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Dephospho-CoA kinase

From Wikipedia, the free encyclopedia

In enzymology, a dephospho-CoA kinase (EC 2.7.1.24) is an enzyme that catalyzes the chemical reaction

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

As 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

  • 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 adenylyltransferase, EC 2.7.7.3 and ATP:dephospho-CoA-3'-phosphotransferase EC 2.7.1.24)". Methods Enzymol. 18A: 358–364. doi:10.1016/0076-6879(71)18327-9.
  • HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. Biol. Chem. 207 (2): 767–73. PMID 13163064.
  • Wang TP, Kaplan NO (1954). "Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide". J. Biol. Chem. 206 (1): 311–325. PMID 13130551.


This page was last edited on 26 August 2023, at 13:47
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