Information on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase:
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EC NUMBERCOMMENTARY
3.2.1.133-

RECOMMENDED NAMEGeneOntology No.
glucan 1,4-alpha-maltohydrolaseGO:0043897

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysisBacillus sp.--693292
hydrolysisGeobacillus stearothermophilus--698428
hydrolysisThermus sp.--699487
hydrolysis of O-glycosyl bond----
transglycosylation----
transglycosylationThermus sp.--699487

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
4-alpha-D-glucan alpha-maltohydrolaseActs on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
BbmABacillus subtilis--646799
BSMAGeobacillus stearothermophilus--646797, 646798, 646802, 664522, 666955, 680324, 710128
BSTAGeobacillus stearothermophilus--698428
BTMABacillus thermoalkalophilus--663819, 679745
glucan 1,4-alpha-maltohydrolaseThermoplasma volcanium--678461
glucan 1,4-alpha-maltohydrolaseThermus sp.--678795
glucan 1,4-alpha-maltohydrolaseBacillus thermoalkalophilusQ68KL3-679745
glucan 1,4-alpha-maltohydrolaseGeobacillus stearothermophilusP19531-680324
glucan 1,4-alpha-maltohydrolaseLactobacillus gasseri--681349
glucan 1,4-alpha-maltohydrolaseBacillus sp.A7DWA8-681861
LGMALactobacillus gasseri--664997, 681349
MAaseGeobacillus caldoxylosilyticusC0LZ63-710449
maltogenic alpha-amylase----
maltogenic alpha-amylaseBacillus sp.--693292
maltogenic alpha-amylaseGeobacillus stearothermophilus--698428, 714654
maltogenic alpha-amylaseThermus sp.--699487
maltogenic amylaseThermus sp.--665335, 678795
maltogenic amylaseThermoplasma volcanium--678461
maltogenic amylaseBacillus thermoalkalophilusQ68KL3-679745
maltogenic amylaseGeobacillus stearothermophilus--680324, 710128
maltogenic amylaseLactobacillus gasseri--681349
maltogenic amylaseBacillus sp.--681861, 714495
maltogenic amylaseThermofilum pendens--707248, 715074
maltogenic amylaseGeobacillus caldoxylosilyticusC0LZ63-710449
NM319Bacillus sp.-Novamyl variant693292
NM326Bacillus sp.-Novamyl variant693292
NM398Bacillus sp.-Novamyl variant693292
NM404Bacillus sp.-Novamyl variant693292
NM447Bacillus sp.-Novamyl variant693292
NovamylGeobacillus stearothermophilusP19531-646796
NovamylBacillus sp.-; trade name693292
NovamylGeobacillus stearothermophilus-commercial preparation714654
Thermus maltogenic amylaseThermus sp.-hydrolyzes cyclodextrin faster than starch699487
ThMAThermus sp.--646797, 646800, 646803, 646806, 664208, 678795, 699487
TK4MAGeobacillus caldoxylosilyticusC0LZ63-710449
MAUS149Bacillus sp.A7DWA8-714495
additional informationGeobacillus caldoxylosilyticusC0LZ63the enzyme belongs to a subclass of cyclodextrin-hydrolyzing enzymes, belonging to glycoside hydrolase family 13, GH13710449

