Cyclomaltodextrinase
| cyclomaltodextrinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.54 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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 and H2O, whereas its product is .
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 and acarbose degradation.[1][2] The cyclomaltodextrinase is capable of degradation of acarbose to glucose and acarviosine-glucose.[3]
Structural studies[]
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EA9 and 1H3G.
References[]
- ^ Jang MU, Jeong CK, Kang HJ, Kim MJ, Lee MJ, Son BS, Kim TJ (2016). "Gene Cluster Analysis and Functional Characterization of Cyclomaltodextrinase from Listeria innocua". Microbiology and Biotechnology Letters. 44 (3): 363–369. doi:10.4014/mbl.1608.08008. ISSN 1598-642X.
- ^ Jang MU, Kang HJ, Jeong CK, Kang Y, Park JE, Kim TJ (February 2018). "Functional expression and enzymatic characterization of Lactobacillus plantarum cyclomaltodextrinase catalyzing novel acarbose hydrolysis". Journal of Microbiology. 56 (2): 113–118. doi:10.1007/s12275-018-7551-3. PMID 29392561.
- ^ Park KH (2006). "Function and Tertiary- and Quaternary-structure of Cyclodextrin-hydrolyzing Enzymes (CDase), a Group of Multisubstrate Specific Enzymes Belonging to the α-Amylase Family". Journal of Applied Glycoscience. 53 (1): 35–44. doi:10.5458/jag.53.35.
Further reading[]
- DePinto JA, Campbell LL (January 1968). "Purification and properties of the cyclodextrinase of Bacillus macerans". Biochemistry. 7 (1): 121–125. doi:10.1021/bi00841a016. PMID 4922856.
- EC 3.2.1
- Enzymes of known structure
- EC 3.2 stubs