of the plant Salacia reticulata, contains an intriguing inner-salt sulfonium-sulfate structure, inhibition of glucosidases by salacinol and kotalanol is due to their ability to mimic both the shape and charge of the oxacarbenium-ion-like transition state involved in the enzymatic reactions
methyl alpha-D-glucoside
-
competitive with maltose and non-competitive with starch
Mn2+
-
activates 51% and 65% at 5 mM and 10 mM, respectively, inhibitory at above 15 mM
N-bromosuccinimide
-
complete inhibition at 1 mM of isozyme GA-I and isozyme GA-II
salacinol
-
a naturally occurring glycosidase inhibitor isolated from roots and stems of a Sri Lankan plant, Salacia reticulata, the OH group on C-2 of salacinol is critical as a hydrogen-bond donor with functional groups in the active site of the enzyme
salacinol
-
isolated from Salacia reticulata, a plant native to Sri Lanka and India that has been used in the Ayurvedic system of medicine for the treatment of diabetes, inhibition of the isolated recombinant N-terminal catalytic domain
salacinol
-
natural inhibitor isolated from the roots and stems of the plant Salacia reticulata
salacinol
-
isolated from the roots and stems of the plant Salacia reticulata, contains an intriguing inner-salt sulfonium-sulfate structure, inhibition of glucosidases by salacinol is due to their ability to mimic both the shape and charge of the oxacarbenium-ion-like transition state involved in the enzymatic reactions, the compound is capable of attenuating the spike in blood glucose levels
additional information
-
remarkable insensitivity of the enzyme to end product inhibition
-
additional information
EDTA and Na2EDTA do not affect the enzyme activity
-
additional information
-
the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme
-
additional information
-
glucose, cycloheximide, and actinomycin D nearly completely suppresses enzyme expression, repression mechanism, overview
-
additional information
-
binding of a short heterobidentate inhibitor simultaneously directed toward the catalytic and starch binding domains causes dimerization of glucoamylase and not, an intramolecular conformational rearrangement mediated by linker flexibility
-
additional information
-
not inhibitory at 5 mM: Ag2+, Ca2+, Zn2+, Mg2+ and Cd2+ and EDTA
-
additional information
-
tannins isolated from extracts of pomegranate, cranberry, grape, and cocoa inhibit the activity of glucoamylase and alpha-amylase in vitro. In general, larger and more complex tannins, such as those in pomegranate and cranberry, more effectively inhibit the enzymes than less polymerized cocoa tannins
-
additional information
-
neither inhibitory nor activating: EDTA, ions Mg2+, Cl-, NH4+, Co2+, and Ca2+. Slight inhibition: glycerol, K+, and Na+
-
additional information
enzyme activity is significantly inhibited when the substrate concentration exceeds approximately 10fold the Km value
-
additional information
-
the purified enzyme is sensitive to proteolytic degradation by alpha-chymotrypsin
-
additional information
structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
-
additional information
-
structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
-
additional information
-
structure-activity relationship and stereochemistry of inhibitors, synthesis of chain-extended sulfonium and selenonium salts of 1,4-anhydro-4-thio- or 4-seleno-D-arabinitol, analogues of the naturally occurring glycosidase inhibitor salacinol, by nucleophilic attack at the least hindered carbon atom of 4,6-O-benzylidene-2,5-di-O-p-methoxybenzyl-D-mannitol-1,3-cyclic sulfate by 2,3,5-tri-O-p-methoxybenzyl-1,4-anhydro-4-thio-or 4-seleno-D-arabinitol, giving the sulfonium and selenonium sulfates, respectively, and subsequent deprotection with trifluoroacetic acid, the extended polyhydroxylated aliphatic side chain is incorporated while maintaining the stereochemistry of C-2' and C-3' of salacinol or blintol, overview
-
additional information
-
ghavamiol, a nitrogen analogue of salacinol, is inactive as inhibitor
-
additional information
kinetics and mechanism of inhibition of the recombinant glucoamylase subunit Ct-MGAM and sucrase subunit Ct-SI, overview
-
additional information
-
kinetics and mechanism of inhibition of the recombinant glucoamylase subunit Ct-MGAM and sucrase subunit Ct-SI, overview
-
additional information
-
no inhibition by neuraminidase inhibitor and EDTA at 1-10 mM
-
additional information
-
AmyC, but not AmyD, exhibits substrate inhibition, the Ki for substrate inhibition decreases with increasing length of the oligosaccharides. AmyC accumulates an enzyme maltose-maltotriose dead-end complex in the steady state, kinetics and modelling, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Schardinger dextrin
-
slight stimulation of activity with maltose as substrate
sorbitol
-
presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2
trehalose
-
presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2
EDTA
-
chemical modification of the enzyme's carboxyl groups with EDTA as nucleophile in presence of 1-ethyl-3(3-dimethylaminopropyl)carbodiimide leads to a dramatic enhancement of enzyme catalytic activity and thermal stability
additional information
EDTA and Na2EDTA do not affect the enzyme activity
-
additional information
-
wheat bran, rice bran, and cellulose highly induce enzyme expression, maltose, cello-dextrins, cellulose, and cellulose- and hemicellulose-containing substrates also induce the enzyme to a lesser extent, induction mechanism, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
maltoheptaose
-
wild-type enzyme or mutant enzymes Gly183Lys or S184H
0.2
maltotriose
-
15°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.25
maltotriose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
0.89
maltotriose
-
30°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.017
starch
-
30°C, pH 4.2, glucoamylase immobilized on macroporous silica
additional information
maltodextrin
Km value of free enzyme, enzyme encapsulated within a metal organic framework and within biological metal organic framework is 8.97, 10.31 and 9.75 mg/ml, respectively
additional information
maltose
-
Km value 0.029 mg/ml, pH 5.5, temperature not specified in the publication
additional information
maltose
-
S0.5 value 2.2 mg/ml, Hill coefficient 1.0, pH 5, 75°C
additional information
additional information
-
0.56 g/l for amylopectin from potato
-
additional information
additional information
-
6.8 mg/ml for maltose, 1.9 mg/ml for soluble starch
-
additional information
additional information
-
0.76 g/l for glycogen from oyster
-
additional information
additional information
-
0.97 g/l for soluble starch of Zulkowsky type
-
additional information
additional information
-
0.92% for soluble starch, glucoamylase M2
-
additional information
additional information
-
101 g/l for dextran
-
additional information
additional information
-
Km-values for the wild type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
-
additional information
additional information
-
0.48 mg/ml for starch with glucoamylase II and III. 0.5 mg/ml for starch with glucoamylase I
-
additional information
additional information
-
0.741 mg/ml, hydrolysis of amylopectin with glucoamylase I. 0.667 mg/ml, hydrolysis of amylopectin with glucoamylase II. 0.455 mg/ml. Hydrolysis of amylose with glucoamylase I. 0.286 mg/ml, hydrolysis of amylose with glucoamylase II. 1.11 mg/ml, hydrolysis of glycogen with glucoamylase I. 1.54 mg/ml, hydrolysis of glycogen with glucoamylase II
-
additional information
additional information
-
4 g/l for maltose
-
additional information
additional information
-
3.8 g/l for pullulan
-
additional information
additional information
-
6.57 mg/ml for glucoamylase I with starch as substrate, 4.52 mg/ml for glucoamylase II with starch as substrate. 0.15 mg/ml for glucoamylase II with alpha-cyclodextrin as substrate, 2.0 mg/ml for glucoamylase II with beta-cyclodextrin as substrate
-
additional information
additional information
-
0.37 g/l for glycogen from rat liver
-
additional information
additional information
-
1.2 g/l for soluble starch
-
additional information
additional information
-
0.333 mg/ml for maltose
-
additional information
additional information
-
Km-values for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
-
additional information
additional information
-
kinetics and thermodynamics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics and thermodynamics, substrate specificity for fermentation
-
additional information
additional information
-
kinetics, recombinant enzyme
-
additional information
additional information
-
ligand binding kinetics, wild-type enzyme and mutants
-
additional information
additional information
-
modelling of potato starch saccharification by commercial Aspergillus niger enzyme, kinetics
-
additional information
additional information
-
biphasic kinetics for maltodextrin degradation
-
additional information
additional information
-
kinetics of native enzyme, and aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, overview
-
additional information
additional information
-
kinetics and thermodynamics of polyacrylamide gel-immobilized purified enzyme
-
additional information
additional information
-
kinetics and thermodynamics of native and EDTA-coupled enzyme, overview
-
additional information
additional information
-
kinetic analysis of glucoamylase-catalyzed hydrolysis of starch granules from various botanical sources, overview, Ko increases as the starch granule crystaline structure becomes dense