CAS REGISTRY NUMBERCOMMENTARY
160611-47-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus sp.-714495A7DWA8SwissProtManually annotated by BRENDA team
Bacillus sp.ma gene; US149681861A7DWA8SwissProtManually annotated by BRENDA team
Bacillus sp.strain TS-25; TS-25693292--Manually annotated by BRENDA team
Bacillus sp. TS-25TS-25693292--Manually annotated by BRENDA team
Bacillus sp. US149ma gene; US149681861A7DWA8SwissProtManually annotated by BRENDA team
Bacillus subtilisSUH4-2646799--Manually annotated by BRENDA team
Bacillus subtilis SUH4-2SUH4-2646799--Manually annotated by BRENDA team
Bacillus thermoalkalophilusstrain ET2663819--Manually annotated by BRENDA team
Bacillus thermoalkalophilusstrain ET2679745Q68KL3SwissProtManually annotated by BRENDA team
Bacillus thermoalkalophilus ET2strain ET2663819--Manually annotated by BRENDA team
Bacillus thermoalkalophilus ET2strain ET2679745Q68KL3SwissProtManually annotated by BRENDA team
Geobacillus caldoxylosilyticusgene GcaTK4MA; strain TK4, gene GcaTK4MA710449C0LZ63UniProtManually annotated by BRENDA team
Geobacillus stearothermophilus-646794, 646797, 646798, 646802, 664522, 666955, 698428, 710128, 714654--Manually annotated by BRENDA team
Geobacillus stearothermophilus-646796P19531SwissProtManually annotated by BRENDA team
Geobacillus stearothermophilusC599646795--Manually annotated by BRENDA team
Geobacillus stearothermophilusmaltogenic alpha-amylase precursor, amyM gene680324P19531SwissProtManually annotated by BRENDA team
Geobacillus stearothermophilus C599C599646795--Manually annotated by BRENDA team
Lactobacillus gasseriATCC 33323664997--Manually annotated by BRENDA team
Lactobacillus gasseriATCC33323681349--Manually annotated by BRENDA team
Lactobacillus gasseri ATCC33323ATCC33323681349--Manually annotated by BRENDA team
Thermofilum pendens-707248, 715074--Manually annotated by BRENDA team
Thermofilum pendens Hrk 5 (DSM 2475)-707248--Manually annotated by BRENDA team
Thermoplasma volcaniumGSS1678461--Manually annotated by BRENDA team
Thermus sp.-646800, 646801, 646803, 646804, 665335, 678795, 699487--Manually annotated by BRENDA team
Thermus sp.atomic coordinates and structure factors, PDB: 1SMA646797--Manually annotated by BRENDA team
Thermus sp.recombinant664208--Manually annotated by BRENDA team
Thermus sp.strain IM6501646805, 646806--Manually annotated by BRENDA team
Thermus sp. IM6501strain IM6501646805--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
acarbose + alpha-D-glucoseisoacarbose
show the reaction diagram		Thermus sp.--646804--?
acarbose + alpha-D-glucoseisoacarbose
show the reaction diagram		Geobacillus stearothermophilus-transglycosylation646798--?
acarbose + alpha-D-glucoseisoacarbose
show the reaction diagram		Thermus sp.-transglycosylation646800--?
acarbose + H2Oacarviosine-glucose + alpha-D-glucose
show the reaction diagram		Bacillus subtilis--646799--?
acarbose + H2Oacarviosine-glucose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus, Thermus sp.--646797--?
acarbose + H2Oacarviosine-glucose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus-hydrolysis646798--?
acarbose + H2Oacarviosine-glucose + alpha-D-glucose
show the reaction diagram		Thermus sp.-hydrolysis646800--?
acarbose + H2OD-glucose + acarviosine-glucose
show the reaction diagram		Bacillus thermoalkalophilus--663819--?
acarbose + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
acarbose + H2Oglucose + acarviosine-glucose
show the reaction diagram		Thermus sp.--699487--?
acarbose + H2Oacarviosine-glucose
show the reaction diagram		Thermofilum pendens--707248--?
alpha-(1,4)-glycosidic linked cyclodextrins + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.-main depolymerization of outer amylopectin branches699487--?
alpha-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794molar ratio 10:1646794?
alpha-cyclodextrin + H2O?
show the reaction diagram		Thermofilum pendens-64.7% activity compared to gamma-cyclodextrin707248--?
alpha-Schardinger dextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794--?
amylopectin + H2O?
show the reaction diagram		Geobacillus stearothermophilus-the maltogenic Bacillus stearothermophilus alpha-amylase preferentially hydrolyses the exterior chains of amylopectin. However, during the later phases, the enzyme also hydrolyses inner chains, presumably with a high multiple attack action714654--?
amylopectin + H2Omaltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794in the initial stages of hydrolysis enzyme produces maltotetraose, maltotriose and maltose, as the reaction progresses, the maltotriose and maltotetraose disappears, glucose being formed by the splitting of maltotriose into equimolar amounts of maltose and glucose646794?
amylopectin + H2Ofragments of amylopectin
show the reaction diagram		Geobacillus stearothermophilus-main depolymerization of outer amylopectin branches698428mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained-?
amylopectin + H2Omaltose + maltotriose
show the reaction diagram		Bacillus sp.--693292wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P-?
amylopectin + H2Oalpha-maltose + ?
show the reaction diagram		Thermus sp.-hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site678795--?
amylopectin + H2Ofragments of amylopectin + dextrin
show the reaction diagram		Geobacillus stearothermophilus-main depolymerization of outer amylopectin branches698428mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained-?
amylose + H2Oalpha-maltose + ?
show the reaction diagram		Thermus sp.-substrate size and geometric shape of catalytic site analyzed, wild-type, double and triple mutant enzymes tested, wild-type enzyme hydrolyzed amylose more favourably than amylopectin678795--?
beta-cyclodextrin + H2O?
show the reaction diagram		Geobacillus caldoxylosilyticusC0LZ63-710449--?
beta-cyclodextrin + H2O?
show the reaction diagram		Thermofilum pendens-78.1% activity compared to gamma-cyclodextrin707248--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Bacillus subtilis--646799--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646797--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermus sp.--646800, 646801--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794molar ratio 3:1646794?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Bacillus sp.A7DWA8highest catalytic efficiency714495--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermus sp.-prefers cyclodextrins to starch or pullulan as substrate646797--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermofilum pendens-hydrolytic activity715074--?
beta-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermoplasma volcanium-high thermostability, substrate preference dependent on oligomeric state678461--?
beta-cyclodextrin + H2Omaltose
show the reaction diagram		Bacillus thermoalkalophilus--663819mainly hydrolyzed to maltose-?
beta-cyclodextrin + H2Omaltose + ?
show the reaction diagram		Thermus sp.--665335--?
beta-cyclodextrin + H2Omaltose + ?
show the reaction diagram		Lactobacillus gasseri-relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9664997--?
beta-cyclodextrin + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus thermoalkalophilusQ68KL3main product alpha-maltose679745--?
beta-cyclodextrin + H2Oalpha-maltose + ?
show the reaction diagram		Lactobacillus gasseri-recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363681349--?
beta-cyclodextrin + H2Oalpha-maltose + glucose
show the reaction diagram		Bacillus sp.A7DWA8substrate determination for recombinant enzyme MAUS149681861--?
beta-cyclodextrin + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.--699487--?
cyclomaltodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermus sp.--646803, 646804--?
D-tagatose + maltotriosemaltosyl-tagatose
show the reaction diagram		Geobacillus stearothermophilus-transglycosylation666955--?
gamma-cyclodextrin + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermofilum pendens-maximal activity (100%)707248--?
gelatinised waxy maize starch + H2Oalpha-maltose + ?
show the reaction diagram		Geobacillus stearothermophilus--714654main product-?
maltoheptaose + H2Omaltose + D-glucose
show the reaction diagram		Thermus sp.--664208mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose-?
maltoheptaose + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
maltohexaose + H2O?
show the reaction diagram		Thermus sp.--664208--?
maltohexaose + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
maltopentaose + H2O?
show the reaction diagram		Thermus sp.--664208--?
maltopentaose + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
maltose + H2OD-glucose
show the reaction diagram		Thermus sp.--664208--?
maltotetraose + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794--?
maltotetraose + H2Omaltose + D-glucose
show the reaction diagram		Thermus sp.--664208mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose-?
maltotetraose + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
maltotriose + H2O?
show the reaction diagram		Thermus sp.--664208--?
maltotriose + H2O?
show the reaction diagram		Lactobacillus gasseri-recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363681349--?
maltotriose + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Geobacillus stearothermophilus--646794--?
maltotriose + H2Oalpha-maltose + alpha-D-glucose
show the reaction diagram		Thermoplasma volcanium--678461--?
puerarin + beta-cyclodextrindaidzein 8-C-glucosyl-(alpha-glucosyl)n-1
show the reaction diagram		Thermofilum pendens-transglycosylation activity715074--?
pullulan + H2O?
show the reaction diagram		Bacillus sp.A7DWA8-714495--?
pullulan + H2Opanose
show the reaction diagram		Bacillus subtilis--646799--?
pullulan + H2Opanose
show the reaction diagram		Thermus sp.--646800, 646804, 699487--?
pullulan + H2Opanose
show the reaction diagram		Thermofilum pendens--707248--?
pullulan + H2Opanose
show the reaction diagram		Bacillus thermoalkalophilus--663819mainly hydrolyzed to panose-?
pullulan + H2Omaltose + D-glucose + panose
show the reaction diagram		Lactobacillus gasseri-relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9664997mainly maltose and glucose with relatively minor quantity of panose and other maltooligosaccharides-?
pullulan + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
pullulan + H2Oalpha-maltose + ?
show the reaction diagram		Lactobacillus gasseri-recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363681349--?
pullulan + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus sp.A7DWA8substrate determination for recombinant enzyme MAUS149681861--?
pullulan + H2Opanose + ?
show the reaction diagram		Bacillus thermoalkalophilusQ68KL3main product panose679745--?
simmondsin + acarviosine-glucoseacarviosine-simmondsin + alpha-D-glucose
show the reaction diagram		Thermus sp.-transglycosylation646804novel compound in which acarviosine is attached to the glucose-moiety of simmondsin by an alpha-(1,6)-glycosidic linkage, with both antiobesity and hypoglycemic activity646804?
soluble starch + H2Omaltose + ?
show the reaction diagram		Lactobacillus gasseri-relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9664997--?
starch + H2O?
show the reaction diagram		Thermofilum pendens-the enzyme shows a substrate hydrolysis preference for cyclodextrins over starch715074--?
starch + H2Omaltose
show the reaction diagram		Bacillus thermoalkalophilus--663819mainly hydrolyzed to maltose-?
starch + H2Oalpha-maltose
show the reaction diagram		Bacillus subtilis--646799--?
starch + H2Oalpha-maltose
show the reaction diagram		Geobacillus stearothermophilus--646794-646794?
starch + H2Oalpha-maltose
show the reaction diagram		Geobacillus stearothermophilus, Thermus sp.--646797-646797?
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646800-646800?
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646801-646801?
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646804-646804?
starch + H2Oalpha-maltose
show the reaction diagram		Lactobacillus gasseri--681349--?
starch + H2Oalpha-maltose
show the reaction diagram		Bacillus sp.A7DWA8-714495--?
starch + H2Oalpha-maltose
show the reaction diagram		Thermofilum pendens--707248--?
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.-catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism646797-646797?
starch + H2Oalpha-maltose
show the reaction diagram		Geobacillus stearothermophilus-exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends646794-646794?
starch + H2Oalpha-maltose
show the reaction diagram		Bacillus subtilis-carbohydrate metabolism in the cytoplasm646799-646799?
starch + H2Oalpha-maltose
show the reaction diagram		Bacillus sp.A7DWA8substrate determination for recombinant enzyme MAUS149681861--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Thermus sp.--678795--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium--678461--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus thermoalkalophilusQ68KL3-679745--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Geobacillus stearothermophilusP19531-680324--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus sp.A7DWA8maltogenic amylase from Bacillus sp.681861--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium-transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products678461--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Geobacillus stearothermophilusP19531utilization of BSMA for production of highly branched amylopectin and amylose from enzymatically modified rice starch, branching by transglycosylation mediated by BSMA, increased number of branched side chains in modified amylopectin clusters determined680324--?
starch + H2Oalpha-maltose + ?
show the reaction diagram		Lactobacillus gasseri-wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration681349--?
starch + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.--699487--?
maltotriose + H2Oisomaltose + isopanose + panose + branched glucooligosaccharides
show the reaction diagram		Thermus sp.--699487transfer products of transglycosylation-?
additional information?-Thermus sp.-exhibits dual activity of alpha-D-(1,4)- and alpha-D-(1,6)- glycosidic bond cleavages, shows activity of alpha-D(1,4)- to alpha-D-(1,3), alpha-D-(1,4), or alpha-D-(1,6)-transglycosylation and cleaves acarbose, a pseudotetrasaccharide competitive inhibitor of alpha-amylases646797---
additional information?-Thermus sp.-nearly indistinguishable from cyclomaltodextrinase from Bacillus sp. and Bacillus stearothermophilus neopullulanase, distinguished from typicsl alpha-amylases by containing a novel N-terminal domain and exhibiting preferential substrate specificities for cyclomaltodextrins over starch646803---
additional information?-Lactobacillus gasseri-enzyme shows hydrolytic activity towards alpha-1,6-glycosidic linkage664997---
additional information?-Geobacillus stearothermophilus-BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages, the enzyme forms highly branched products from branched glucan and branching enzyme-treated tapioca starch710128---
additional information?-Thermofilum pendens-maltooligosaccharides G3-G7 show 5.4-24.1% relative activity compared to gamma-cyclodextrin707248---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
acarbose + H2Oglucose + acarviosine-glucose
show the reaction diagram		Thermus sp.--699487--
alpha-(1,4)-glycosidic linked cyclodextrins + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.-main depolymerization of outer amylopectin branches699487--
amylopectin + H2Omaltose + maltotriose
show the reaction diagram		Bacillus sp.--693292wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P-
amylopectin + H2Ofragments of amylopectin + dextrin
show the reaction diagram		Geobacillus stearothermophilus-main depolymerization of outer amylopectin branches698428mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained-
beta-cyclodextrin + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.--699487--
pullulan + H2Opanose
show the reaction diagram		Thermus sp.--699487--
starch + H2Oalpha-maltose
show the reaction diagram		Geobacillus stearothermophilus--646797-646797
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646800-646800
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646801-646801
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.--646804-646804
starch + H2Oalpha-maltose
show the reaction diagram		Lactobacillus gasseri--681349--
starch + H2Oalpha-maltose
show the reaction diagram		Thermus sp.-catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism646797-646797
starch + H2Oalpha-maltose
show the reaction diagram		Geobacillus stearothermophilus-exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends646794-646794
starch + H2Oalpha-maltose
show the reaction diagram		Bacillus subtilis-carbohydrate metabolism in the cytoplasm646799-646799
starch + H2Oalpha-maltose + ?
show the reaction diagram		Thermus sp.--678795--
starch + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus thermoalkalophilusQ68KL3-679745--
starch + H2Oalpha-maltose + ?
show the reaction diagram		Geobacillus stearothermophilusP19531-680324--
starch + H2Oalpha-maltose + ?
show the reaction diagram		Bacillus sp.A7DWA8maltogenic amylase from Bacillus sp.681861--
starch + H2Oalpha-maltose + ?
show the reaction diagram		Thermoplasma volcanium-transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products678461--
starch + H2Omaltooligosaccharide
show the reaction diagram		Thermus sp.--699487--
maltotriose + H2Oisomaltose + isopanose + panose + branched glucooligosaccharides
show the reaction diagram		Thermus sp.--699487transfer products of transglycosylation-
additional information?-Geobacillus stearothermophilus-BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages710128--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Al3+Thermofilum pendens-enzyme activity increases to 146.8% in the presence of 5 mM AlCl3707248
Ca2+Lactobacillus gasseri-5 mM, causes 20% increase in hydrolysis of starch664997
Ca2+Thermus sp.-mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L shows highly improved thermostability and catalytic activity in presence of Ca2+.665335
Ca2+Thermofilum pendens-enzyme activity increases to 136% in the presence of 5 mM CaCl2707248
Mg2+Lactobacillus gasseri-5 mM, causes 9% increase in hydrolysis of starch664997
Mg2+Thermofilum pendens-enzyme activity increases to 130% in the presence of 5 mM CaCl2707248
additional informationGeobacillus caldoxylosilyticusC0LZ635 mM Zn2+ has no effect on the enzyme activity710449

