α-Amylase
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process:
- Endohydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides containing three or more (1→4)-α-linked D-glucose units
α-Amylase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.1.1 | ||||||||
CAS no. | 9000-90-2 | ||||||||
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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GH13 catalytic domain | |||||||||
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Cyclodextrin glucanotransferase (e.c.2.4.1.19) (cgtase) | |||||||||
Identifiers | |||||||||
Symbol | Alpha-amylase | ||||||||
Pfam | PF00128 | ||||||||
Pfam clan | CL0058 | ||||||||
InterPro | IPR006047 | ||||||||
SCOP2 | 1ppi / SCOPe / SUPFAM | ||||||||
OPM superfamily | 117 | ||||||||
OPM protein | 1wza | ||||||||
CAZy | GH13 | ||||||||
CDD | cd11338 | ||||||||
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Alpha-amylase C-terminal beta-sheet domain | |||||||||
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Crystal structure of barley alpha-amylase isozyme 1 (amy1) inactive mutant d180a in complex with maltoheptaose | |||||||||
Identifiers | |||||||||
Symbol | Alpha-amyl_C2 | ||||||||
Pfam | PF07821 | ||||||||
InterPro | IPR012850 | ||||||||
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Alpha amylase, C-terminal all-beta domain | |||||||||
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maltotriose complex of preconditioned cyclodextrin glycosyltransferase mutant | |||||||||
Identifiers | |||||||||
Symbol | Alpha-amylase_C | ||||||||
Pfam | PF02806 | ||||||||
Pfam clan | CL0369 | ||||||||
InterPro | IPR006048 | ||||||||
SCOP2 | 1ppi / SCOPe / SUPFAM | ||||||||
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It is the major form of amylase found in humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. It is a member of glycoside hydrolase family 13.
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