-
additional information
additional information
-
kinetics of starch hydrolysis by AMG modeled for two different systems, free enzyme in aqueous solution and entrapped enzyme within vesicles in aqueous suspension, overview, Michaelis-Menten kinetic model with product inhibition for intrinsic kinetics
-
additional information
additional information
-
Km-value: 4.34 g/l with corn maltodextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 7.51 U/mg with corn maltodextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 7.01 g/l with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 0.06 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Km-value: 0.49 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the immunoprecipitated maltase-glucoamylase
-
additional information
additional information
-
thermodynamics and kinetics of starch hydrolysis, overview
-
additional information
additional information
-
steady-state and pre-steady-state kinetic measurements using maltooligosacchrides as substrates, analysis and modelling, overview
-
additional information
additional information
-
Michaelis-Menten and Lineweaver-Burk kinetics
-
additional information
additional information
Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C
-
additional information
additional information
-
kinetic values Km and Vmax with soluble starch are 2.84 mg/ml and 239.2 U/ml, respectively, Lineweaver-Burk kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
KM values for amylopectin, glycogen and starch are 0.056, 0.062 and 0.065 mg/ml, respectively
-
additional information
additional information
-
using raw cassava starch as substrate, the enzyme has a Km value of 0.72 mg/mL with Vmax of 0.01248 mmol/min/mg
-
additional information
additional information
-
4.5 g/l with soluble starch
-
additional information
potato starch
-
S0.5 value 4.2 mg/ml, Hill coefficient 1.1, pH 5, 75°C
-
additional information
soluble starch
-
Km value of wild-type, mutant S132C/Y492C/L548C/A562C and mutant S132C/Y492C/L548C/A562C/Q108E is 0.77 mg/ml, 0.62 mg/ml and 0.29 mg/ml, respectively, 55°C, pH 4.5
-
additional information
starch
-
value is between 0.21 and 0.28 mg/ml
additional information
starch
-
value is about 18 mg/ml
additional information
starch
Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
-
Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
-
Km value 0.094 mg/ml, pH 5.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057 - 0.65
maltose
-
pH 4.5, 35°C, recombinant mutant D20C/A27C/S30P/G137A
30.9
maltotriose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
additional information
additional information
-
turnover numbers for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
-
additional information
additional information
-
turnover numbers for the wild-type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
-
additional information
additional information
-
turnover numbers for the recombinant enzymes with maltose through maltoheptaose as substrates
-
additional information
additional information
substrate specificity
-
additional information
additional information
-
substrate specificity
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
maltose
-
kcat/S0.5 value 45 ml/s/mg, Hill coefficient 1.0, pH 5, 75°C
additional information
additional information
Kcat/Km value is calculated as 4.47 l/g/s
-
additional information
potato starch
-
kcat/S0.5 value 4.8 ml/s/mg, Hill coefficient 1.1, pH 5, 75°C
-
additional information
soluble starch
-
kcat/Km value of wild-type, mutant S132C/Y492C/L548C/A562C and mutant S132C/Y492C/L548C/A562C/Q108E is 982.3 ml/s/mg, 1529 ml/s/mg and 3982.6 ml/s/mg, respectively, 55°C, pH 4.5
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00014
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-selenophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
pH 6.5, 37°C
0.00065
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-thiophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
pH 6.5, 37°C
0.01
(2S,3S,4S)-1-[(2S,3S,4S)-4-carboxy-2,3,4-trihydroxybutyl]-3,4-dihydroxy-2-methoxytetrahydrothiophenium
-
pH 6.5, 37°C, derived from D-arabinitol, recombinant enzyme
0.032
1,4-dideoxy-1,4-[(1-butyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.075
1,4-dideoxy-1,4-[(1-hexyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.051
1,4-dideoxy-1,4-[(1-octadecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.051
1,4-dideoxy-1,4-[(1-octyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.006
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.01
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol triflate
-
pH 6.5, 37°C
0.0001
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.00015
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.035
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
pH 6.5, 37°C
0.00014
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-seleniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.00065
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-sulfoniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.0101
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(S)-epi-seleniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.0001
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.00017
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.008
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
pH 6.5, 37°C
0.067
1,4-dideoxy-1,4-[[1-(3-methyl)-butyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.052
1,4-dideoxy-1,4-[[1-(6-ethoxy)-hexyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.033
1,4-dideoxy-1,4-[[1-(9-methoxy)-nonyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
additional information
additional information
-
Ki-value: 12.7 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Ki-value: 37.6 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase
-
0.000074
acarbose
-
IP-MGAM is highly sensitive to acarbose with a calculated Ki of 74 nmol/l
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
acarviostatin 103
Homo sapiens
-
IC50 value is 1.25 microg/ml, pH not specified in the publication, temperature not specified in the publication
0.0204
(+)-catechin
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-MGAM
0.0216
(+)-catechin
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-SI
0.0565
caffeic acid
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-MGAM
0.0582
caffeic acid
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-SI
0.0018
chlorogenic acid
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-SI
0.003
chlorogenic acid
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-MGAM
0.00151
epigallocatechin gallate
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-SI
0.0017
epigallocatechin gallate
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-MGAM
0.0249
gallic acid
Mus musculus
pH not specified in the publication, 37°C, recombinant glucoamylase subunit Ct-MGAM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1054.5
-
mutant S132C/Y492C/L548C/A562C/Q108E, substrate soluble starch, pH 4.5, 55°C
11.2
purified native enzyme, pH 4.5, 40°C, substrate raw cassava starch
13.2
purified enzyme, pH 5.0, 60°C, with soluble starch as substrate
22.7
purified native enzyme, pH 4.5, 40°C, substrate raw corn starch
24.7
purified native enzyme, pH 4.5, 40°C, substrate raw rice starch
298
purified recombinant enzyme, pH 4.5, 60°C, substarte raw potato starch
3 - 8
3.6
37.1
beta domain plus catalytic domain independently expressed, pH 4.6, 70°C
38
38.5
4.5
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw rice starch
4.7
43.8
-
substrate starch, pH 5.5, temperature not specified in the publication
5.1
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw potato starch
5.3
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw cassava starch
57.9
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate soluble starch
6.8
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw corn starch
80
80.5
purified native enzyme, pH 4.5, 40°C, substrate soluble starch
805.8
-
mutant S132C/Y492C/L548C/A562C, substrate soluble starch, pH 4.5, 55°C
9.4
-
substrate starch, pH 5.5, temperature not specified in the publication
9.9
purified native enzyme, pH 4.5, 40°C, substrate raw potato starch
additional information
additional information
-
values between 0.56 to 1.02 U/ml for different transformants
additional information
-
purified enzyme, 7.33 U/ml at pH 2.0 and 32.85 U/ml at pH 5.5, 50°C
additional information
-
activities of native enzyme, and aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, overview
additional information
-
enzyme activity of different recombinant constructs in Saccharomyces cerevisiae cultures, overview
additional information
-
enzyme amount adsorbed on the starch granule surface per unit area
additional information
-
activities of the enzyme immobilized on different polymers, overview
additional information
-
fermentation activity of diverse commercial enzyme samples, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
4 - 5.5
4.2
4.4
4.5
4.5 - 5
4.6
4.7
4.8
5 - 5.5
5.4
5.5
5.6
6.5
6.6
6.8
additional information
-
optimal pH for growth and enzyme production is pH 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5
1.5 - 6.5
-
pH 1.5: about 70% of maximal activity with starch as substrate, about 60% of the activity with maltose as substrate, pH 6.5: about 15% of maximal activity with maltose as substrate, about 55% of maximal activity with starch as substrate