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
acarboseLactobacillus gasseri--664997 2D-image
Ba2+Thermofilum pendens-enzyme activity decreases to 77.3% in the presence of 5 mM BaCl2707248 2D-image
Co2+Lactobacillus gasseri-5 mM, 76% inhibition664997 2D-image
Co2+Geobacillus caldoxylosilyticusC0LZ63the enzyme is inhibited by 23% at 5 mM710449 2D-image
Cu2+Thermofilum pendens-enzyme activity decreases to 17% in the presence of 5 mM CuCl2707248 2D-image
Cu2+Geobacillus caldoxylosilyticusC0LZ63the enzyme is inhibited by 15% at 5 mM710449 2D-image
CuCl2Geobacillus stearothermophilus--646794 2D-image
EDTALactobacillus gasseri-5 mM, 74% inhibition664997 2D-image
Fe2+Lactobacillus gasseri-5 mM, 90% inhibition664997 2D-image
Fe2+Thermofilum pendens-enzyme activity decreases to 18.4% in the presence of 5 mM FeSO4707248 2D-image
Fe2+Geobacillus caldoxylosilyticusC0LZ63the enzyme is inhibited by 28% at 5 mM710449 2D-image
Hg2+Thermofilum pendens-enzyme activity decreases to 17.5% in the presence of 5 mM HgCl2707248 2D-image
HgCl2Geobacillus stearothermophilus--646794 2D-image
Li+Geobacillus caldoxylosilyticusC0LZ63the enzyme is inhibited by 67% at 5 mM710449 2D-image
Zn2+Lactobacillus gasseri-5 mM, 96% inhibition664997 2D-image
Zn2+Thermofilum pendens-enzyme activity decreases to 17.8% in the presence of 5 mM ZnCl2707248 2D-image
ZnCl2Geobacillus stearothermophilus--646794 2D-image
Mn2+Thermofilum pendens-enzyme activity decreases to 50.2% in the presence of 5 mM MnCl2707248 2D-image
additional informationGeobacillus stearothermophilus-no inhibition by sulfhydryl reagents, no inhibition with p-chloromercuribenzoate or Schardinger dextrins646794-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Ca2+Geobacillus caldoxylosilyticusC0LZ63the enzyme is activated by 15% at 5 mM710449 2D-image
DMSOThermofilum pendens-enzyme activity increases to 136% in the presence of 10% (v/v) DMSO707248 2D-image
EDTAThermus sp.-increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L665335 2D-image
ethanolThermofilum pendens-enzyme activity increases to 113% in the presence of 10% (v/v) ethanol707248 2D-image
methanolThermofilum pendens-enzyme activity increases to 104.4% in the presence of 10% (v/v) methanol707248 2D-image
Mn2+Geobacillus caldoxylosilyticusC0LZ63the enzyme is activated by 51% at 5 mM710449 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.426-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646800 2D-image
0.545-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332D646800 2D-image
1-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332Q646800 2D-image
1.08-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332H646800 2D-image
0.05-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant DM646805 2D-image
0.09-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 4B74646805 2D-image
0.128-beta-cyclodextrinBacillus thermoalkalophilus--663819 2D-image
0.16-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type and variants 3C71, 4B78 and 4A48646805 2D-image
0.17-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variants 1B76, 1B100646805 2D-image
0.174-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, wild-type646803 2D-image
0.19-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 2A39646805 2D-image
0.263-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646801 2D-image
0.308-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl646801 2D-image
0.36-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA DELTA124, 1M KCl646801 2D-image
0.461-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124646801 2D-image
2.03-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, mutant W47A646803 2D-image
1.5-maltoheptaoseThermoplasma volcanium-kinetic parameters for C14-labelled maltooligosaccharides678461 2D-image
8.18-maltoheptaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
9.21-maltoheptaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
3.8-maltohexaoseThermoplasma volcanium-kinetic parameters for C14-labelled maltooligosaccharides678461 2D-image
7.16-maltohexaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
7.53-maltohexaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
3.5-maltopentaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
3.97-maltopentaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
4.4-maltopentaoseThermoplasma volcanium-kinetic parameters for C14-labelled maltooligosaccharides678461 2D-image
63.43-maltoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
427-maltoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
1.6-maltotetraoseThermoplasma volcanium-kinetic parameters for C14-labelled maltooligosaccharides678461 2D-image
2.95-maltotetraoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
3.38-maltotetraoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
1.13-maltotrioseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
2.52-maltotrioseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
4.1-soluble starchThermoplasma volcanium-estimated for monomeric conformation, in presence of 1 M NaCl678461-
13-soluble starchThermoplasma volcanium-estimated for the high oligomer conformation678461-
3.6-maltotrioseThermoplasma volcanium-kinetic parameters for C14-labelled maltooligosaccharides678461 2D-image
additional information-additional informationThermus sp.-Km 49.7 mg/ml, starch as substrate, pH 6.0, 60°C, wild-type, 1 M KCl; Km 5.34 mg mL-1, starch as substrate, pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124; Km 61.0 mg/ml, starch as substrate, pH 6.0, 60°C, hydrolysis, wild-type; Km 7.72 mg/ml, starch as substrate, pH 6.0, 60°C, truncated mutant ThMA-DELTA124, 1M KCl646801-
additional information-additional informationThermus sp.-Km 131 mg/ml, starch as substrate, mutant W47A; Km 73.5 mg/ml, starch as substrate, wild-type646803-
additional information-additional informationThermus sp.-lower affinity for binding of amylopectin but higher affinity for amylose in mutant enzymes demonstrated, sterospecific substrate binding properties of triple mutant enzyme determined by molecular modelling678795-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
18.7-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332H646800 2D-image
41.4-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332Q646800 2D-image
45.4-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, mutant E332D646800 2D-image
67.8-acarboseThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646800 2D-image
3.43e-06-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124646801 2D-image
3.67e-06-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl646801 2D-image
20-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variants DM and 4B74646805 2D-image
110-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 4B78646805 2D-image
120-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 3C71646805 2D-image
126-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl646801 2D-image
126-beta-cyclodextrinThermus sp.--646803 2D-image
130-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 4A48646805 2D-image
160-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646805 2D-image
167-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646801 2D-image
170-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 2A39646805 2D-image
180-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, mutantW47A646803 2D-image
190-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 1B100646805 2D-image
200-beta-cyclodextrinThermus sp.-pH 6.0, 60°C, hydrolysis, variant 1B76646805 2D-image
2-maltoheptaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
42.5-maltoheptaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
72.08-maltoheptaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
384.1-maltoheptaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
9.2-maltohexaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
2050maltohexaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
88.45-maltohexaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
160.3-maltohexaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
69.01-maltopentaoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
197-maltopentaoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
0.04-maltoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
0.29-maltoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
29.8-maltotetraoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
173.5-maltotetraoseThermus sp.-50°C, pH 6.0, mutant enzyme A290I664208 2D-image
574.1-maltotetraoseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
0.0370.23maltotrioseThermus sp.-50°C, pH 6.0, mutant enzyme A29I664208 2D-image
79.07-maltotrioseThermus sp.-50°C, pH 6.0, mutant enzyme A29I664208 2D-image
652.5-maltotrioseThermus sp.-50°C, pH 6.0, wild-type enzyme664208 2D-image
0.000245-StarchThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124646801 2D-image
0.000332-StarchThermus sp.-pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl646801 2D-image
249-StarchThermus sp.-pH 6.0, 60°C, wild-type646803 2D-image
301-StarchThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type646801 2D-image
335-StarchThermus sp.-pH 6.0, 60°C, mutant W47A646803 2D-image
457-StarchThermus sp.-pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl646801 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.2-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variant DM646805
0.3-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B74646805
1-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B78646805
1.5-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, wild-type646805
1.7-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variants 2A39, 4A48 and 3C71646805
2-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B100646805
2.04-Thermus sp.--646806
2.1-Thermus sp.-pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B76646805
5.4-Thermus sp.-beta-cyclodextrin as substrate, dimer646801
14.2-Thermus sp.-starch as substrate646801
21.1-Thermus sp.-starch as substrate, 0.2 M KCl646801
24-Thermus sp.-starch as substrate, 0.4 M KCl646801
26-Thermus sp.-starch as substrate, 0.6 M KCl646801
26.3-Thermus sp.-starch as substrate, 0.8 M KCl646801
27.6-Thermus sp.-starch as substrate, 1.0 M KCl646801
30.5-Thermus sp.-soluble starch as substrate, monomer646801
58.7-Lactobacillus gasseri-hydrolysis of beta-cyclodextrin664997
91-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CuCl2707248
93.6-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM HgCl2707248
95.2-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM ZnCl2707248
98.5-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM FeSO4707248
177.4-Thermofilum pendens-cell extract, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)707248
194.1-Thermus sp.-beta-cyclodextrin as substrate, monomer646801
206.8-Thermus sp.-beta-cyclodextrin as substrate, 1.0 M KCl646801
210-Thermus sp.-beta-cyclodextrin as substrate, 0.8 M KCl646801
227.2-Thermus sp.-beta-cyclodextrin as substrate, 0.6 M KCl646801
242.9-Thermus sp.-beta-cyclodextrin as substrate, 0.4 M KCl646801
257.8-Thermus sp.-beta-cyclodextrin as substrate, 0.2 M KCl646801
268.6-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MnCl2707248
278-Thermus sp.-beta-cyclodextrin as substrate646801
342.7-Thermus sp.-beta-cyclodextrin as substrate, dimer646801
413.6-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM BaCl2707248
535.1-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)707248
558.6-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) methanol707248
568.8-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CoCl2707248
592.9-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) DMSO707248
604.7-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) ethanol707248
695.6-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MgCl2707248
728.8-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CaCl2707248
785.5-Thermofilum pendens-after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM AlCl3707248
additional information-Thermoplasma volcanium-specific activity of starch hydrolysis estimated for the high oligomer conformation is about 7 U/mg and for monomeric state about 110 U/mg678461
additional information-Thermus sp.-kinetic properties determined towards amylose and amylopectin in wild-type, double and triple mutant enzymes, bicinchonimate method, determination of reducing sugars678795
additional information-Bacillus thermoalkalophilusQ68KL3kinetic properties determined in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling679745
additional information-Geobacillus stearothermophilusP19531kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method680324
additional information-Lactobacillus gasseri-catalytic activity of wild-type LGMA and recombinant rLGMA tested in liquid and solid media, kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method, reaction at pH 6.5 for 13.5 h at 50°C, yields of 53.1% obtained681349
additional information-Bacillus sp.A7DWA8kinetic mechanism for recombinant enzyme MAUS149 shown, determined by measuring the amount of reducing sugars released during incubation with starch using the dinitrosalicylic acid method, substrate concentrations ranging from 1 to 7.5 g/ml for starch and from 0.5 to 4 g/l for cyclodextrin and pullulan681861

