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Erythritol kinase 
Summary
In enzymology, an erythritol kinase (EC 2.7.1.27) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- 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: 2581–4. PMID 13908588.
- HOLTEN D, FROMM HJ (1961). "Purification and properties of erythritol kinase from Propionibacterium pentosaceum". J. Biol. Chem. 236: 2581–4. PMID 13908588.
