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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
-
bake
-
baking
- food industry
- synthesis
-
enzyme-total
- alpha-amylases
- maltooligosaccharide
- amylopectin
- cgtases
-
novozymes
-
stale
- beta-cds
-
crumb
-
staling
-
antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-amylase, AmyB, BbmA, BSMA, BSTA, BTMA, CAZy-GH13, glucan 1,4-alpha-maltohydrolase, glucan-1,4-alpha-maltohydrolase, Gt-MamyIII, 
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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
-
-
-
-
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
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
transglycosylation
transglycosylation
-
-
-
-
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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
-
-
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
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
-
-
?
maltotetraose + H2O
maltose + 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
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose
-
-
mainly hydrolyzed to maltose
-
?
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 + ?
-
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
-
-
?
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
-
-
?
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
substrate determination for recombinant enzyme MAUS149
-
-
?
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
-
catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
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
maltose
-
the enzyme shows higher affinity to the starch at negative pressure (-200 mbar) compared to the atmospheric pressure
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
alpha-(1,4)-glycosidic linked cyclodextrins + H2O
maltooligosaccharide
-
main depolymerization of outer amylopectin branches
-
-
?
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
-
?
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
-
-
transfer products of transglycosylation
-
?
starch + H2O
maltose
-
the enzyme shows higher affinity to the starch at negative pressure (-200 mbar) compared to the atmospheric pressure
-
-
?
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
-
-
?
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
-
?
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
-
?
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
-
catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Ca2+
Co2+
Mg2+
Mn2+
additional information
Ca2+
-
calcium can stabilize the enzyme activity up to 50ĆĀ°C at atmospheric pressure (% of residual activities at 50, 60, and 70ĆĀ°C are 100, 4.93, 0, respectively)
Ca2+
-
mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L shows highly improved thermostability and catalytic activity in presence of Ca2+.
additional information
K+, Ni2+, Ca2+, and Ba2+ do not exert any observable effect on enzyme activity
additional information
5 mM Zn2+ has no effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
in the presence of beta-cyclodextrin the effector has a biphasic effect. While it stimulates the enzyme activity at low concentrations (with a decreasein Hill constant), it acts as allosteric inhibitor at higher concentrations
phenylmethylsulfonyl fluoride
about 2% residual activity at 1% (v/v)
maltose
in the presence of beta-cyclodextrin the effector has a biphasic effect. While it stimulates the enzyme activity at low concentrations (with a decreasein Hill constant), it acts as allosteric inhibitor at higher concentrations
additional information
not inhibited by EDTA and Tween 20
-
additional information
-
no inhibition by sulfhydryl reagents, no inhibition with p-chloromercuribenzoate or Schardinger dextrins
-
additional information
EGTA and EDTA have no observable effect on the activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
-
enzyme activity increases to 136% in the presence of 10% (v/v) DMSO
EDTA
-
increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L
ethanol
-
enzyme activity increases to 113% in the presence of 10% (v/v) ethanol
methanol
-
enzyme activity increases to 104.4% in the presence of 10% (v/v) methanol
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Lapatinib versus hormone therapy in patients with advanced renal cell carcinoma: A randomized Phase III clinical trial Ravaud A, Hawkins R, Gardner JP, von der Maase H, Zantl N, Harper P, Rolland F, Audhuy B, Machiels JP, PĆĀĆĀ©tavy F, Gore M, SchĆĀĆĀ¶ffski P, El-Hariry I, Department of Medical Oncology, HĆĀĆĀ“pital Saint AndrĆĀĆĀ©, Bordeaux, France.
Carcinoma, Renal Cell
Lapatinib versus hormone therapy in patients with advanced renal cell carcinoma: A randomized Phase III clinical trial Ravaud A, Hawkins R, Gardner JP, von der Maase H, Zantl N, Harper P, Rolland F, Audhuy B, Machiels JP, PĆĀĆĀ©tavy F, Gore M, SchĆĀĆĀ¶ffski P, El-Hariry I, Department of Medical Oncology, HĆĀĆĀ“pital Saint AndrĆĀĆĀ©, Bordeaux, France.
Hyperglycemia
Acarviosine-simmondsin, a novel compound obtained from acarviosine-glucose and simmondsin by Thermus maltogenic amylase and its in vivo effect on food intake and hyperglycemia.
Neoplasms
Application of a whole-body pharmacokinetic model for targeted radionuclide therapy to NM404 and FLT.
Seminoma
Radiotherapy versus single-dose carboplatin in adjuvant treatment of stage I seminoma: a randomised trial Oliver RT, Mason MD, Mead GM, von der Maase H, Rustin GJ, Joffe JK, de Wit R, Aass N, Graham JD, Coleman R, Kirk SJ, Stenning SP, MRC TE19 Collaborators and the EORTC 30982 Collaborators, Department of Medical Oncology, St. Bart's and the London Hospital, London, United Kingdom.
