3.2.1.133: glucan 1,4-alpha-maltohydrolase
This is an abbreviated version!
For detailed information about glucan 1,4-alpha-maltohydrolase, go to the full flat file.
Word Map on EC 3.2.1.133
-
3.2.1.133
-
amylases
-
baking
-
bake
-
food industry
-
synthesis
-
cgtases
-
maltooligosaccharide
-
amylopectin
-
enzyme-total
-
alpha-amylases
-
novozymes
-
staling
-
beta-cds
-
crumb
-
stale
-
antistaling
-
nutrition
-
biotechnology
-
medicine
-
degradation
-
pharmacology
- 3.2.1.133
- amylases
-
baking
-
bake
- food industry
- synthesis
- cgtases
- maltooligosaccharide
- amylopectin
-
enzyme-total
- alpha-amylases
-
novozymes
-
staling
- beta-cds
-
crumb
-
stale
-
antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
Reaction
Synonyms
alpha-amylase, AmyB, BbmA, BSMA, BSTA, BTMA, CAZy-GH13, glucan 1,4-alpha-maltohydrolase, glucan-1,4-alpha-maltohydrolase, Gt-MamyIII, LGMA, MAase, MABS, MAG1, maltogenase L, maltogenic alpha-amylase, maltogenic amylase, maltose-forming alpha-amylase, MAmy, MAUS149, More, NM319, NM326, NM398, NM404, NM447, Novamyl, PSMA, Smar_0613, SMMA, TCMA, Thermus maltogenic amylase, ThMA, TK4MA
ECTree
3.2.1.133 glucan 1,4-alpha-maltohydrolaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
poor substrate
-
-
?
4-nitrophenyl maltopyranoside + H2O
4-nitrophenol + maltose
excellent substrate
-
-
?
alpha-(1,4)-glycosidic linked cyclodextrins + H2O
maltooligosaccharide
-
main depolymerization of outer amylopectin branches
-
-
?
alpha-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 10:1
?
alpha-Schardinger dextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
amylopectin + H2O
alpha-maltose + ?
-
hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site
-
-
?
amylopectin + H2O
fragments of amylopectin
-
main depolymerization of outer amylopectin branches
mainly 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 + H2O
fragments of amylopectin + dextrin
-
main depolymerization of outer amylopectin branches
mainly 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 + H2O
maltose + alpha-D-glucose
-
-
in 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 glucose
?
amylose + H2O
alpha-maltose + ?
-
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 amylopectin
-
-
?
beta-cyclodextrin + H2O
D-glucose + maltose + maltotriose + maltooligosaccharides
100% activity
-
-
?
D-tagatose + maltotriose
maltosyl-tagatose
-
transglycosylation
-
-
?
gamma-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
maximal activity (100%)
-
-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
-
-
main product
-
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose
-
?
maltopentaose + H2O
2 maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotetraose + H2O
maltose + 2 D-glucose
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose
-
?
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
-
-
transfer products of transglycosylation
-
?
puerarin + beta-cyclodextrin
daidzein 8-C-glucosyl-(alpha-glucosyl)n-1
-
transglycosylation activity
-
-
?
pullulan + H2O
maltose + D-glucose + panose
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
mainly maltose and glucose with relatively minor quantity of panose and other maltooligosaccharides
-
?
simmondsin + acarviosine-glucose
acarviosine-simmondsin + alpha-D-glucose
-
transglycosylation
novel compound in which acarviosine is attached to the glucose-moiety of simmondsin by an alpha-(1,6)-glycosidic linkage, with both antiobesity and hypoglycemic activity
?
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
alpha-cyclodextrin + H2O
?
80% activity compared to beta-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
high specificity for alpha-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
-
64.7% activity compared to gamma-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
-
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 action
-
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylopectin + H2O
maltose + maltotriose
-
-
wild-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 + H2O
maltose + maltotriose
-
-
wild-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
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
maltose + ?
-
high preference toward amylose compared to amylopectin
-
-
?
beta-cyclodextrin + H2O
?
-
78.1% activity compared to gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 3:1
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
hydrolytic activity
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
prefers cyclodextrins to starch or pullulan as substrate
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose + ?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
gamma-cyclodextrin + H2O
?
10% activity compared to beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
?
10% activity compared to beta-cyclodextrin
-
-
?
glycogen + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotriose + H2O
?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
maltose + D-glucose
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
pullulan + H2O
?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
pullulan + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
panose + ?
-
-
mainly hydrolyzed to panose
-
?
soluble starch + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O
maltose + ?
the enzyme displays less hydrolytic action on raw starches than on soluble starch
-
-
?
soluble starch + H2O
maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
starch + H2O
?
-
the enzyme shows a substrate hydrolysis preference for cyclodextrins over starch
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose + ?
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose + ?
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose + ?
-
exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends
-
?
starch + H2O
alpha-maltose + ?
utilization 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 determined
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
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 products
-
-
?
starch + H2O
alpha-maltose + ?
-
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 products
-
-
?
starch + H2O
alpha-maltose + ?
-
catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism
-
?
starch + H2O
maltose + ?
-
the enzyme shows higher affinity to the starch at negative pressure (-200 mbar) compared to the atmospheric pressure
-
-
?
starch + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
starch + H2O
maltose + ?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
starch + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
starch + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
additional information
?
-
the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above
-
-
?
additional information
?
-
the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme forms highly branched products from branched glucan and branching enzyme-treated tapioca starch
-
-
?
additional information
?
-
the dimeric enzyme transglycosylates hydrolytic products of G4/G5 and acarbose, while the monomeric form does not because of the lack of extra sugar-binding space formed due to dimerization
-
-
?
additional information
?
-
-
enzyme shows hydrolytic activity towards alpha-1,6-glycosidic linkage
-
-
?
additional information
?
-
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
?
additional information
?
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
?
additional information
?
-
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
?
additional information
?
-
acarbose is not cleaved by the enzyme
-
-
?
additional information
?
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
?
additional information
?
-
-
maltooligosaccharides G3-G7 show 5.4-24.1% relative activity compared to gamma-cyclodextrin
-
-
?
additional information
?
-
does not hydrolyze cyclodextrin, pullulan and acarbose
-
-
?
additional information
?
-
-
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-amylases
-
-
?
additional information
?
-
-
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 starch
-
-
?