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4-Bacillus sp.-or pH 5.0, assay at693292
5-Lactobacillus gasseri-recombinant rLGMA681349
5-Bacillus sp.-or pH 4.0, assay at693292
5.3-Geobacillus stearothermophilus--646794
5.5-Thermofilum pendens--707248
6-Geobacillus stearothermophilusP19531assay at, 50 mM sodium citrate buffer680324
6-Geobacillus stearothermophilus-assay at710128
6.5-Bacillus sp.A7DWA8maximal activity, effect of pH on activity studied at 40°C using 50 mM buffers with different pH values ranging from 3.5 to 10681861
6.5-Bacillus sp.A7DWA8wild type enzyme714495
7-Geobacillus caldoxylosilyticusC0LZ63-710449
8-Bacillus thermoalkalophilus--663819
8-Bacillus thermoalkalophilusQ68KL3thermostability tested at679745

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3.57Geobacillus stearothermophilus-about 65% of activity maximum at pH 3.5, about 35% of activity maximum at pH 7.3646794
56.5Thermofilum pendens-more than 50% of the maximum activity is retained in the range between pH 5.0 and pH 6.5707248
59.5Bacillus sp.A7DWA8more than 80% of enzyme activity retained at pH ranges from 5 to 7, recombinant maltogenic amylase stable at pH ranging from 5 to 9.5 and mainly between 6 and 8681861
69Geobacillus caldoxylosilyticusC0LZ63activity range, profile, overview710449

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
40-Bacillus sp.A7DWA8maximal activity, effect of temperature on activity investigated in a 50 mM sodium phosphate buffer at pH 6.5 using different temperatures ranging from 10°C to 60°C681861
40-Bacillus sp.A7DWA8-714495
45-Thermus sp.-truncated mutant ThMA-DELTA124646801
50-Geobacillus stearothermophilusP19531activity assay at680324
50-Geobacillus stearothermophilus-assay at710128
50-Geobacillus caldoxylosilyticusC0LZ63-710449
55-Lactobacillus gasseri-hydrolysis of beta-cyclodextrin, starch and pullulan664997
55-Thermus sp.-assay at, wild-type, double and triple mutant enzymes analyzed678795
55-Geobacillus stearothermophilusP19531synthesis reaction performed for 12 h using 500 units/g substrate for transgylcosylation680324
55-Lactobacillus gasseri-recombinant rLGMA681349
60-Geobacillus stearothermophilus--646794, 646797
60-Thermus sp.--646797, 646801
60-Thermus sp.-wild-type646805
60-Bacillus sp.-assay at693292
70-Bacillus thermoalkalophilus--663819
70-Thermus sp.-mutant R26Q/S169N/I333V/A398V/Q411L/P453L665335
70-Bacillus thermoalkalophilusQ68KL3wild-type enzyme679745
75-Thermus sp.-ThMA-DM, highly thermostable mutant enzyme646805
75-Thermus sp.-mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L665335
80-Bacillus thermoalkalophilusQ68KL3mutants III-1 and III-2679745
95-Thermofilum pendens--707248

