Cyclomaltodextrinase
| cyclomaltodextrinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.54 | ||||||||
| CAS number | 37288-41-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a cyclomaltodextrinase (EC 3.2.1.54) is an enzyme that catalyzes the chemical reaction
- cyclomaltodextrin + H2O linear maltodextrin
Thus, the two substrates of this enzyme are cyclomaltodextrin and H2O, whereas its product is linear maltodextrin.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is cyclomaltodextrin dextrin-hydrolase (decyclizing). Other names in common use include cycloheptaglucanase, cyclohexaglucanase, and cyclodextrinase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EA9 and 1H3G.
References
- DePinto JA, Campbell LL (1968). "Purification and properties of the cyclodextrinase of Bacillus macerans". Biochemistry. 7 (1): 121–5. doi:10.1021/bi00841a016. PMID 4922856.
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