2 - 13
-
over 20% of maximal activity within this range, profile overview
2 - 7
2 - 8
2 - 9
2.3 - 6.5
-
pH 2.3: about 20% of maximal maltase activity, about 50% of glucoamylase activity, pH 6.5: about 25% of maltase activity, about 35% of glucoamylase activity
2.5 - 8
-
pH 2.5: about 35% of maximal activity, immobilized enzyme, pH 2.5: about 55% of maximal activity, free enzyme, pH 8.0: about 25% of maximal activity, free enzyme, pH 8.0: about 50% of maximal activity, immobilized enzyme
2.5 - 8.5
-
soluble glucoamylase, approx. 70% of maximal activity at pH 2.5, approx. 50% of maximal activity at pH 8.5, crosslinked glucoamylase crystals, approx. 20% of maximal activity at pH 2.5, approx. 25% of maximal activity at pH 8.5
2.5 - 9
-
30% of maximal activity at pH 3.0 and pH 8.5, 50% of maximal activity at pH 3.5 and pH 7.0
3 - 10
3 - 6
3 - 7
3 - 8
3 - 9
3.5 - 10
3.5 - 10.5
85% of maximal activity at pH 4.0-10.0, and 70% of maximal activity at pH 3.5 and 75% at pH 10.5, respectively
3.5 - 6
-
pH 3.5: about 50% of maximal activity, pH 6.0: about 35% of maximal activity
3.5 - 8
4 - 10
-
approx. 15% of maximal activity at pH 4.0, approx. 85% of maximal activity at pH 10.0
4 - 6.5
-
over 50% of maximal activity within this range, profile overview
4 - 7
4 - 7.5
-
activity range, 75% of maximal activity at pH 4.8 and 6.8, profile overview
4 - 8
4.5 - 5
4.5 - 6
-
pH 4.5: about 40% of maximal activity, pH 6.0: about 75% of maximal activity
4.5 - 6.5
4.7
5.5 - 6.5
1 - 5
-
approx. 60% of maximal activity at pH 1.0, almost no activity at pH 5.0
1 - 5
-
approx. 50% of maximal activity at pH 1.0, almost no activity at pH 5.0
1 - 5
-
activity range of both free and immobilized enzymes, profiles, overview
1 - 5
-
approx. 70% of maximal activity at pH 1.0, almost no activity at pH 5.0
2 - 7
-
native glucoamylase, approx. 20% of maximal activity at pH 2.0 and pH 6.0, respectively, immobilized glucoamylase, approx. 30% of maximal activity at pH 2.0, approx. 40% of maximal activity at pH 6.0
2 - 7
-
pH 2.0: about 55% of maximal activity, pH 7.0: about 25% of maximal activity, free and immobilized enzyme
2 - 8
-
20% of maximal activity at pH 2.0 and 60% at pH 8.0, immobilized enzyme
2 - 8
-
pH 2.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity
3 - 10
recombinant enzyme, activity range, profile overview
3 - 6
-
pH 3.0: about 60% of maximal activity, pH 6.0: about 55% of maximal activity
3 - 6
-
pH 3.0: about 40% of maximal activity for glucoamylase II, about 70% of maximal activity for glucoamylase I. pH 6.0: about 75% of maximal activity for glucoamylase I and II
3 - 7
-
pH 3.0: about 55% of maximal activity, pH 7.0: about 60% of maximal activity
3 - 7
over 60% activity within this range, broad pH optimum, profile overview
3 - 7
approx. 50% of maximal activity at pH 3.0, almost no activity at pH 7.0
3 - 8
-
approx. 70% of maximal activity at pH 4.0, approx. 5% of maximal activity at pH 8.0
3 - 9
-
approx. 40% of maximal activity at pH 3.0, approx. 10% of maximal activity at pH 9.0
3.5 - 10
-
over 50% of maximal activity within this range, profile overview
3.5 - 8
-
approx. 10% of maximal activity at pH 3.5, approx. 30% of maximal activity at pH 8.0
4 - 7
Endomycopsis fibuligera
-
pH 4.0: about 15% of maximal activity, pH 7.0: about 25% of maximal activity
4 - 7
-
pH 4.0: about 80% of maximal activity, pH 7.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
45
50
55
60
60 - 70
65
70
75
80
90
additional information
50
-
immobilized enzyme, the enzyme immobilized on polyaniline polymer shows a 10°C decreased temperature optimum
55
-
hydrolysis of soluble starch, enzyme form GA-I and GA-II
additional information
-
optimal temperature for growth and enzyme production is 30°C
additional information
-
optimum temperature for growth and glucoamylase production is 40°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 80
-
30% of maximal activity at 0°C, 80% at 60°C, 70% at 20°C and 80°C, maximal activity at 40°C, profile overview
10 - 60
20 - 75
25 - 65
-
activity range, maximal activity at 50°C, 75% of maximal activity at 60°C, profile overview
25 - 90
approx. 15% of maximal activity at 25°C, approx. 20% of maximal activity a 90°C
30 - 100
30 - 60
30 - 70
30 - 80
30 - 90
35 - 60
-
35°C: about 50% of maximal activity, 60°C: about 90% of maximal activity
4 - 60
-
at 22°C and 4°C, the enzyme shows 55% and 25% of its maximal activity, lower activity above 45°C, highest activity between 30°C and 45°C
40 - 60
-
40°C: about 65% of maximal activity, 60°C: about 50% of maximal activity, glucoamylase II, about 60% of maximal activity, amylase I
40 - 65
-
approx. 35% of maximal activity at 40°C, approx. 30% of maximal activity at 65°C
45 - 70
-
45°C: about 35% of maximal activity, glucoamylase I, about 60% of maximal activity, glucoamylase II. 70°C: about 30% of maximal activity, glucoamylase I and II
50 - 100
50 - 75
-
50°C: about 40% of maximal activity, 75°C: about 25% of maximal activity
55 - 75
over 60% activity within this range, profile overview
60 - 100
90% of maximal activity at 80°C, low activity at 100°C
additional information
10 - 60
-
activity increases linearly from 10°C to 60°C and reaches a maximum at 60°C
20 - 75
-
immobilized glucamylase, approx. 20% of maximal activity at 30°C, approx. 50% of maximal activity at 75°C
30 - 100
-
approx. 15% of maximal activity at 30°C, approx. 50% of maximal activity at 100%
30 - 100
-
approx. 30% of maximal activity at 30°C, approx. 70% of maimal activity at 100%
30 - 60
-
30°C: about 30% of maximal activity, immobilized enzyme, 30°C: about 50% of maximal activity, free enzyme, 60°C: about 50% of maximal activity, free enzyme, 60°C: about 90% of maximal activity, immobilized enzyme
30 - 70
Endomycopsis fibuligera
-
30°C: about 70% of maximal activity, 70°C: about 15% of maximal activity
30 - 80
-
at temperatures between 55°C and 65°C the glucoamylase retains 95-100% of its activity, at 70°C over 75% of the activity remains, 23% at 80°C
30 - 80
recombinant enzyme, activity range, profile overview
50 - 100
-
approx. 20% of maximal activity at 50°C and 100°C, respectively
50 - 100
-
approx. 20% of maximal activity at 50°C and 100°C, respectively
additional information
-
glucoamylase secreted by Tetracladium sp. is a novel cold-adapted enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
3.8
4.5 - 4.8
4.9
5.5
polypeptide without the signal peptide (616 amino acid residues), sequence calculation
6.9
6
-
isoelectric focusing, probably 4 to 5 isoforms with pIs from 4.8 to 5.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
traditional Korean Nuruk fungi, two isozymes GA-I and GA-II
-
-
brenda
isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
UniProt
brenda
Aspergillus neotritici CGMCC 3.15694.3.2
isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
UniProt
brenda
isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
UniProt
brenda
strains 643.92 and 127.49, high identity with Aspergillus niger strain DSM 823
-
-
brenda
Penicillium oxalicum CGMCC 3.15650
the DELTAPoxKu70 strain is derived from Penicillium oxalicum strain HP7-1
UniProt
brenda
a soil-borne thermophilic fungus, gene gla
SwissProt
brenda
soil-borne thermophilic fungus, synonym, allescheria terrestris
-
-
brenda
i.e. Hypocrea lixii, strain CECT 2413, gene gla66
SwissProt
brenda
-
-
-
brenda
gene of glucoamylase from Aspergillus awamori integrated into genome of Saccharomyces cerevisiae
-
-
brenda
-
654806, 655179, 655380, 658791, 663906, 664207, 664391, 665281, 666778, 666786, 667009, 680931, 682864, 693054, 708235, 710494, 729537, 729773, 729868, 730189
-
-
brenda
locally isolated Aspergillus niger, wild-type and deoxy-D-glucose-resistant mutant
-
-
brenda
marine yeast, strain N13d isolated from deep sea of Pacific Ocean
-
-
brenda
high glucoamylase-producing strain RY3410, two isozymes GA-I and GA-II
-
-
brenda
the DELTAPoxKu70 strain is derived from Penicillium oxalicum strain HP7-1
UniProt
brenda
integration of the glucoamylase gene from Rhizopus oryzae into genome of Saccharomyces cerevisiae
-
-
brenda
a soil-borne thermophilic fungus, gene gla
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
cell culture growth conditions, optimization, partition factors, overview
brenda
-
the fungus is cultivated in Khanna medium, pH 5.5, for 4 days, at 25°C, in static condition, supplemented with potato starch and maltose in different concentrations, effects on Aspergillus japonicus cultivation, overview
brenda
Aspergillus japonicus Saito
-
the fungus is cultivated in Khanna medium, pH 5.5, for 4 days, at 25°C, in static condition, supplemented with potato starch and maltose in different concentrations, effects on Aspergillus japonicus cultivation, overview
-
brenda
high glucoamylase activity is induced upon culture of the fungus in a medium containing amylose compared with other saccharides such as glucose, rice starch, wheat starch, corn starch, and potato starch
brenda
Tricholoma matsutake NBRC 30605
-
high glucoamylase activity is induced upon culture of the fungus in a medium containing amylose compared with other saccharides such as glucose, rice starch, wheat starch, corn starch, and potato starch
-
brenda
additional information
significant glucoamylase activity is detected specifically in the seeds but not other tissues of the transgenic rice lines
brenda
additional information
-
significant glucoamylase activity is detected specifically in the seeds but not other tissues of the transgenic rice lines
brenda
additional information
-