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1060Bacillus sp.A7DWA8kinetics shown, more than 50% of activity retained at the temperature range of 10–50°C, rapid decrease in activity above 60°C681861
2080Geobacillus stearothermophilus-about 20% of activity maximum at 30°C, about 60% of activity maximum at 80°C646794
3060Lactobacillus gasseri-30°C: about 20% of maximal activity with starch, about 25% of maximal activity with beta-cyclodextrin and about 35% of maximal activity with pullulan, 60°C: about 40% of maximal activity with pullulan, about 50% of maximal activity with starch anf about 80% of maximal activity with beta-cyclodextrin664997
3080Geobacillus caldoxylosilyticusC0LZ63profile, overview710449
7580Thermoplasma volcanium-high thermostability, dependent on oligomer structure of the enzyme, optimal activity at 75°C and 80°C for beta-cyclodextrin and soluble starch, half-lifes of 61 min at 75°C and of 24 min at 80°C678461
80105Thermofilum pendens-at 105°C, almost 50% of the maximum activity is detected707248

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
8.5-Geobacillus stearothermophilus-determined by thin layer gel-electrofocusing646794

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
culture fluidLactobacillus gasseri-activity tested in both, liquid and solid media681349Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytoplasmBacillus subtilis--5737646799Manually annotated by BRENDA team
extracellularLactobacillus gasseri-secretion-681349Manually annotated by BRENDA team
intracellularBacillus subtilis--5622646799Manually annotated by BRENDA team
intracellularLactobacillus gasseri--5622664997Manually annotated by BRENDA team
intracellularBacillus sp.A7DWA8recombinant enzyme MAUS1495622681861Manually annotated by BRENDA team
additional informationGeobacillus caldoxylosilyticusC0LZ63the enzyme sequence contains no signal sequence-710449Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1qho, downloadSCOP (1qho)CATH (1qho)Geobacillus stearothermophilus
1qhp, downloadSCOP (1qhp)CATH (1qhp)Geobacillus stearothermophilus
4aee, downloadSCOP (4aee)CATH (4aee)Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
64000-Bacillus subtilis-SDS-PAGE646799
65000-Lactobacillus gasseri-SDS-PAGE, difference in molecular masses due to the presence of the six-histidine tag and two additional amino acids681349
66000-Thermus sp.-SDS-PAGE, recombinant and wild-type protein678795
66630-Lactobacillus gasseri-deduced from sequence681349
67500-Bacillus sp.A7DWA8each of the two subunits of the dimer681861
68000-Thermus sp.-gel filtration646801
68830-Bacillus subtilis-predicted from nucleotide sequence data646799
68900-Bacillus subtilis-MALDI-TOF-MS spectra646799
70000-Geobacillus stearothermophilus-SDS-PAGE646794
72060-Thermoplasma volcanium-MALDI-TOF678461
72090-Thermoplasma volcanium-deduced from sequence678461
94000112000Thermus sp.-gel filtration646801
109000-Bacillus subtilis-native BbmA, gel filtration646799
135000-Bacillus sp.A7DWA8SDS-PAGE, gel filtration681861
211000-Lactobacillus gasseri-gel filtration664997

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Thermofilum pendens-x * 74000, SDS-PAGE; x * 74252, calculated from amino acid sequence707248
?Geobacillus caldoxylosilyticusC0LZ63x * 70030, sequence calculation710449
?Bacillus sp.A7DWA8x * 67500, SDS-PAGE714495
dimerBacillus subtilis-2 * 64000, monomer-dimer equilibrium, molar ratio 3:2, SDS-PAGE646799
dimerThermus sp.-2 * 68000, monomer/dimer equilibrium, ultracentrifugation646801
dimerThermus sp.--646803
dimerBacillus thermoalkalophilus-monomer:dimer equilibrium with a molar ratio of 54:46 in 50 mM glycine-NaOH buffer pH 8.0663819
dimerBacillus sp.A7DWA82 * 67500, SDS-PAGE681861
homodimerThermus sp.--646797, 646801
homodimerThermus sp.-SDS-PAGE678795
monomerBacillus subtilis-monomer-dimer equilibrium, molar ratio 3:2646799
monomerThermus sp.-1 * 68000, monomer/dimer equilibrium, ratio 48:52, ultracentrifugation; truncated mutant ThMAdelta124 exists only as a monomeric form646801
monomerBacillus thermoalkalophilus-monomer:dimer equilibrium with a molar ratio of 54:46 in 50 mM glycine-NaOH buffer pH 8.0663819
oligomerThermoplasma volcanium-recombinant protein, high oligomer in solution, dissociation into dimer and monomer mixture by a high concentration of NaCl678461
tetramerLactobacillus gasseri-4 * 65000, SDS-PAGE664997

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Geobacillus stearothermophilus-646796, 646797
crystals obtained by vapor diffusion, space group P6(1), cell dimensions of a = b = 118.04 A, c = 266.88 AThermus sp.-646797
mutant E357L, space group P6(1), a = b = 119.09, c = 270.20Thermus sp.-646803

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4.55.5Geobacillus stearothermophilus-stable646794
additional information-Bacillus sp.A7DWA8determined in different buffers ranging from pH 5 to pH 10 for 12 h at 4°C followed by activity assay681861

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5055Bacillus sp.A7DWA8after incubation for 2 h at 50°C, the wild type enzyme retains 35% of its initial activity. The wild type enzyme has a half-life of 15 min at 55°C714495
6070Geobacillus stearothermophilus-stable at pH 5.5 at 60°C, 25% loss of activity at 70°C646794
60-Thermus sp.-truncated mutant ThMA-DELTA124 unstable646801
64-Bacillus sp.-Tm of Novamyl wild-type at pH 4.0693292
75-Bacillus sp.-Tm of variant NM447 at pH 4.0693292
77-Bacillus thermoalkalophilus-Tm-value at pH 8 is 76.7°C663819
78-Bacillus thermoalkalophilusQ68KL3half-life of mutant III-1 about 20 times greater than half-life of the wild-type at 78°C679745
80-Thermus sp.-ThMA-DM, highly thermostable mutant enzyme, half-life 172 min, wild type enzyme completely inactivated in less than 1 min646805
80-Bacillus thermoalkalophilusQ68KL3half-life of mutant III-2 is 568 min, half-life of the wild-type is below 1 min at 80°C679745
80-Bacillus sp.-the variants NM447 and NM319 retain 67 and 40% specific activity following a 25-min incubation, respectively693292
82-Thermus sp.-Tm-value of mutant R26Q/S169N/I333V/A398V/Q411L/P453L is 81.5°C665335
83-Bacillus sp.-Tm of Novamyl wild-type at pH 5.0693292
85100Thermofilum pendens-purified enzyme is extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. The enzyme retains about 80% relative activity after 60 min of incubation at 85°C and 90°C, about 50% relative activity after 60 min of incubation at 95°C, and about 25% relative activity after 60 min of incubation at 100°C707248
85-Thermus sp.-Tm-value of mutant enzyme R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L, Tm-value decreases to 79.9°C in presence of EDTA. Tm-value increases to 87.4°C in presence of CaCl2665335
88-Bacillus sp.-TD of variant NM447 at pH 4.0, an increase of 10°C relative to the wild-type Novamyl693292
95-Bacillus sp.-Tm of variant NM447 at pH 5.0693292
210-Geobacillus stearothermophilus-baking at 210°C for 40 min leaves the enzyme active698428
additional information-Thermoplasma volcanium-high thermostability, half-lives of thermal inactivation and melting temperature tested678461
additional information-Bacillus thermoalkalophilusQ68KL3half-lives determined at 75°C, 78°C, 80°C, and 85°C, melting temperatures of mutants III-1 and III-2 determined by differential scanning calorimetry increased by 6.1°C and 11.4°C, respectively, hydrogen bonding, hydrophobic interaction, electrostatic interaction, proper packing, and deamidation predicted as mechanisms for enhanced thermostability in the mutant enzymes679745
additional information-Bacillus sp.A7DWA8kinetics shown, stable at 45°C for 90 min, half-life duration of 18 min at 55°C681861
additional information-Bacillus sp.-NM404 and NM398 has modest improvements in thermal stability, whereas NM326 shows no significant improvement in thermal stability693292