Urinary Bladder Neoplasms
Checkpoint inhibitors: the new treatment paradigm for urothelial bladder cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
alpha-cyclodextrin
pH and temperature not specified in the publication
2.68
gamma-cyclodextrin
pH and temperature not specified in the publication
0.16
beta-cyclodextrin
-
pH 6.0, 60ĆĀ°C, hydrolysis, wild-type and variants 3C71, 4B78 and 4A48
0.36
beta-cyclodextrin
-
pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA DELTA124, 1M KCl
0.461
beta-cyclodextrin
-
pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA- DELTA124
1.48
beta-cyclodextrin
pH and temperature not specified in the publication
1.5
maltoheptaose
-
kinetic parameters for C14-labelled maltooligosaccharides
3.8
maltohexaose
-
kinetic parameters for C14-labelled maltooligosaccharides
4.4
maltopentaose
-
kinetic parameters for C14-labelled maltooligosaccharides
1.6
maltotetraose
-
kinetic parameters for C14-labelled maltooligosaccharides
3.6
maltotriose
-
kinetic parameters for C14-labelled maltooligosaccharides
4.1
soluble starch
-
estimated for monomeric conformation, in presence of 1 M NaCl
-
additional information
additional information
-
Km 5.34 mg mL-1, starch as substrate, pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA-DELTA124
-
additional information
additional information
-
Km 49.7 mg/ml, starch as substrate, pH 6.0, 60ĆĀ°C, wild-type, 1 M KCl
-
additional information
additional information
-
Km 7.72 mg/ml, starch as substrate, pH 6.0, 60ĆĀ°C, truncated mutant ThMA-DELTA124, 1M KCl
-
additional information
additional information
-
Km 131 mg/ml, starch as substrate, mutant W47A
-
additional information
additional information
-
Km 73.5 mg/ml, starch as substrate, wild-type
-
additional information
additional information
-
Km 61.0 mg/ml, starch as substrate, pH 6.0, 60ĆĀ°C, hydrolysis, wild-type
-
additional information
additional information
-
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 modelling
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
alpha-cyclodextrin
monomeric enzyme form, at pH 7.0 and 80ĆĀ°C
0.75
alpha-cyclodextrin
mutant enzyme D109A, at pH 7.0 and 80ĆĀ°C
1.39
alpha-cyclodextrin
mutant enzyme D109E, at pH 7.0 and 80ĆĀ°C
1.45
alpha-cyclodextrin
pH and temperature not specified in the publication
2.78
alpha-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80ĆĀ°C
500
alpha-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60ĆĀ°C
0.005
amylopectin
mutant enzyme D109E, at pH 7.0 and 80ĆĀ°C
0.04
amylopectin
dimeric enzyme form, at pH 7.0 and 80ĆĀ°C
0.1
amylopectin
mutant enzyme D109A, at pH 7.0 and 80ĆĀ°C
0.17
amylopectin
monomeric enzyme form, at pH 7.0 and 80ĆĀ°C
0.8
amylopectin
pH and temperature not specified in the publication
15.38
amylopectin
in sodium-acetate buffer (50 mM, pH 6.0), at 60ĆĀ°C
0.59
amylose
pH and temperature not specified in the publication
0.00000343
beta-cyclodextrin
-
pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA-DELTA124
0.00000367
beta-cyclodextrin
-
pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
0.12
beta-cyclodextrin
monomeric enzyme form, at pH 7.0 and 80ĆĀ°C
0.49
beta-cyclodextrin
mutant enzyme D109A at pH 7.0 and 80ĆĀ°C
0.66
beta-cyclodextrin
mutant enzyme D109E at pH 7.0 and 80ĆĀ°C
1.33
beta-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80ĆĀ°C
5.36
beta-cyclodextrin
pH and temperature not specified in the publication
280.8
beta-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60ĆĀ°C
29.1
gamma-cyclodextrin
pH and temperature not specified in the publication
225.6
gamma-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60ĆĀ°C
108.25
maltotriose
pH 5.5, 60ĆĀ°C, mutant enzyme W177Y
150.98
maltotriose
pH 5.5, 60ĆĀ°C, mutant enzyme W177N
182.82
maltotriose
pH 5.5, 60ĆĀ°C, mutant enzyme W177S
0.021
soluble starch
mutant enzyme D109E, at pH 7.0 and 80ĆĀ°C
-
0.04
soluble starch
dimeric enzyme form, at pH 7.0 and 80ĆĀ°C
-
0.12
soluble starch
mutant enzyme D109A, at pH 7.0 and 80ĆĀ°C
-
0.2
soluble starch
monomeric enzyme form, at pH 7.0 and 80ĆĀ°C
-
0.000332
starch
-
pH 6.0, 60ĆĀ°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.37
alpha-cyclodextrin
pH and temperature not specified in the publication
3.62
beta-cyclodextrin
pH and temperature not specified in the publication
10.86
gamma-cyclodextrin
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.7
-
pH 6.0, 60ĆĀ°C, beta-cyclodextrin as substrate, variants 2A39, 4A48 and 3C71
