3.2.1.B8: malto-alpha-amylase (reducing end)
This is an abbreviated version!
For detailed information about malto-alpha-amylase (reducing end), go to the full flat file.
Reaction
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains =
Synonyms
cyclodextrinase, MAase, maltogenic amylase, MalZ, More, SMMA, TMG, YvdF
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Substrates Products
Substrates Products on EC 3.2.1.B8 - malto-alpha-amylase (reducing end)
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REACTION DIAGRAM
4-nitrophenyl alpha-maltopentaoside
maltopentaose + 4-nitrophenol
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4-nitrophenyl alpha-maltopentaoside + H2O
maltopentaose + 4-nitrophenol
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further hydrolysis of maltopentaose by TMG
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linear maltoheptaose + H2O
maltose + D-glucose
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SMMA preferentially hydrolyzed the first and second glycosidic bonds from the reducing end
primary products
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linear maltohexaose + H2O
maltose + D-glucose
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best substrate
primary products
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linear maltooligosaccharide + H2O
maltose + D-glucose
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maximal activity of SMMA toward G6, but almost no activity toward G3
primary products
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maltose + D-glucose
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primary products
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gamma-cyclodextrin + H2O
maltose + D-glucose
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primary products
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MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6
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additional information
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MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6
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additional information
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MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4
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additional information
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SMMA hydrolyzes linear maltooligosaccharides, starch, cyclodextrins, and cycloamylose, primarily to maltose and glucose, and shows highest activity toward acarbose and pullulan, hydrolyzed to acarviosine-glucose and panose, respectively. Product analysis, overview
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additional information
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TMG is an exo-acting glucosidase possessing the characteristics of both CD-/pullulan hydrolyzing enzyme and alpha-glucosidase. It hydrolyzes various maltodextrins including maltotriose to maltoheptaose and cyclomaltodextrins to mainly glucose and maltose, but it cannot hydrolyze pullulan, but acarbose
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additional information
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the enzyme specifically cleaves a glucose unit from the reducing end of maltooligosaccharides unlike to other glucosidases. Since its enzymatic activity is negligible if alpha-methylglucoside is present in the reducing end, the type of the residue at the reducing end of the substrate is important for the TMG activity. It hydrolyzes various maltodextrins including maltotriose to maltoheptaose and cyclomaltodextrins to mainly glucose and maltose, but it cannot hydrolyze pullulan, but acarbose
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