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
DMSOThermofilum pendens-enzyme activity increases to 136% in the presence of 10% (v/v) DMSO707248
EthanolThermofilum pendens-enzyme activity increases to 113% in the presence of 10% (v/v) ethanol707248
MethanolThermofilum pendens-enzyme activity increases to 104.4% in the presence of 10% (v/v) methanol707248

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
mutagenic PCR fragment purification with Quiaquick Gel Extract kit, and agarose electrophoresis, then cloned into plasmid pHP13amp, fermentation in bioreactors, enzyme variants purified on alpha-cyclodextrin coupled to agarose column, corroborated by SDS-PAGE; recombinant protein, the variants NM319, NM326, NM398, NM404, and NM447 are grown in fermenters and the expressed enzymes are purifiedBacillus sp.-693292
recombinant protein, from cell crude extracts with a yield of 23%Bacillus sp.A7DWA8681861
wild-type and mutant enzymesBacillus thermoalkalophilusQ68KL3679745
His-tagged protein purified via Ni-NTA colummnsGeobacillus stearothermophilusP19531680324
recombinant enzymeGeobacillus stearothermophilus-646802
His-tagged recombinant protein purified via Ni-NTA colummnsLactobacillus gasseri-681349
recombinantLactobacillus gasseri-664997
Ni-NTA column chromatographyThermofilum pendens-707248
recombinant protein, gel filtrationThermoplasma volcanium-678461
-Thermus sp.-665335
mutant E357LThermus sp.-646803
purification of ThMA variants with N-terminal six-histidines by nickel-nitrilotriacetic acid column chromatographyThermus sp.-699487
truncated mutant ThMA-DELTA124Thermus sp.-646801
wild-type and mutant enzyme A290IThermus sp.-664208
wild-type and mutant enzymesThermus sp.-646800, 646805
wild-type and recombinant protein, gel filtrationThermus sp.-678795

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coli DH5alpha using expression vectors pBMS1-4, open reading frame of 1749 bp encoding a protein of 582 residues, low sequence similarity of 60% to maltogenic amylase of Thermus sp., four known conserved regions at position 241 to 246, 324 to 331, 355 to 360, and 418 to 423 identifiedBacillus sp.A7DWA8681861
Novamyl libraries are iniatially made in Escherichia coli, then shuttled and expressed in the screen host Bacillus subtilis. The variants NM319, NM326, NM398, NM404, and NM447 are grown in fermenters, and the expressed enzymes are purified and tested for anti-staling properties in standard bread pH 5.5-5.9 and/or bread at sourdough (pH 4.0-4.3); shuffled libraries of Novamyl are produced in in Escherichia coli, shuttled to screening host B. subtilis strain A164 delta 5, plasmid pHP13ampBacillus sp.-693292
cloned and expressed in Escherichia coliBacillus subtilis-646799
-Bacillus thermoalkalophilus-663819
expressed in Escherichia coli MC1061, His-tagged, wild-type and mutant proteinBacillus thermoalkalophilusQ68KL3679745
gene GcaTK4MA, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression of His6-tagged TK4MA in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM101Geobacillus caldoxylosilyticusC0LZ63710449
cloned and overexpressed in Escherichia coliGeobacillus stearothermophilus-646802
gene amyM cloned in Escherichia coli, transferred with plasmid pDN400 carrier to a Bacillus subtilis 168 host and expressed heterogenouslyGeobacillus stearothermophilus-646794, 646795
heterogenous expression in Bacillus subtilis host strain ISW1214Geobacillus stearothermophilusP19531680324
amplified in Escherichia coli DH5alpha, heterogenous expression in Lactococcus lactis MG1363, P170 expression system for production of recombinant LGMALactobacillus gasseri-681349
expression in Escherichia coliLactobacillus gasseri-664997
expressed in Escherichia coli BL21(DE3) cellsThermofilum pendens-707248
expressed in Escherichia coli MC1061Thermoplasma volcanium-678461
-Thermus sp.-646797
cloned and expressed in Escherichia coli BL21 (DE3)Thermus sp.-646806
cloned and overproduced in Escherichia coli MC1061Thermus sp.-646803
cloning and expression in Escherichia coli MC 1061 with p6xHTMX, transformants grown in Luria-Bertani medium with ampicillin at 37°CThermus sp.-699487
expressed in Escherichia coli MC1061, His-tagged, recombinant proteinThermus sp.-678795
wild-type and mutant ThMAs expressed in Escherichia coliThermus sp.-646800

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D30A/K40R/D261GBacillus sp.-Novamyl variant NM398, similar to wild-type at pH 4.0; variant NM398, medium thermotolerance due to D261G mutation693292
F188L/D261G/T288PBacillus sp.-Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.; variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min693292
G312ABacillus sp.A7DWA8the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme714495
G312A/K436RBacillus sp.A7DWA8the half-life time at 55°C increase from 15 to 25 min for the double mutant714495
N115D/F188LBacillus sp.-Novamyl variant NM319, similar to wild-type at pH 4.0, at pH 5.5 the variant outperform wild-type Novamyl, significantly more thermally stable that wild-type; variant NM319, most thermotolerant, probably due to F188L mutation, but reduced activity, improved anti-staling performance in application test, about 40% activity retained after incubation at 80°C at pH 4.3 for 25 min693292
T142ABacillus sp.-Novamyl variant NM326, similar to wild-type at pH 4.0; variant NM326, inducing 20% activity increase and 50% thermal stability increase693292
T142A/D261G/N327S/K425E/K520R/N5951Bacillus sp.-variant NM404, medium thermotolerance due to D261G mutation693292
T142A/D261G/N327S/K425E/K520R/N595IBacillus sp.-Novamyl variant NM404, similar to wild-type at pH 4.0693292
N147D/F195L/N263S/D311G/A344V/F397S/N508DBacillus thermoalkalophilusQ68KL3mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated679745
A290IThermus sp.-mutant enzyme A290I produces mostly maltose from maltotetraose, while wild-type enzyme produces glucose as well as maltose. kcat/KM of mutant enzyme 290I for maltose is 48times less than that of wild-type enzyme. kcat/Km for maltotriose is 18.5fold lower than wild-type enzyme. kcat/Km for maltotetraose is 2.9fold lower than wild-type enzyme. kcat/Km for maltopentaose is 2.5fold lower than wild-type enzyme. kcat/Km for maltohexaose is 1.9fold lower than wild-type enzyme. kcat/Km for maltoheptaose is 4.7fold lower than wild-type enzyme664208
A330G/N331C/E332CThermus sp.-F-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330G/N331G/E332CThermus sp.-C-20, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330G/N331G/E332GThermus sp.-G-91, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose699487
A330G/N331G/E332SThermus sp.-G-22, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330G/N331P/E332GThermus sp.-C-43, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330G/N331V/E332GThermus sp.-G-90, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330M/N331G/E332CThermus sp.-B-96, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A330S/N331AThermus sp.-F-80, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose699487
A330S/N331G/E332TThermus sp.-K-37, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodexxtrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
A398VThermus sp.-random mutagenesis, using DNA shuffling646805
E332DThermus sp.-site-directed mutagenesis, significantly decreased transglycosylation activity646800
E332HThermus sp.-site-directed mutagenesis, replacing Glu 332 with histidine reduces transglycosylation activity significantly, but enhances hydrolysis activity on alpha-(1,3)-, alpha-(1,4)- and alpha-(1,6) glycosidic bonds relative to the wild-type646800
E332QThermus sp.-site-directed mutagenesis646800
E357LThermus sp.-site-directed mutagenesis646803
G50I/D109EThermus sp.-double mutation, two main residues of the catalytic binding pocket, site-directed mutagenesis678795
G50I/D109E/V431IThermus sp.-triple mutation of three main residues of the catalytic binding pocket, site-directed mutagenesis678795
I333VThermus sp.-random mutagenesis, using DNA shuffling646805
N331S/E332GThermus sp.-I-69, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
P453LThermus sp.-random mutagenesis, using DNA shuffling646805
Q411LThermus sp.-random mutagenesis, using DNA shuffling646805
R26QThermus sp.-random mutagenesis, using DNA shuffling646805
R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453LThermus sp.-mutant enzyme shows highly improved thermostability and catalytic activity in presence of Ca2+665335
S169NThermus sp.-random mutagenesis, using DNA shuffling646805
V329A/A330C/N331G/E332VThermus sp.-A-39, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329A/A330G/N331V/E332AThermus sp.-G-13, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329A/N331LThermus sp.-B-4, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type699487
V329C/N331H/E332RThermus sp.-D-3, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329F/A330T/N331G/E332WThermus sp.-I-70, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329G/A330L/N331V/E332YThermus sp.-H-16, slightly higher activity with cyclodextrin, pullulan, and starch, reduced activities with maltotriose, and acarbose, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type, similar transglysocylation pattern as wild-type699487
V329I/A330G/N331WThermus sp.-C-56, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329S/A330C/N331S/E332PThermus sp.-A-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329S/A330G/N331DThermus sp.-K-33, strong reduction of all substrate hydrolyzing activities, products of acarbose hydrolization are glucose, maltose, and acarviosine instead of only glucose and carviosine-glucose as in the wild-type reaction, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: very little amount of transfer products, with acarbose significant amount of acarviosine and maltose699487
V329S/A330G/N331G/E332VThermus sp.-E-74, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
V329T/A330C/N331T/E332VThermus sp.-E-50, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type699487
W47AThermus sp.-site-directed mutagenesis646803
K436RBacillus sp.A7DWA8the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme714495
additional informationBacillus sp.-mutagenesis is induced by error-prone PCR, mutagenic fragments screened for thermostable variants (80°C) at low pH 4.3, most thermostable variants show a decreased activity to the wild-type enzyme693292
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375TBacillus thermoalkalophilusQ68KL3additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown679745
additional informationGeobacillus stearothermophilus-tapioca starch is modified using branching enzyme, BE, isolated from, Bacillus subtilis strain 168, and Bacillus stearothermophilus maltogenic amylase, BSMA. BE cleaves alpha-1,4 linkages of amylose and amylopectin, and moiety of glycosyl residues are transferred to another amylose and amylopectin to produce branched glucan and branching enzyme-treated tapioca starch by forming alpha-1,6 branch linkages. The product is further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points, overview710128
M375TThermus sp.-random mutagenesis, using DNA shuffling646805
additional informationThermus sp.-Random substitutions of amino acid residues Val329, Ala330, Asn331, and Glu332 that are forming an extra sugar-binding space with combinatorial saturation mutagenesis technique: substrate specificity, hydrolysis pattern, and transglycosylation activity of ThMA are modulated by these mutations. Activity assays with substrates: soluble starch, pullulan, beta-cyclodextrin, maltotriose, and acarbose at 60°C, pH 6.0 sodium-acetate buffer699487