culture on uncooked solid-state wheat bran medium
brenda
additional information
-
culture on uncooked solid-state wheat bran medium
-
brenda
additional information
-
optimization of growth conditions, enzyme expression depends on carbon source for growth, glucose nearly completely suppresses enzyme expression, while wheat bran, rice bran, and cellulose induce it, the enzyme prefers monosaccharides to disaccharides for growth, overview
brenda
additional information
-
culture conditions for enzyme production, overview
brenda
additional information
-
optimization of growth conditions, enzyme expression depends on carbon source for growth, glucose nearly completely suppresses enzyme expression, while wheat bran, rice bran, and cellulose induce it, the enzyme prefers monosaccharides to disaccharides for growth, overview
-
brenda
additional information
-
culture conditions for enzyme production, overview
-
brenda
additional information
-
high enzyme expression in solid-state fermentation on surface of wheat-based solid medium or wheat kernels, evaluation of culture conditions, overview
brenda
additional information
-
maximal enzyme expression at 65°C and pH 7.0
brenda
additional information
-
maximal enzyme expression at 65°C and pH 7.0
-
brenda
additional information
-
influence of different culture conditions on enzyme production, overview. A solid barley plate is the most suitable for mycelial growth, but glucoamylase production per growth area does not differ according to the raw material. During enzyme production in red koji, reducing the temperature from 35°C to 25°C for 48 h in the late stages of growth results in 1.4fold higher glucoamylase production with a concomitant increase in protein stability
brenda
additional information
-
culture conditions for enzyme production, overview
brenda
additional information
-
culture conditions for enzyme production, overview
brenda
additional information
-
culture conditions for enzyme production, overview
brenda
additional information
expression analysis, expression of the enzyme is controlled by growth conditions on translational level
brenda
additional information
-
expression analysis, expression of the enzyme is controlled by growth conditions on translational level
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the extracellular enzyme is attached to the cell wall
brenda
additional information
-
the enzyme is secreted by the cells in pancreas to small intestine
-
brenda
the enzyme contains a signal peptide, it is secreted
-
brenda
-
the enzyme contains a signal peptide, it is secreted
-
brenda
Penicillium oxalicum CGMCC 3.15650
-
the enzyme contains a signal peptide, it is secreted
-
-
brenda
-
the enzyme is secreted to the culture medium
-
brenda
the enzyme contains a signal peptide for secretion
-
brenda
-
the enzyme is anchored in the membrane of small intestinal epithelial cells
brenda
additional information
the N-terminal 17 amino acids are presumed to be a signal peptide
-
brenda
additional information
-
the N-terminal 17 amino acids are presumed to be a signal peptide
-
brenda
additional information
Aspergillus flavus NSH9
-
the N-terminal 17 amino acids are presumed to be a signal peptide
-
-
brenda
additional information
-
in callus the enzyme is present in the soluble fraction, in suspension culture it is present predominantly in the extracellular fraction
-
brenda
additional information
the extracellular enzyme contains a signal sequence
-
brenda
additional information
-
no potential signal peptide sequence
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
dynamic metabolic response of Aspergillus niger to glucose perturbation, regulatory mechanism for reduced glucoamylase production. Reduction of the total adenine nucleotides and major precursor amino acids indicate the upregulated RNA synthesis is required to produce stress proteins, and partially explains the drop of glucoamylase production when Aspergillus niger experiences a fluctuated glucose concentration environment, adenine nucleotides dynamic concentration profiles, overview
physiological function
additional information
evolution
-
the enzyme belongs to the superfamily of CBM 20, phylogenetic tree
evolution
the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the enzyme belongs to the glycosyl hydrolase family 15, GH15
evolution
the enzyme belongs to the glycosyl hydrolase family 15, GH15
evolution
-
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
-
evolution
-
the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
-
evolution
Aspergillus neotritici CGMCC 3.15694.3.2
-
the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
-
evolution
-
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
-
evolution
Penicillium oxalicum GXU20
-
the enzyme belongs to the glycosyl hydrolase family 15, GH15
-
evolution
Tricholoma matsutake NBRC 30605
-
the enzyme belongs to the glycosyl hydrolase family 15, GH15
-
evolution
Aspergillus japonicus Saito
-
the enzyme belongs to the superfamily of CBM 20, phylogenetic tree
-
malfunction
the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
malfunction
Penicillium oxalicum GXU20
-
the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
-
physiological function
-
enzyme hydrolyses glycogen to meet the energy requirements during asexual development
physiological function
glucoamylase is an exoglucohydrolase that primarily catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in raw starch and soluble oligosaccharides to generate beta-D-glucose
physiological function
-
glucoamylase enzymes catalyze hydrolysis of alpha(1-4) glycosidic bonds to release D-glucose residues from the non-reducing ends of starch and oligosaccharides. Glucoamylase also has limited ability to release D-glucose residues by promoting hydrolysis of alpha(1-6) linkages of amylopectin
physiological function
-
glucoamylase is an exo-acting enzyme that catalyses the production of beta-glucose from the non-reducing ends of amylose, amylopectin and glycogen
physiological function
reduction of the total adenine nucleotides and major precursor amino acids indicate the upregulated RNA synthesis is required to produce stress proteins, and partially explains the drop of glucoamylase production when Aspergillus niger experiences a fluctuated glucose concentration environment
physiological function
Rhizopus arrhizus 99-880
-
glucoamylase enzymes catalyze hydrolysis of alpha(1-4) glycosidic bonds to release D-glucose residues from the non-reducing ends of starch and oligosaccharides. Glucoamylase also has limited ability to release D-glucose residues by promoting hydrolysis of alpha(1-6) linkages of amylopectin
-
physiological function
-
glucoamylase is an exo-acting enzyme that catalyses the production of beta-glucose from the non-reducing ends of amylose, amylopectin and glycogen
-
additional information
-
the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
-
the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
the starch-binding domain (SBD) plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
additional information
-
enzyme structure modelling and comparison of the structural model of Tetracladium sp. glucoamylase with the solved structure of the Hypocrea jecorina glucoamylase
additional information
-
the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
-
additional information
-
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
Aspergillus flavus NSH9
-
the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
-
additional information
-
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
Penicillium oxalicum GXU20
-
the starch-binding domain (SBD) plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
-
Show AA Sequence and Transmembrane Helices (2804 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
105360
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
140000
26850
40000
42000
48000
49000
54000
55000
56000
57000
58000
59000
60000
61000
62000
63000
64000
65000
66000
68000
-
experimental molecular weight for glucoamylase 2, excellent agreement with the theoretical value
68400
69000
70000
72000
72063
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
72876
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
73000
74000
75000
76000
77000
78000
79920
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
82000
82327
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
82330
-
recombinant enzyme expressed in Pichia pastoris, matrix-assisted laser desorption ionization mass spectrometry
82839
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
83000
83869
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
83870
-
recombinant enzyme expressed in Saccharomyces cerevisiae, matrix-assisted laser desorption ionization mass spectrometry
84000
-
glucoamylase I, calculation from diffusion and sedimentation data
85000
86000
-
glucoamylase II, calculation from diffusion and sedimentation data
87000
88000
89000
-
x * 60000, isozyme GA-I, SDS-PAGE, x * 89000, isozyme GA-II, SDS-PAGE
90000
91000
93000
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
additional information
60000
-
x * 60000, isozyme GA-I, SDS-PAGE, x * 89000, isozyme GA-II, SDS-PAGE
62000
-
experimental molecular weight for low-glycosylated linker variant dgGA
64000
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
70000
-
calculated molecular weight for low-glycosylated linker variant dgGA
77000
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
91000
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
additional information
?
