In enzymology, a hydroxyanthraquinone glucosyltransferase (EC 2.4.1.181) is an enzyme that catalyzes the chemical reaction
| hydroxyanthraquinone glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.181 | ||||||||
| CAS no. | 112198-78-4 | ||||||||
| 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 | ||||||||
| |||||||||
- UDP-glucose + an hydroxyanthraquinone UDP + a glucosyloxyanthraquinone
Thus, the two substrates of this enzyme are UDP-glucose and hydroxyanthraquinone, whereas its two products are UDP and glucosyloxyanthraquinone.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:hydroxyanthraquinone O-glucosyltransferase. Other names in common use include uridine diphosphoglucose-anthraquinone glucosyltransferase, and anthraquinone-specific glucosyltransferase.
References
edit- Khouri HE, Ibrahim RK (1987). "Purification and some properties of five anthraquinone-specific glucosyltransferases from Cinchona succiruba cell suspension culture". Phytochemistry. 26 (9): 2531–2535. doi:10.1016/S0031-9422(00)83870-4.