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
food industryBacillus sp.-Novamyl is currently used in the baking industry as an anti-staling agent in breads at neutral or near neutral pH. It is rapidly inactivated during the baking process. Relative to the Novamyl wild-type the variants exhibit more than 10°C increase in thermal stability at pH 4.5, improving the anti-staling effect; wild-type enzyme is not thermostable at low pH as encountered in recipes such as sourdough and rye dough, recombined variants increase thermal stability more than 10°C at pH 4.0-4.5, application test is performed with wheat flour dough at pH 5.5-5.9 and sourdough at pH 4.0-4.3 baked at 230°C for 22 min, firmness and elasticity tested at days 1, 3, and 7 after baking and vacuum packing693292
nutritionBacillus subtilis-transglycosylation activity of BbmA can be applied for the preparation of branched oligosaccharide mixtures, which are used as low calorie sweeteners or humectants646799
food industryGeobacillus stearothermophilus-impact on crumb texture, and amylopectin recrystallization: reduction of bread firmness increase during storage compared to control or other amylases, bread firmness is slightly increased at day 0, firmness at day 6 is 9.00, 7.15, and 4.40 N (compared to 16.85 N in control) for BStA dosages of 5.05, 10.1, and 20.2 enzyme units/g flour, respectively, though highest dosage leads to sticky dough and low resilience. Enzyme unit = amount of enzyme releasing 1 micromol maltose/minute at 40°C, pH 6.0, 100 mM sodium maleate buffer with 5.0 mM CaCl2. BStA almost completely suppresses amylopectin recrystallization. Hot water extractable dextrin content is increased largely by BStA698428
medicineGeobacillus stearothermophilus-pierarin (daidzein 8-C-glucoside), can be used to treat coronary heart disease, cardiac infarction, problems in ocular blood flow, sudden deafness, and alcoholism. However puerarin cannot be given by injection due to its low solubility in water. To increase its solubility, puerarin is transglycosylated using Bacillus stearothermophilus maltogenic amylase. Two major transfer products are alpha-D-glucosyl-(1,6)-puerarin and alpha-D-maltosyl-(1,6)-puerarin. The solubility of the transfer products is 14 and 168 times higher than that of puerarin, respectively664522
nutritionGeobacillus stearothermophilus-utilization of starch from corn, cereals, potatoes, sorghum and other plants as valuable raw material for the production of glucose, fructose, oligosaccharides, and alcohol646795
nutritionGeobacillus stearothermophilus-production of isomaltosaccharides with various compositions and useful properties is in great demand in the starch industry, efficient process with cooperative action of maltogenic amylase and alpha-glucanotransferase from Thermotoga maritima646802
pharmacologyGeobacillus stearothermophilus-increasing interest for pure maltose in the pharmaceutical industry, maltose may be used instead of D-glucose for intravenous feeding646794
synthesisGeobacillus stearothermophilus-thermostable maltogenic amylase with industrial potential, suitable for producing high maltose syrups from liquefied starch646794
synthesisGeobacillus stearothermophilus-industrial processes use heat-stable alpha-amylase for degrading starch646795
synthesisGeobacillus stearothermophilus-formation of maltosyl-tagatose from D-tagatose and maltotriose with maltogenic amylase. Glucosyl-tagatose is produced from maltosyl-tagatose by removal of a glucosyl moiety by glucoamylase. Glucosyl-tagatose has potential as a low-calorie sweetener and cryostabilizer666955
synthesisGeobacillus stearothermophilusP19531production of highly branched amylopectin and amylose from enzymatically modified rice starch680324
synthesisLactobacillus gasseri-production of branched maltooligosaccharide681349
biotechnologyThermus sp.-natural design of the transglycosylation activtiy of the enzyme at high concentrations of acceptor sugar molecules may now be altered for biotechnological applications to produce branched oligosaccharides with higher efficiency646797
biotechnologyThermus sp.-producing enzymes with modified substrate specificity, hydrolysis, and transglycosilation activities, as a way to produce specific functional carbohydrate materials699487
medicineThermus sp.-synthesis of acarvisione-simmondsin, a novel compound with both antiobesity and hypoglycemic activity646804
synthesisThermus sp.-heterologous protein expression in Escherichia coli may contribute to better industrial production of maltogenic amylase646806

