Glucuronokinase
From Wikipedia the free encyclopedia
| glucuronokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.43 | ||||||||
| CAS no. | 9026-62-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glucuronokinase (EC 2.7.1.43) is an enzyme that catalyzes the chemical reaction
- ATP + D-glucuronate ADP + 1-phospho-alpha-D-glucuronate
Thus, the two substrates of this enzyme are ATP and D-glucuronate, whereas its two products are ADP and 1-phospho-alpha-D-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glucuronate 1-phosphotransferase. Other names in common use include glucuronokinase (phosphorylating), and glucurono-glucuronokinase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References[edit]
- Neufeld EF, Feingold DS, Hassid WZ (1959). "Enzymic phosphorylation of D-glucuronic acid by extracts from seedlings of Phaseolus aureus". Arch. Biochem. Biophys. 83 (1): 96–100. doi:10.1016/0003-9861(59)90014-1. PMID 13661996.