177.4
-
cell extract, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5)
268.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MnCl2
413.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM BaCl2
535.1
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5)
558.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) methanol
568.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CoCl2
592.9
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) DMSO
604.7
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) ethanol
695.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MgCl2
728.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CaCl2
785.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM AlCl3
91
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CuCl2
93.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM HgCl2
95.2
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM ZnCl2
98.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90ĆĀ°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM FeSO4
additional information
additional information
kinetic 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 pullulan
additional information
-
kinetic 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 pullulan
additional information
kinetic properties determined in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling
additional information
kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method
additional information
-
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 50ĆĀ°C, yields of 53.1% obtained
additional information
-
specific activity of starch hydrolysis estimated for the high oligomer conformation is about 7 U/mg and for monomeric state about 110 U/mg
additional information
-
kinetic properties determined towards amylose and amylopectin in wild-type, double and triple mutant enzymes, bicinchonimate method, determination of reducing sugars
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
5.5
hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, W177Y and W177S
6.5
maximal activity, effect of pH on activity studied at 40ĆĀ°C using 50 mM buffers with different pH values ranging from 3.5 to 10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7
-
about 65% of activity maximum at pH 3.5, about 35% of activity maximum at pH 7.3
4 - 6
4 - 6.5
pH 4.0: about 65% of maximal activity, pH 6.5: about 60% of maximal activity, hydrolysis of maltotriose, wild-type enzyme
4 - 8
5 - 6.5
-
more than 50% of the maximum activity is retained in the range between pH 5.0 and pH 6.5
5 - 9
5 - 9.5
more 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 8
6 - 8
-
pH 6.0: about 80% of maximal activity, pH 8.0: about 30% of maximal activity
4 - 6
pH 4.0: less than 10% of maximal activity, pH 6.0: about 40% of maximal activity
4 - 6
pH 4.0: about 85% of maximal activity, pH 6.0: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose
4 - 8
pH 4.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin
4 - 8
-
more than 70% activity between pH 4.0 and 7.0, about 40% activity at pH 8.0
5 - 9
about 35% activity at pH 5.0, 100% activity at pH 6.0, about 85% activity at pH 7.0, about 60% activity at pH 8.0, about 40% activity at pH 9.0
5 - 9
the enzyme is active over a wide range of pH between 5.0 and 9.0 (more than 90% activity) but the activity drastically declines at pH 4.0 and 10.0 to 20 and less than 5%, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
55
60
70
75
80
40
maximal activity, effect of temperature on activity investigated in a 50 mM sodium phosphate buffer at pH 6.5 using different temperatures ranging from 10ĆĀ°C to 60ĆĀ°C
55
synthesis reaction performed for 12 h using 500 units/g substrate for transgylcosylation
60
hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, and W177S
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
kinetics shown, more than 50% of activity retained at the temperature range of 10Ć¢ĀĀ50ĆĀ°C, rapid decrease in activity above 60ĆĀ°C
20 - 55
more than 50% activity between 20 and 50ĆĀ°C, at 55ĆĀ°C the enzyme retains 38% of activity
20 - 80
-
about 20% of activity maximum at 30ĆĀ°C, about 60% of activity maximum at 80ĆĀ°C
30 - 60
-
30ĆĀ°C: about 20% of maximal activity with starch, about 25% of maximal activity with beta-cyclodextrin and about 35% of maximal activity with pullulan, 60ĆĀ°C: about 40% of maximal activity with pullulan, about 50% of maximal activity with starch anf about 80% of maximal activity with beta-cyclodextrin
