Cellulose synthase (GDP-forming)
| cellulose synthase (GDP-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.29 | ||||||||
| CAS no. | 9027-18-3 | ||||||||
| 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 cellulose synthase (GDP-forming) (EC 2.4.1.29) is an enzyme that catalyzes the chemical reaction
- GDP-glucose + (1,4-beta-D-glucosyl)n GDP + (1,4-beta-D-glucosyl)n+1
Thus, the two substrates of this enzyme are GDP-glucose and (1,4-beta-D-glucosyl)n, whereas its two products are GDP and (1,4-beta-D-glucosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-glucose:1,4-beta-D-glucan 4-beta-D-glucosyltransferase. Other names in common use include cellulose synthase (guanosine diphosphate-forming), cellulose synthetase, guanosine diphosphoglucose-1,4-beta-glucan glucosyltransferase, and guanosine diphosphoglucose-cellulose glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
As of August 2019[update], no proteins with this activity are known in the UniProt/NiceZYme or the gene ontology database.
References
[edit]- Chambers J, Elbein AD (1970). "Biosynthesis of glucans in mung bean seedlings. Formation of beta-(1,4)-glucans from GDP-glucose and beta-(1,3)-glucans from UDP-glucose". Arch. Biochem. Biophys. 138 (2): 620–31. doi:10.1016/0003-9861(70)90389-9. PMID 4317490.
- Flowers HM, Batra KK, Kemp J, Hassid WZ (1969). "Biosynthesis of cellulose in vitro from guanosine diphosphate D-glucose with enzymic preparations from Phaseolus aureus and Lupinus albus". J. Biol. Chem. 244 (18): 4969–74. doi:10.1016/S0021-9258(18)94297-3. PMID 5824571.
