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Information on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase
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EC Tree
3.2.1.133 glucan 1,4-alpha-maltohydrolaseIUBMB Comments
Acts on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.
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Word Map
- 3.2.1.133
- amylases
-
baking
-
bake
- food industry
- synthesis
- cgtases
- maltooligosaccharide
- amylopectin
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enzyme-total
- alpha-amylases
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novozymes
-
staling
- beta-cds
-
crumb
-
stale
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antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
maase, novamyl, maltogenic alpha-amylase, nm404, thermus maltogenic amylase, maus149, gt-mamyiii, maltogenase l, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BbmA
BSMA
BTMA
glucan 1,4-alpha-maltohydrolase
LGMA
MAase
MAG1
maltogenic alpha-amylase
maltogenic amylase
maltose-forming alpha-amylase
MAUS149
NM319
NM447
Novamyl
PSMA
Smar_0613
SMMA
TCMA
ThMA
TK4MA
additional information
maltogenic alpha-amylase
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-
-
-
additional information
the enzyme belongs to a subclass of cyclodextrin-hydrolyzing enzymes, belonging to glycoside hydrolase family 13, GH13
additional information
the enzyme belongs to a subclass of cyclodextrin-hydrolyzing enzymes, belonging to glycoside hydrolase family 13, GH13
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(Glcalpha(1-4))n + H2O = (Glcalpha(1-4))n-2 + alpha-maltose
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
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-
-
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transglycosylation
transglycosylation
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan alpha-maltohydrolase
Acts on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.
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CAS REGISTRY NUMBER
COMMENTARY
160611-47-2
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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
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-
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
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-
?
amylopectin + H2O
fragments of amylopectin
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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
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?
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
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?
amylopectin + H2O
maltose + alpha-D-glucose
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-
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
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-
?
beta-cyclodextrin + H2O
D-glucose + maltose + maltotriose + maltooligosaccharides
100% activity
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-
?
D-tagatose + maltotriose
maltosyl-tagatose
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transglycosylation
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-
?
gamma-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
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maximal activity (100%)
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-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
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-
main product
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?
maltoheptaose + H2O
maltose + D-glucose + ?
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-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose
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?
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
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-
?
maltotetraose + H2O
maltose + 2 D-glucose
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-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose
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?
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
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-
transfer products of transglycosylation
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?
puerarin + beta-cyclodextrin
daidzein 8-C-glucosyl-(alpha-glucosyl)n-1
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transglycosylation activity
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-
?
pullulan + H2O
maltose + D-glucose + panose
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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
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?
simmondsin + acarviosine-glucose
acarviosine-simmondsin + alpha-D-glucose
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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
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transglycosylation
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-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
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-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
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hydrolysis
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-
?
alpha-cyclodextrin + H2O
?
80% activity compared to beta-cyclodextrin
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-
?
alpha-cyclodextrin + H2O
?
high specificity for alpha-cyclodextrin
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-
?
alpha-cyclodextrin + H2O
?
-
64.7% activity compared to gamma-cyclodextrin
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-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
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-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
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-
?
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
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-
?
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
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?
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
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?
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
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-
?
amylopectin + H2O
maltose + maltotriose
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-
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
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?
amylopectin + H2O
maltose + maltotriose
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-
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
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?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
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-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
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-
?
amylose + H2O
maltose + ?
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high preference toward amylose compared to amylopectin
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-
?
beta-cyclodextrin + H2O
?
-
78.1% activity compared to gamma-cyclodextrin
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-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
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-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
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-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
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-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
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-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
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-
?
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