Erythritol kinase
| erythritol kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.27 | ||||||||
| CAS no. | 9030-64-2 | ||||||||
| 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, an erythritol kinase (EC 2.7.1.27) is an enzyme that catalyzes the chemical reaction
- ATP + erythritol ADP + D-erythritol 4-phosphate
Thus, the two substrates of this enzyme are ATP and erythritol, whereas its two products are ADP and D-erythritol 4-phosphate.
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:erythritol 4-phosphotransferase. This enzyme is also called erythritol kinase (phosphorylating).
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V5S.
References
[edit]- HOLTEN D, FROMM HJ (1961). "Purification and properties of erythritol kinase from Propionibacterium pentosaceum". J. Biol. Chem. 236 (10): 2581–4. doi:10.1016/S0021-9258(19)61702-3. PMID 13908588.
- HOLTEN D, FROMM HJ (1961). "Purification and properties of erythritol kinase from Propionibacterium pentosaceum". J. Biol. Chem. 236 (10): 2581–4. doi:10.1016/S0021-9258(19)61702-3. PMID 13908588.