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
?
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
?
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
?
x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation
?
x * 65400, calculated from sequence, x * 80000, SDS-PAGE, recombinant protein
?
Aspergillus flavus NSH9
-
x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation
-
?
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
?
-
x * 63300, calculated from sequence, x * 65000, SDS-PAGE of recombinant protein
?
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
?
x * 75400, SDS-PAGE, x* 65400, polypeptide without the signal peptide (616 amino acid residues), sequence calculation
?
Penicillium oxalicum GXU20
-
x * 75400, SDS-PAGE, x* 65400, polypeptide without the signal peptide (616 amino acid residues), sequence calculation
-
dimer
-
complex formation with a heterobidentate ligand induces dimerization
monomer
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
monomer
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
-
monomer
-
a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker
monomer
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
-
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
Aspergillus flavus NSH9
-
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region
additional information
-
the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the starch-binding domain (SBD) of glucoamylase from Aspergillus niger is a small globular protein containing a disulfide bond. The structure of the SBD has been determined by NMR. Cys509 and Cys604 are at the N- and C-termini, respectively, and they are linked by a disulfide bond, analysis of the conformation surrounding the disulfide bond, overview
additional information
-
the starch-binding domain (SBD) of glucoamylase from Aspergillus niger is a small globular protein containing a disulfide bond. The structure of the SBD has been determined by NMR. Cys509 and Cys604 are at the N- and C-termini, respectively, and they are linked by a disulfide bond, analysis of the conformation surrounding the disulfide bond, overview
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
enzyme amino acid sequence analysis by MALDI-TOF mass spectrometry
additional information
the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview
additional information
-
the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
Mucor rouxians
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
Mucor rouxians
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the sequences from 1-19, 39-454, and 533-629 belong to the signal peptide, the catalytic domain of the glycosyl hydrolase family 15, and the starch-binding domain, respectively. Construction of a three-dimensional structure of PoGA15A by modelling using the known crystal structure of the glucoamylase from Hypocrea jecorina (PDB 2vn7). The three-dimensional structure shows that the catalytic domain is predicted to mainly contain an alpha-helix and a beta-propeller, which form the barrel structure. The starch-binding domain is predicted to have a beta-sandwich fold with eight beta-strands distributed in the two beta-sheets
additional information
-
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
-
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
Penicillium oxalicum GXU20
-
the sequences from 1-19, 39-454, and 533-629 belong to the signal peptide, the catalytic domain of the glycosyl hydrolase family 15, and the starch-binding domain, respectively. Construction of a three-dimensional structure of PoGA15A by modelling using the known crystal structure of the glucoamylase from Hypocrea jecorina (PDB 2vn7). The three-dimensional structure shows that the catalytic domain is predicted to mainly contain an alpha-helix and a beta-propeller, which form the barrel structure. The starch-binding domain is predicted to have a beta-sandwich fold with eight beta-strands distributed in the two beta-sheets
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
secondary structure analysis, the enzyme contains a family 21 carbohydrate-binding module involving residues W47, Y83, and Y93, the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, molecular modelling, structure-function relatioship
additional information
the enzyme contains a carbohydrate-binding module, which functions independently to assist the carbohydrate-active enzyme, structure of a family 21 CBM from the starch-binding domain of Rhizopus oryzae glucoamylase, RoCBM21, determined by NMR spectroscopy, CBM has a beta-sandwich fold with an immunoglobulin-like structure, ligand-binding properties, comparisons of CBM structures and topologies, docking simulations, overview
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
structure analysis of Sta1p, modelling
additional information
-
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
additional information
-
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
-
additional information
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
enzyme structure modelling and comparison of the structural model of Tetracladium sp. glucoamylase with the solved structure of the Hypocrea jecorina glucoamylase
additional information
-
two protein bands with MW of 70000 Da and 76000 Da are deteced by SDS-PAGE
additional information
the enzyme contains a signal peptide for secretion joined to the catalytic domain by a linker
additional information
-
the enzyme contains a signal peptide for secretion joined to the catalytic domain by a linker
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
glycoprotein
-
glucoamylase G1 contains 8.1% carbohydrate, glucoamylase G2 contains 7.6% carbohydrate, glucoamylase G3 contains 8.0% carbohydrate, glucoamylase G4 and G5 contain 7.5% carbohydrate
glycoprotein
Agroathelia rolfsii AHU 9627
-
glucoamylase G1 contains 8.1% carbohydrate, glucoamylase G2 contains 7.6% carbohydrate, glucoamylase G3 contains 8.0% carbohydrate, glucoamylase G4 and G5 contain 7.5% carbohydrate
-
glycoprotein
the model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The full-length structure of HrGA shows extensive N-glycosylation, where the resolved sites are at Asn99, Asn200, Asn427, Asn500, Asn514, Asn528 and Asn587. Asn200 is the only site that shows branching of the glycosylation chain
glycoprotein
-
carbohydrate content of the enzyme is 26.3%, 34% glycosyl content is lost at 2.1 mM of periodate
glycoprotein
-
two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-linked sugars essentially contribute to the stabilization of glucoamylase domains
glycoprotein
-
glycosyl chains of 5 and 8 sugar residues are linked to Asp171 and Asp395 respectively
glycoprotein
-
deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation
glycoprotein
-
deglycosylation of the enzyme leads to reduced thermal stability and a decrease in enzyme secretion, O-glycosylation
-
glycoprotein
-
carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
-
glucoamylase I and glucoamylase II contain 53.0 mol of carbohydrate per mol of enzyme
glycoprotein
mature protein is predicted to be glycosylated with at amino acid residues Asp39, Asp120 and Asp541
glycoprotein
-
carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
-
glucoamylase I contains 52.2 mol of carbohydrate per mol of enzyme, glucoamylase II contains 48.5 mol of carbohydrate per mol of enzyme
glycoprotein
glycan chains Man9GlcNAc2 (2.1 kDa) and Man3GlcNAc2 (0.98 kDa) are attached at residues Asn99 and Asn111, respcetively
glycoprotein
-
glycan chains Man9GlcNAc2 (2.1 kDa) and Man3GlcNAc2 (0.98 kDa) are attached at residues Asn99 and Asn111, respcetively
-
glycoprotein
-
the glycoprotein composition is estimated as 15% for the crude enzyme and 5.5% for the purified glucoamylase
glycoprotein
Aspergillus japonicus Saito
-
the glycoprotein composition is estimated as 15% for the crude enzyme and 5.5% for the purified glucoamylase
-
glycoprotein
-
carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
-
effects of deglycosylation on enzyme structure, activity and stability, overview, deglycosylation by alpha-mannosidase does not affect the pH optimum or the active site and catalytic reaction mechanism including conformational changes of the enzyme, the secondary enzyme structure remains unaltered, deglycosylation increases the enzyme aggregation and reduces the thermal stability, the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme
glycoprotein
-
O-glycosylation, required for enzyme stability and activity, structure overview
glycoprotein
the linker region between starch-binding and catalytic domains is heavily glycosylated. The O-glycosylated residues are Ser467(443), Ser468(444), Thr476(452), Ser477(453), Ser483(459), Ser484(460) and Thr486(462)
glycoprotein
O-glycosylation is observed in enzyme AnGA, in particular in the linker domain, which connects to the carbohydrate-binding domain. Only two sites, at Ser483 and Ser484, can be modelled with confidence. The catalytic domain of AnGA has two resolved N-glycosylation sites at Asn195 and Asn419, with two GlcNAc residues visible at Asn195 and one at Asn419
glycoprotein
-
O-glycosylation, required for enzyme stability and activity, structure overview
-
glycoprotein
-
alpha-D-mannopyranose is the dominant sugar present - about 91 residues. Hexosamine is also present as a minor component, 2.6% of the total carbohydrate. 41 alpha-D-mannopyranose residues are O-2 and O-3 glycosylated and 17 alpha-D-mannopyranose residues are involved in O-4 glycosylation
glycoprotein
-
contains 0.55% glucosamine and 12% neutral sugar which consists of a large amount of mannose and small amounts of galactose and glucose
glycoprotein
-
carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
-
glucoamylase II contains 40 mol of carbohydrate per mol of enzyme
glycoprotein
-
glucoamylase M1 contains 18% neutral sugar and 0.77% glucosamine
glycoprotein
-
glucoamylase M1 contains 102 mol of carbohydrate per mol of enzyme, glucoamylase M2 contains 57 mol of carbohydrate per mol of enzyme
glycoprotein
recombinant N-terminal catalytic subunit secreted from transformed S2 cells
glycoprotein
-
glucoamylase I contains 7.5% carbohydrate, glucoamylase II contains 6.5% carbohydrate
glycoprotein
-
enzyme form E3 contains 7% carbohydrate, enzyme form E4 contains 9% carbohydrate, enzyme form E4' contains 2.7% carbohydrate. Degree of N-glycosylation causes the conformational difference between the multiple forms of glucoamylase. Removal of N-linked sugar leeds to a significant thermostability decrease, wheras it has little effect on the catalytic activity
glycoprotein
-
carbohydrate content of isozymes GA-I and GA-II is 15.0% and 16.2%, respectively