30 - 70
30ĆĀ°C: about 40% of maximal activity, 70ĆĀ°C: about 65% of maximal activity, hydrolysis of maltotriose, mutant enzyme W177Y
40 - 100
about 35% activity at 40ĆĀ°C, about 60% activity at 50ĆĀ°C, about 80% activity at 90ĆĀ°C, about 35% activity at 70ĆĀ°C, 100% activity at 80ĆĀ°C, about 97% activity at 90ĆĀ°C, and about 75% activity at 100ĆĀ°C
40 - 70
about 40% activity at 40ĆĀ°C, about 80% activity at 50ĆĀ°C, 100% activity at 60ĆĀ°C, about 30% activity at 70ĆĀ°C
50 - 60
-
50ĆĀ°C: about 75% of maximal activity, 60ĆĀ°C: about 88% of maximal activity
50 - 80
50ĆĀ°C: about 70% of maximal activity, 80ĆĀ°C: about 40% of maximal activity, hydrolysis of maltotriose, wild-type enzyme
60 - 95
60ĆĀ°C; about 50% of maximal activity, 60ĆĀ°C: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose
75 - 80
-
high thermostability, dependent on oligomer structure of the enzyme, optimal activity at 75ĆĀ°C and 80ĆĀ°C for beta-cyclodextrin and soluble starch, half-lifes of 61 min at 75ĆĀ°C and of 24 min at 80ĆĀ°C
80 - 98
activity at 80ĆĀ°C is about 50% compared to the activity at 98ĆĀ°C, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
maltogenic alpha-amylase precursor, amyM gene
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity tested in both, liquid and solid media
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme sequence contains no signal sequence
-
brenda
additional information
-
the enzyme sequence contains no signal sequence
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme has a key role in carbohydrate metabolization
physiological function
physiological function
the enzyme may have a role in regulating the concentration of maltose during maltodextrin metabolism
physiological function
-
the enzyme may have a role in regulating the concentration of maltose during maltodextrin metabolism
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A150M1H3_9BACI
767
1
85785
TrEMBL
-
Q1J674_STRPF
Streptococcus pyogenes serotype M4 (strain MGAS10750)
571
1
66178
TrEMBL
-
E6QP40_9ZZZZ
711
0
77523
TrEMBL
Secretory Pathway (Reliability: 1)
Q48T00_STRPM
Streptococcus pyogenes serotype M28 (strain MGAS6180)
567
1
65689
TrEMBL
-
A0A7T1AJT3_9BACT
105
0
10700
TrEMBL
-
A0A1V5W509_9BACT
778
0
89430
TrEMBL
-
A0A1V5WY73_9DELT
586
0
66460
TrEMBL
-
A0A086ZUY9_9BIFI
448
0
50064
TrEMBL
-
A0A3B0UKL9_9ZZZZ
814
0
89672
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V5YXI4_9BACT
932
1
102899
TrEMBL
-
A0A7T1F2F7_9BACT
122
0
12690
TrEMBL
-
A0A1Y5Q734_9GAMM
uncultured Stenotrophomonas sp
576
1
63037
TrEMBL
-
C2EJN0_9LACO
581
0
67321
TrEMBL
-
A0A068LQV2_BACMM
Bacillus methanolicus (strain MGA3 / ATCC 53907)
586
0
68909
TrEMBL
-
Q1WVM9_LACS1
Lactobacillus salivarius (strain UCC118)
581
0
67308
TrEMBL
-
C2EJJ5_9LACO
587
0
68794
TrEMBL
-
A0A1V6JHM6_9BACT
792
0
89868
TrEMBL
-
Q1JGF7_STRPD
Streptococcus pyogenes serotype M2 (strain MGAS10270)
571
1
66236
TrEMBL
-
Q3EM70_BACTI
574
0
66884
TrEMBL
-
G4L513_TETHN
Tetragenococcus halophilus (strain DSM 20338 / JCM 20259 / NCIMB 9735 / NBRC 12172)
586
0
68285
TrEMBL
-
A0A343TIV7_9EURY
618
0
71409
TrEMBL
-
Q1WSM7_LACS1
Lactobacillus salivarius (strain UCC118)
587
0
69000
TrEMBL
-
A0A1W6VNX3_GEOTD
588
0
68956
TrEMBL
-
B2J5W8_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
527
0
60444
TrEMBL
-
B2FSK3_STRMK
Stenotrophomonas maltophilia (strain K279a)
572
0
62789
TrEMBL
-
A0A7T1AME0_9BACT
152
1
16249
TrEMBL
-
A0A087CV71_9BIFI
434
0
48258
TrEMBL
-
A0A1V5SSF7_9BACT
110
0
11398
TrEMBL
-
D2BPI3_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
600
0
69663
TrEMBL
-
A0A1V5KZV1_9FIRM
888
0
95428
TrEMBL
-
Q5E352_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
610
0
70385
TrEMBL
-
K4Q9V8_STREQ
567
0
65498
TrEMBL
-
F9URM8_LACPL
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
574
0
64395
TrEMBL
-
A0A0H3J849_CLOPA
454
0
53442
TrEMBL
-
A0A2S3U1J1_LACPN
574
0
64429
TrEMBL
-
A3DM60_STAMF
Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)
696
0
82468
TrEMBL
-
G8N704_GEOTH
511
0
59734
TrEMBL
-
I3ZTN9_THECF
Thermococcus cleftensis (strain DSM 27260 / KACC 17922 / CL1)
575
0
66999
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
135000
65000
67500
68000
70000
65000
-
SDS-PAGE, difference in molecular masses due to the presence of the six-histidine tag and two additional amino acids
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer