| cellobiose phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Cellobiose phosphorylase dimer, Cellulomonas uda | |||||||||
| Identifiers | |||||||||
| EC no. | 2.4.1.20 | ||||||||
| CAS no. | 9030-20-0 | ||||||||
| 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 | ||||||||
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In enzymology, a cellobiose phosphorylase (EC 2.4.1.20) is an enzyme that catalyzes the chemical reaction
- cellobiose + phosphate alpha-D-glucose 1-phosphate + D-glucose
alpha-D-glucose 1-phosphate + D-glucoseThus, the two substrates of this enzyme are cellobiose and phosphate, whereas its two products are alpha-D-glucose 1-phosphate and D-glucose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is cellobiose:phosphate alpha-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2006, two structures have been solved for this class of enzymes, with PDB accession codes 2CQS and 2CQT.
References
- Alexander JK (June 1968). "Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum". The Journal of Biological Chemistry. 243 (11): 2899–904. doi:10.1016/S0021-9258(18)93356-9. PMID 5653182.
- Ayers WA (November 1959). "Phosphorolysis and synthesis of cellobiose by cell extracts from Ruminococcus flavefaciens". The Journal of Biological Chemistry. 234 (11): 2819–22. doi:10.1016/S0021-9258(18)69677-2. PMID 13795349.
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