In enzymology, a dephospho-CoA kinase (EC 2.7.1.24) is an enzyme that catalyzes the chemical reaction
| dephospho-CoA kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.24 | ||||||||
| CAS no. | 9026-83-9 | ||||||||
| 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 + dephospho-CoA ADP + CoA
Thus, the two substrates of this enzyme are ATP and dephospho-CoA, whereas its two products are ADP and CoA.
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:dephospho-CoA 3'-phosphotransferase. Other names in common use include dephosphocoenzyme A kinase (phosphorylating), 3'-dephospho-CoA kinase, and dephosphocoenzyme A kinase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
editAs of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1JJV, 1N3B, 1T3H, 1VHL, 1VHT, 1VIY, 2GRJ, and 2IF2.
References
edit- Abiko Y (1970). "Pantothenic acid and coenzyme A: Dephospho-CoA pyrophosphorylase and dephospho-CoA kinase as a possible bifunctional enzyme complex (ATP: Pantetheine-4′-phosphate adenyltransferase, EC 2.7.7.3 and ATP: Dephospho-CoA 3′-phosphotransferase, EC 2.7.1.24)". Vitamins and Coenzymes. Methods Enzymol. Vol. 18A. pp. 358–364. doi:10.1016/0076-6879(71)18327-9. ISBN 978-0-12-181879-1.
- HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. Biol. Chem. 207 (2): 767–73. doi:10.1016/S0021-9258(18)65696-0. PMID 13163064.
- Wang TP, Kaplan NO (1954). "Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide". J. Biol. Chem. 206 (1): 311–325. doi:10.1016/S0021-9258(18)71320-3. PMID 13130551.
