Glucan 1,4-alpha-maltohydrolase
Glucan 1,4-alpha-maltohydrolase | |||||||||
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Identifiers | |||||||||
EC number | 3.2.1.133 | ||||||||
CAS number | 160611-47-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with systematic name 4-alpha-D-glucan alpha-maltohydrolase.[1][2] This enzyme catalyses the following chemical reaction
- 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
This enzyme acts on starch and related polysaccharides and oligosaccharides.
References
- ↑ Diderichsen B, Christiansen L (1988). "Cloning of a maltogenic α-amylase from Bacillus stearothermophilus". FEMS Microbiol. Lett. 56: 53–59. doi:10.1111/j.1574-6968.1988.tb03149.x.
- ↑ Outtrup H, Norman BE (1984). "Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques". Stärke. 36: 405–411. doi:10.1002/star.19840361202.
External links
- Glucan+1,4-alpha-maltohydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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