3.2.1.B36: maltose-forming alpha-amylase
This is an abbreviated version!
For detailed information about maltose-forming alpha-amylase, go to the full flat file.
Reaction
An exo-type maltose-forming alpha-amylase alpha-1,4- and alpha-1,6-glucan hydrolytic activity. It acts on the non-reducing end of the substrate and requires at least a G2 unit at its working site =
Synonyms
maltose-forming alpha-amylase, PSMA, Py04_0872, Pyrococcus ST04 alpha-amylase, TCMA
ECTree
3.2.1.B36 maltose-forming alpha-amylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.B36 - maltose-forming alpha-amylase
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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-nitrophenyl alpha-D-maltotetraoside + maltose
at an early stage of the reaction only maltose and 4-nitrophenol alpha-D-maltotetraoside, but not maltotetraose are observed. Even as the reaction proceeded, maltotetraose does not appear at all
-
-
?
amylopectin + H2O
maltose + ?
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
glycogen + H2O
maltose + ?
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
6-O-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
-
-
-
?
6-O-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
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
-
-
?
6-O-maltotetraosyl-beta-cyclodextrin + H2O
2 maltose + beta-cyclodextrin
no formation of matotetraose
-
-
?
6-O-maltotetraosyl-beta-cyclodextrin + H2O
2 maltose + beta-cyclodextrin
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a maltose 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 maltose 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. 6-O-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant to hydrolysis
-
-
?
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. Substrate specificity and binding, docking modelling, overview
-
-
?
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. Substrate specificity and binding, docking modelling, overview
-
-
?