glycoprotein
-
enzyme form GA-I contains 13.5% carbohydrate, enzyme form GA-II contains 9.4% carbohydrate
glycoprotein
-
enzyme form GA-I contains 13.5% carbohydrate, enzyme form GA-II contains 9.4% carbohydrate
-
glycoprotein
-
glucoamylase I contains 3.93% neutral sugar and glucoamylase II contains 3.22% neutral sugar
glycoprotein
the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
glycoprotein
glycosylation may occur during enzyme protein expression
glycoprotein
-
the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
-
glycoprotein
-
the enzyme is N-glycosylated. The purified recombinant enzyme is treated with enzyme Endo H to minimize N-glycosylation. The full-length structure of PoGA shows a greater degree of N-glycosylation, PoGA three glycosylation sites at Asn184, Asn410 and Asn514 are observed, most extensive at Asn184
-
glycoprotein
Penicillium oxalicum GXU20
-
glycosylation may occur during enzyme protein expression
-
glycoprotein
-
carbohydrate groups seem to play an important role in stabilizing the structure against inactivation by heat and storage
glycoprotein
-
O-glycosylation, isozymes glucoamylase C and D have 14.9% and 12.7% carbohydrate content, respectively
glycoprotein
-
glucoamylase C and D contain 14.9% and 12.7% carbohydrate, respectively
glycoprotein
Sta1p is hyperglycosylized, over 80% carbohydrate content
proteolytic modification
-
acid proteinases are involved in generating multiple glucoamylase forms in the fungus Aspergillus awamori through limited hydrolysis of this enzyme decreasing the stability of the enzyme in a pH-dependent manner, methods for removal of proteolytic activity, overview
proteolytic modification
-
the small enzyme form G2 consists of two molecular species identical to the residues 1-512 and 1-513 of the large enzyme form G1. The enzyme form G2 is generated by limited proteolysis of the larger enzyme form G1
proteolytic modification
-
cleavage of signal peptide of the recombinant enzyme expressed in Saccharomyces cerevisiae
proteolytic modification
-
enzyme form GI and GII are transformed products of enzyme form GIII due to the limited action of proteases and glucosidases. GII is formed from GIII upon the release of a peptide portion of approximately 8000 Da. Enzyme form GI is formed from enzyme form GII and GIII on the removal of both peptide and carbohydrate chains and/or glycopeptide fragments
additional information
the extracellular enzyme contains a signal sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 150 nl of 37 mg/ml protein in 20 mM sodium acetate, pH 5.0, with 150 nl of reservoir solution containing 60% Tacsimate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement using the catalytic domain of Aspergillus awamori glucoamylase as a search model (PDB entry 1glm)
cross linked glucoamylase crystals, glucoamylase is crystallized by the batch method using ammonium sulfate as precipitant, 65% saturation, along with 20% 2-propanol as cosolvent in 500 mM acetate buffer, pH 4.5, the solution is stirred at 4°C for 30 min and then kept for 16 h at the same temperature
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purified isolated N-terminal catalytic domain of the G1 isoform, generated by subtilisin cleavage, sitting-drop vapour-diffusion method, 20 mg/ml protein at pH 8.5, 22°C room temperatur, the reservoir solution contains 50 mM Tris acetate, pH 8.5, 22.5% PEG 6000, 0.4 M sodium acetate and 10% glycerol, mixing of 0.001 ml protein and reservoir solution and equilibration against 1 ml reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, the active site of the enzyme is in complex with both Tris and glycerol molecules, structure modelling
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 150 nl of 18 mg/ml protein in 25 mM piperazine, pH 5.0, and 150 mM NaCl, with 150 nl of reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement using the catalytic domain of Aspergillus awamori glucoamylase as a search model (PDB entry 1glm)
purified starch-binding domain (SBD)-containing polypeptide (amino acids 509-616) of Aspergillus niger glucoamylase, hanging drop vapour diffusion method, using 2.0-2.3 M ammonium sulfate, 1.7% w/v PEG 400, 15% v/v glycerol, and 85 mM HEPES, pH 7.5, as the reservoir solution, the asymmetric unit of the starch-binding domain is composed of four protein molecules, 20°C, two weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution, NMR structures of the SBD of Aspergillus niger glucoamylase (PDB entries 1kum, 1kul, 1aco, and 1acz) are used as search models for molecular replacement
apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 200 nl of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, with 150 nl of reservoir solution containing 100 nl of sodium propionate + sodium cacodylate, bis-tris-propane, pH 4.0, and 25% PEG 1500, and 50 nl of 0.2% thiodiglycolic acid, 0.2% adipic acid, 0.2% benzoic acid, 0.2% anhydrous oxalic acid, 0.2% terephthalic acid, and 20 mM HEPES, pH 6.8, and with 50 nl of a seeding stock solution containing 0.2 M sodium sulfate, and 20% PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using the catalytic domain of Aspergillus awamori glucoamylase as a search model (PDB entry 1glm)
in complex with alpha-(1,6)-linked isomaltotriose and isomaltotetraose at 1.2 and 1.3 A resolution, respectively. Site II binding is observed in both complexes, while site I binding is only found in the isomaltotetraose complex. Hence, site II acts as the recognition binding site for carbohydrate and site I accommodates site II to bind isomaltotetraose. Site I participates in sugar binding only when the number of glucosyl units of oligosaccharides is more than three
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling
purified recombinant enzyme, hanging drop vapour diffusion method, 20°C, 0.0015 ml of 20 mg/ml enzyme solution is mixed with 0.0015 ml of reservoir solution containing 10% w/v PEG 5000 monomethyl ether, 186 mM D-glucose, 10 mM DTT, and 1.0 M lithium chloride, in 100 mM MES, pH 6.1, cryoprotection by 20% w/v PEG 6000, 20% v/v 2-methyl-2,4-pentanediol, 2.5 mM CaCl2, 40 mM MES, pH 6.1, X-ray diffraction structure determination and analysis at 3.3 A resolution
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tGA crystals are grown at 24°C by the hanging-drop vapor diffusion method, 0.002 ml of a 14 mg/ml tGA solution in 20 mM Tris-HCl, pH 7.5, are mixed with the same volume of reservoier solution containing 14-16% polyethylene glycol 3350, 100 mm Tris-HCl, pH 8.0 and 200 mM Li2SO4, crystals of native tGA and tGA complexed with acarbose diffract to 2.2 A and 2.1 A resolution, respectively
X-ray crystallography, in two different space groups, at 1.85 and 1.90 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A246C
E400C
G127A/P128A
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site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G183K
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
I136L
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
I82F
173% of wild-type activity, substitution increases thermostability
L7M/H391Y
81% of wild-type activity, substitution significantly improves thermostability
N9H/I82F
145% of wild-type activity, substitution significantly improves thermostability
P128A/G139A/I136L
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site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
P307A/T310V/Y312M/N313G
-
up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates
S119Y
-
slight increase in activity as compared with the wild-type enzyme towards maltose. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S184H
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S411A
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54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6
S411G
-
catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4
S54P/T314A/H415Y
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the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
S8R
97145% of wild-type activity, substitution increases thermostability
S8R/Q338L
145% of wild-type activity, substitution significantly improves thermostability
T390A
138% of wild-type activity, mutant shows high thermostability with free activation energy changes 2.99 kJ/mol at 80°C
T390A/S436P
102% of wild-type activity, mutant shows high thermostability with free activation energy changes 3.1 kJ/mol at 80°C
V181T/N182Y/G183A
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2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G
-
remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency
S54P/T314A/H415Y
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the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
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A246C
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
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G127A/P128A
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site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
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G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
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P128A/G139A/I136L
-
site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
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D139S
mutation in potential N-gylcosylation motif, no change in gylcosylation. Slight decrease in specific specific activity towards raw starch
D139T
mutation in potential N-gylcosylation motif, no change in gylcosylation. Slight decrease in specific specific activity towards raw starch
G101S
mutation in potential N-gylcosylation motif, increase in glycosylation. 1.19fold increase in specific specific activity towards raw starch
G101S/Q113T
1.22fold increase in specific specific activity towards raw starch
G101T
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight increase in specific specific activity towards raw starch
G265T
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight decrease in specific specific activity towards raw starch
I46S
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight increase in specific specific activity towards raw starch
I46T
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight decrease in specific specific activity towards raw starch
L190T
mutation in potential N-gylcosylation motif, increase in glycosylation. Significant decrease in specific specific activity towards raw starch
M211S
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight decrease in specific activity towards raw starch
Q113T
mutation in potential N-gylcosylation motif, increase in glycosylation. 1.21fold increase in specific specific activity towards raw starch
Y174S
mutation in potential N-gylcosylation motif, increase in glycosylation. Specific specific activity towards raw starch similar to wild-type
Y174T
mutation in potential N-gylcosylation motif, increase in glycosylation. Slight increase in specific specific activity towards raw starch
G101S
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mutation in potential N-gylcosylation motif, increase in glycosylation. 1.19fold increase in specific specific activity towards raw starch
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G101T
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mutation in potential N-gylcosylation motif, increase in glycosylation. Slight increase in specific specific activity towards raw starch
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I46S
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mutation in potential N-gylcosylation motif, increase in glycosylation. Slight increase in specific specific activity towards raw starch
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I46T
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mutation in potential N-gylcosylation motif, increase in glycosylation. Slight decrease in specific specific activity towards raw starch
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Q113T
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mutation in potential N-gylcosylation motif, increase in glycosylation. 1.21fold increase in specific specific activity towards raw starch
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D20C/A27C/S30P/G137A
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site-directed mutagenesis, the mutant, designated THS8, is highly thermotolerant with increased stability at 80°C compared to the wild-type enzyme
E180Q
H391Y
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
R54L
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active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
T290A
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
T62A
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random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
W120F
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mutant of G1, 3% of wild-type kcat for maltose, 2% of kcat for maltotriose
W317F
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mutant of G1, 90% of wild-type kcat for maltose, 97% of kcat for maltotriose
Y175F
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mutation in subsite +3. Mutant displays only minor differences to wild-type in affinities to inhibitors acarbose and an acarbose conjugate
I339G
about 10% of wild-type specific activity
T47A
about 50% of wild-type specific activity
T47A/W48A
about 25% of wild-type specific activity
W48A
about 55% of wild-type specific activity
I339G
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about 10% of wild-type specific activity
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T47A
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about 50% of wild-type specific activity
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T47A/W48A
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about 25% of wild-type specific activity
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W48A
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about 55% of wild-type specific activity
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S132C/Y492C/L548C/A562C
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introduction of disulfide bonds between residues S132C-Y492C/L548C-A562C, mutant shows improved optimal temperature, melting temperature, specific activity, and catalytic efficiency
S132C/Y492C/L548C/A562C/Q108E
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introduction of disulfide bonds between residues S132C-Y492C/L548C-A562C, mutant shows improved optimal temperature, melting temperature, specific activity, and catalytic efficiency
W47A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A/Y47A
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site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A/D450A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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R15A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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T462A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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H447A/D450A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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R15A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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T462A
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site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
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W622C
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
W622D
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
W622G
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
W622H
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
W622S
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
W622C
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
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W622D
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
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W622G
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
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W622H
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
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W622S
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site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
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additional information
A246C
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the T50-value is enhanced by 4°C to 73°C. Compared to wild-type enzyme, the mutant is twice as active at 66°C but half as active at 45°C
A246C
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site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
E400C
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cysteinesulfinic acid derivative of C320A/E400C-SO2H has a 700times higher turnover number towards maltose relative to C320A/E400C, while the Km-value is unchanged. Compared to wild-type enzyme, the C400-SO2H derivative has a turnover number of 150-190% and 85-320% on maltooliogosaccharides and isomaltooligosaccharides respectively, while Km-values are similar to that of wild-type for disaccharides and 3.5-5.5fold and 1.8-2.5fold higher for the longer maltooligosaccharides and isomaltooligosaccharides. The inhibition constant of cysteinesulfinic acid derivative of C320A/E400C-SO2H for acarbose increases more than 10000-fold
E400C
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further oxidation of Cys thiol group to sulfinic acid, up to 300% higher kcat and decreased Km compared to wild-type, depending on substrate
E180Q
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mutant of G1, 48% of wild-type kcat for maltose, 88% of kcat for maltotriose
E180Q
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active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
additional information
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the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days, method optimization, overview
additional information
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the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview
additional information
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molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
additional information
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immobilization of the enzyme on polyaniline polymer results in improved catalytic performance with decreased temperature optimum, and increased thermal stability and catalytic efficiency with increased Vmax and reduced Km, overview
additional information
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random mutagenesis and mutant screening by plate thermostability assay for increased thermotolerance at 65-80°C, overview
additional information
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entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles, vesicle formation, method optimization, enzyme activity is very stable during the first three batch runs, overview
additional information
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engineered low-glycosylated variant of glucoamylase 1 with a short linker, low-glycosylated GA1 (dgGA). Low-glycosylated linker variant of GA1; GA1:L0 and dgGA:L0
additional information
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disulfide-deficient mutant of the starch-binding domain of glucoamylase
additional information
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improvement of enzyme for inductrial applications
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additional information
presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
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presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
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presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
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additional information
CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
additional information
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CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
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additional information
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purified glucoamylase is chemically modified by cross-linking with aniline hydrochloride in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide for 1, 7, or 13 min, resulting in aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, the aniline coupling of GA has profound enhancing effects on temperature, pH optima, and pKas of active site residues, overview
additional information
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enzyme immobilization on polyacrylamide gel highly decreases the entropy and enthalpy of thermal enzyme deactivation
additional information
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co-expressed recombinant barley alpha-amylase 1 mutant and recombinant GLA synergistically enhanced the rate of hydrolysis by about 3fold for corn and wheat starch granules, compared to the sum of the individual activities, exo-endo synergism, reaction ratios, overview
additional information
effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