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
646794Outtrup, H.; Norman, B.E.Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniquesStarch Staerke36405-4111984Geobacillus stearothermophilus-
646795Diderichsen, B.; Christiansen, L.Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilusFEMS Microbiol. Lett.5653-601988Geobacillus stearothermophilus-
646796Dauter, Z.; Dauter, M.; Brzozowski, A.M.; Christensen, S.; Borchert, T.V.; Beier, L.; Wilson, K.S.; Davies, G.J.X-ray structure of Novamyl, the five-domain 'maltogenic' alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolutionBiochemistry388385-83921999Geobacillus stearothermophilus PubMed
646797Kim, J.S.; Cha, S.S.; Kim, H.J.; Kim, T.J.; Ha, N.C.; Oh, S.T.; Cho, H.S.; Cho, M.J.; Kim, M.J.; Lee, H.S.; Kim, J.W.; Choi, K.Y.; Park, K.H.; Oh, B.H.Crystal structure of a maltogenic amylase provides insights into a catalytic versatilityJ. Biol. Chem.27426279-262861999Geobacillus stearothermophilus, Thermus sp. PubMed
646798Kim, M.J.; Lee, S.B.; Lee, H.S.; Lee, S.Y.; Baek, J.S.; Kim, D.; Moon, T.W.; Robyt, J.F.; Park, K.H.Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucoseArch. Biochem. Biophys.371277-2831999Geobacillus stearothermophilus PubMed
646799Cho, H.Y.; Kim, Y.W.; Kim, T.J.; Lee, H.S.; Kim, D.Y.; Kim, J.W.; Lee, Y.W.; Leed, S.; Park, K.H.Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2Biochim. Biophys. Acta1478333-3402000Bacillus subtilis PubMed
646800Kim, T.J.; Park, C.S.; Cho, H.Y.; Cha, S.S.; Kim, J.S.; Lee, S.B.; Moon, T.W.; Kim, J.W.; Oh, B.H.; Park, K.H.Role of the glutamate 332 residue in the transglycosylation activity of ThermusMaltogenic amylaseBiochemistry396773-67802000Thermus sp. PubMed
646801Kim, T.J.; Nguyen, V.D.; Lee, H.S.; Kim, M.J.; Cho, H.Y.; Kim, Y.W.; Moon, T.W.; Park, C.S.; Kim, J.W.; Oh, B.H.; Lee, S.B.; Svensson, B.; Park, K.H.Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibriumBiochemistry4014182-141902001Thermus sp. PubMed
646802Lee, H.S.; Auh, J.H.; Yoon, H.G.; Kim, M.J.; Park, J.H.; Hong, S.S.; Kang, M.H.; Kim, T.J.; Moon, T.W.; Kim, J.W.; Park, K.H.Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) productionJ. Agric. Food Chem.502812-28172002Geobacillus stearothermophilus PubMed
646803Lee, H.S.; Kim, M.S.; Cho, H.S.; Kim, J.I.; Kim, T.J.; Choi, J.H.; Park, C.; Oh, B.H.; Park, K.H.Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each otherJ. Biol. Chem.27721891-218972002Thermus sp. PubMed
646804Baek, J.S.; Kim, H.Y.; Abbott, T.P.; Moon, T.W.; Lee, S.B.; Park, C.S.; Park, K.H.Acarviosine-simmondsin, a novel compound obtained from acarviosine-glucose and simmondsin by Thermus maltogenic amylase and its in vivo effect on food intake and hyperglycemiaBiosci. Biotechnol. Biochem.67532-5392003Thermus sp. PubMed
646805Kim, Y.W.; Choi, J.H.; Kim, J.W.; Park, C.; Cha, H.; Lee, S.B.; Oh, B.H.; Moon, T.W.; Park, K.H.Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistanceAppl. Environ. Microbiol.694866-48742003Thermus sp. PubMed
646806Jung, H.M.; Park, K.H.; Kim, S.Y.; Lee, J.K.L-Glutamate enhances the expression of Thermus maltogenic amylase in Escherichia coliBiotechnol. Prog.2026-312004Thermus sp.-
663819Cheong, K.; Tang, S.; Cheong, T.; Cha, H.; Kim, J.; Park, K.Thermostable and alkalophilic maltogenic amylase of Bacillus thermoalkalophilus ET2 in monomer-dimer equilibriumBiocatal. Biotransform.2379-872005Bacillus thermoalkalophilus-
664208Park, S.; Cha, H.; Kang, H.; Shim, J.; Woo, E.; Kim, J.; Park, K.Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMABiochim. Biophys. Acta1751170-1772005Thermus sp. PubMed
664522Li, D.; Park, S.H.; Shim, J.H.; Lee, H.S.; Tang, S.Y.; Park, C.S.; Park, K.H.In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylaseCarbohydr. Res.3392789-27972004Geobacillus stearothermophilus PubMed
664997Oh, K.W.; Kim, M.J.; Kim, H.Y.; Kim, B.Y.; Baik, M.Y.; Auh, J.H.; Park, C.S.Enzymatic characterization of a maltogenic amylase from Lactobacillus gasseri ATCC 33323 expressed in Escherichia coliFEMS Microbiol. Lett.252175-1812005Lactobacillus gasseri PubMed
665335Kim, Y.; Kim, D.; Kim, M.; Cha, H.; Park, C.; Moon, T.; Park, K.Engineering Thermus maltogenic amylase with improved thermostability: Probing the role of the conserved calcium binding site in cyclodextrin-degrading enzymesJ. Appl. Glycosci.527-132005Thermus sp.-
666955Roh, H.; Kang, S.; Lee, H.; Kim, D.; Byun, S.; Lee, S.; Park, K.Transglycosylation of tagatose with maltotriose by Bacillus stearothermophilus maltogenic amylase (BSMA)Tetrahedron1677-822005Geobacillus stearothermophilus-
678461Kim, J.W.; Kim, Y.H.; Lee, H.S.; Yang, S.J.; Kim, Y.W.; Lee, M.H.; Kim, J.W.; Seo, N.S.; Park, C.S.; Park, K.H.Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1Biochim. Biophys. Acta1774661-6692007Thermoplasma volcanium PubMed
678795Park, S.H.; Kang, H.K.; Shim, J.H.; Woo, E.J.; Hong, J.S.; Kim, J.W.; Oh, B.H.; Lee, B.H.; Cha, H.; Park, K.H.Modulation of substrate preference of thermus maltogenic amylase by mutation of the residues at the interface of a dimerBiosci. Biotechnol. Biochem.711564-15672007Thermus sp. PubMed
679745Tang, S.Y.; Le, Q.T.; Shim, J.H.; Yang, S.J.; Auh, J.H.; Park, C.; Park, K.H.Enhancing thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2 by DNA shufflingFEBS J.2733335-33452006Bacillus thermoalkalophilus PubMed
680324Lee, C.K.; Le, Q.T.; Kim, Y.H.; Shim, J.H.; Lee, S.J.; Park, J.H.; Lee, K.P.; Song, S.H.; Auh, J.H.; Lee, S.J.; Park, K.H.Enzymatic synthesis and properties of highly branched rice starch amylose and amylopectin clusterJ. Agric. Food Chem.56126-1312008Geobacillus stearothermophilus PubMed
681349Cho, M.H.; Park, S.E.; Lee, M.H.; Ha, S.J.; Kim, H.Y.; Kim, M.J.; Lee, S.J.; Madsen, S.M.; Park, C.S.Extracellular secretion of a maltogenic amylase from Lactobacillus gasseri ATCC33323 in Lactococcus lactis MG1363 and its application on the production of branched maltooligosaccharidesJ. Microbiol. Biotechnol.171521-15262007Lactobacillus gasseri PubMed
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693292Jones, A.; Lamsa, M.; Frandsen, T.P.; Spendler, T.; Harris, P.; Sloma, A.; Xu, F.; Nielsen, J.B.; Cherry, J.R.Directed evolution of a maltogenic alpha-amylase from Bacillus sp. TS-25J. Biotechnol.134325-3332008Bacillus sp. PubMed
698428Goesaert, H.; Leman, P.; Bijttebier, A.; Delcour, J.A.Antifirming effects of starch degrading enzymes in bread crumbJ. Agric. Food Chem.572346-23552009Geobacillus stearothermophilus PubMed
699487Oh, S.W.; Jang, M.U.; Jeong, C.K.; Kang, H.J.; Park, J.M.; Kim, T.J.Modulation of hydrolysis and transglycosylation activity of Thermus maltogenic amylase by combinatorial saturation mutagenesisJ. Microbiol. Biotechnol.181401-14072008Thermus sp. PubMed
707248Li, X.; Li, D.; Yin, Y.; Park, K.H.Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activityAppl. Microbiol. Biotechnol.851821-18302010Thermofilum pendens PubMed
710128Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinusNew Biotechnol.27300-3072010Geobacillus stearothermophilus PubMed
710449Kolcuoglu, Y.; Colak, A.; Faiz, O.; Belduz, A.Cloning, expression and characterization of highly thermo- and pH-stable maltogenic amylase from a thermophilic bacterium Geobacillus caldoxylosilyticus TK4Process Biochem.45821-8282010Geobacillus caldoxylosilyticus-
714495Ben Mabrouk, S.; Aghajari, N.; Ben Ali, M.; Ben Messaoud, E.; Juy, M.; Haser, R.; Bejar, S.Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutionsBiores. Technol.1021740-17462011Bacillus sp. PubMed
714654Bijttebier, A.; Goesaert, H.; Delcour, J.Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin populationCarbohydr. Res.345235-2422010Geobacillus stearothermophilus PubMed
715074Li, X.; Li, D.; Park, S.; Gao, C.; Park, K.; Gu, L.Identification and antioxidative properties of transglycosylated puerarins synthesised by an archaeal maltogenic amylaseFood Chem.124603-6082011Thermofilum pendens-

LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.133)
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