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
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3.2.1.133
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amylases
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baking
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bake
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food industry
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synthesis
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cgtases
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maltooligosaccharide
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amylopectin
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enzyme-total
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alpha-amylases
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novozymes
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staling
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beta-cds
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crumb
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stale
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antistaling
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nutrition
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biotechnology
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medicine
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degradation
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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
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Metals Ions
Metals Ions on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase
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Al3+
Ca2+
Co2+
Mg2+
Mn2+
additional information
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calcium can stabilize the enzyme activity up to 50°C at atmospheric pressure (% of residual activities at 50, 60, and 70°C are 100, 4.93, 0, respectively)
Ca2+
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mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L shows highly improved thermostability and catalytic activity in presence of Ca2+.
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