additional information
Penicillium oxalicum GXU20
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effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
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additional information
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preparation of Ca-alginate gel beads, activation by p-benzoquinoone, and immobilization of purified enzyme, method, development, comparison of catalytic activities of free and immobilized enzyme, overview. Km values of free and entrapped glucoamylase are almost identical, while the covalently immobilized enzyme shows the lowest affinity for substrate. The covalently immobilized enzyme retains its activity over 36 days of shelf storage and after 30 repeated use runs
additional information
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use of cell surface engineering to display Rhizopus oryzae glucoamylase on the cell surface of yeast Saccharomyces cerevisiae, improvement in enzymatic desizing of starched cotton cloth using yeast codisplaying glucoamylase and cellulose-binding domain, overview
additional information
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immobilization of the enzyme onto chemically synthesized poly(o-toluidine) salt and base powders using adsorption and covalent crosslinking with glutaraldehyde, overview, The immobilized enzyme has a better thermal stability than the free enzyme
additional information
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construction of a mutant enzymes with improved catalytic activity with substrate starch by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, overview
additional information
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construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
additional information
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construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
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additional information
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enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
additional information
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enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
2 - 10.5
stability range, over 80% activity remaining at pH 2.0-9.5, 75-80% activity remaining at pH 10.0-10.5, 20% at pH 11.0, inactivation above
3 - 10
3 - 6
3 - 7
3 - 8
3 - 9
3.5 - 8
4 - 6.5
4 - 7
4 - 8
4.5 - 10
5 - 7
5.5 - 9
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the recombinant enzyme mutant S54P/T314A/H415Y retains 80% of its activity within this range
6 - 8
additional information
3 - 6
purified recombinant enzyme, stable between pH 3 and pH 6. The catalytic activity of the enzyme is reduced quickly at higher than pH 5 and is totally lost at higher than pH 7
3 - 8
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30 min, purified recombinant AmyC, 70% of maximal activity at pH 3.0, 85% at pH 8.0, profile overview
3 - 9
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approx. 15% loss of activity after 22 h at pH 3.0 and 4°C, approx. 72% loss of activity after 22 h at pH 9.0 and 4°C
3.5 - 8
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30 min, purified recombinant AmyD, 70% of maximal activity at pH 3.5, 85% at pH 8.0, inactive at pH 3.0, profile overview
3.5 - 8
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stable at pH 3.0-8.0, about 50% remaining activity at pH 3.0 and pH 10.0, 30% at pH 2.5 and pH 11.0
4 - 8
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purified native enzyme, stable, over 75% remaining activity after 3 h at 55°C
5 - 7
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purified enzyme, room temperature, 60% of the initial activity remain after 2 h at pH 5.0, and about 70% after 1 h at pH 7.0
5 - 7
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above and below abruptly loss of enzyme activity
6 - 8
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6 h, 40°C, loss of 10% activity at pH 6.0, loss of 20% at pH 7.0, and of 40% at pH 8.0
6 - 8
-
approx. 5% loss of activity after 2 h at pH 6.0, pH 7.0 and pH 8,0, approx. 45% loss of activity after 20 h at pH 6.0 and pH 7.0, 45% loss of activity after 7 h at pH 8.0
additional information
-
there is no growth and glucoamylase production at pH 10.0 and above and below 3.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
30
30 - 40
30 - 60
-
6 h, pH 7.0, completely stable at 30°C, loss of 10% activity at 40°C, loss of 20% at 50°C, and of 30% at 60°C
30 - 80
recombinant enzyme GlucaM retains full activity after 1 h of incubation at below 60°C and retains about 60% of the original activity after 1 h at 70°C, but it loses 60% of the original activity after 1 h of incubation at 80°C
37
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freshly isolated purified commercial preparation, 10 h, loss of 50% activity, purified commercial preparation after 6 months of storage, 10 h, loss of 75% activity
40
45
50
50 - 60
55
60
60 - 80
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the thermal stability at 70°C and other temperatures of the deglycosylated enzyme is reduced compared to the native enzyme
65
70
70 - 80
-
irreversible thermoinactivation kinetic analysis of recombinant wild-type and mutant enzymes, overview
75
80
90
additional information
100
purified recombinant enzyme, pH 5.0, loss of 43% activity after 15 min, loss of 80% activity after 30 min, and of 88% after 45 min, inactivation after 60 min
100
-
36% remaining activity after 10 min at pH 7.0, loss of 89% activity at pH 5.0
30
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enzyme in solid-state fermentation process of chestnut, pH 6.0, about 90% remaining activity after 24 h
40
purified extracellular enzyme, pH 5.0, 1 h, stable up to
40
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30 min, purified recombinant AmyC and AmyD, completely stable, rapid inactivation above
40
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purified enzyme, pH 6.0, loss of 30% activity after 2 h, loss of 60% activity after 8 h
45
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purified native enzyme, after 90 min about 95% of activity is remaining, after 300 min 20% activity remains
45
unstable above, inactivation half-time at 45°C is 9.8 min. Acarbose partially protects
50
-
purified native enzyme, 1 h, stable, 50% activity remaining after 2 h
50
purified extracellular enzyme, pH 5.0, 1 h, loss of 50% activity
50
-
half-life of free enzyme is 33.8 h, half-life of immobilized enzyme is 190 h
50
-
pH 5.0, soluble enzyme half-life: 160 h, liposome-entrapped enzyme shows full activity after 180 h
50
-
15 min, stable in presence of 1.25% soluble starch, about 80% loss of activity without starch
50
endophytic fungus EF6
-
purified enzyme, 1 h, stable up to, rapid decrease in activity above
50
-
2 h, about 50% loss of activity of enzyme form E4', about 15% loss of activity of enzyme form E4
50
purified native enzyme, pH 4.5, 1 h, completely stable up to
50
-
60 min, 45% of activity of the free enzyme is remaining, and 70-95% of the immobilized enzyme
55
-
freshly isolated purified commercial preparation, 10 h, loss of over 80% activity, purified commercial preparation after 6 months of storage, 10 h, loss of over 90% activity
55
purified native enzyme, pH 4.5, 1 h, 90% activity remaining
60
-
purified recombinant enzyme mutant S54P/T314A/H415Y, stable up to, irreversible thermo-inactivation of the mutant enzyme follows first-order kinetics
60
-
purified enzyme, about 62% of initial activity remains after 1 h of incubation
60
purified recombinant enzyme, pH 5.0, stable for 15 min, loss of 20% activity after 30 min, and of 50% after 45 min, 12% activity remains after 90 min, inactivation after 120 min
60
purified extracellular enzyme, pH 5.0, 1 h, inactivation
60
-
native enzyme shows a half-life of 25.67 min, ACG-13 shows a half-life of 67.3 min
60
-
immobilized enzyme, stable up to, melting temperature of the free enzyme
60
purified native enzyme, pH 4.5, 1 h, 30% activity remaining
65
-
purified recombinant enzyme mutant S54P/T314A/H415Y, half-life is 76 min
65
purified native enzyme, pH 4.5, 1 h, 20% activity remaining
65
purified recombinant intracellular enzyme, inctivation within 5 min
65
approx. 20% and 50% losss of activity after 20 h and 48 h, respectively, in the presence of 30% glucose
70
-
purified enzyme, about 45% of initial activity remains after 1 h of incubation
70
-
half-life in absence of starch: 15 min. Half-life in presene of 3% w/v starch or sorbitol: 50 min. Half-life in presence of 10% sorbitol: 40 min. Half-life in presence of 30% sorbitol: 65 min
70
-
250 min, immobilized enzyme loses 60% of its activity, half-life: 220 min. Free enzyme loses 75% of its activity, half-life 140 min
70
-
crosslinked glucoamylase crystals, 1.5% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 17% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
70
-
60 min, loss of activity of the free enzyme, and 60-90% activity remaining of the immobilized enzyme
70
-
stable up to, stability is increased in the presence of PEG8000
70
purified recombinant enzyme, 60 min, 80% remaining activity
70
-
no loss of activity after 24 h, 90% loss of activity after 60 h
70
-
30-40% loss of activity after 10 min, approx. 90% loss of activity after 40 min, complete loss of activity after 60 min
75
-
no activity loss after incubation at 75°C for 6 h, half life at 80°C 2.6 h
80
-
purified enzyme, about 28% of initial activity remains after 1 h of incubation
80
purified recombinant enzyme, pH 5.0, loss of 8% activity after 15 min, loss of 20% activity after 30 min, and of 75% after 45 min, 3% activity remains after 75 min, inactivation after 90 min
80
-
crosslinked glucoamylase crystals, 23% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 38% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
80
-
stable up to for 30 min at pH 7.0, loss of 40% activity at pH 5.0
80
-
no loss of activity after 24 h, 90% loss of activity after 60 h
80
-
purified recombinant enzyme, half-life in absence of Ca2+ is 15 min, in presence of 5 mM Ca2+ is 2 h
90
purified recombinant enzyme, pH 5.0, loss of 12% activity after 15 min, loss of 75% activity after 30 min, and of 85% after 45 min, inactivation after 75 min
90
-
crosslinked glucoamylase crystals, 48% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 55% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
90
-
no loss of activity after 12 h, 50% loss of activity after 24 h
90
-
purified recombinant enzyme, 4 min, 2% of maximal activity remaining in absence of Ca2+, 68% in presence of 5 mM Ca2+