Choline kinase

From Wikipedia, the free encyclopedia

choline kinase (EC 2.7.1.32) is an enzyme that catalyzes the chemical reaction between ATP and choline to make a phosphocholine.

ATP + choline $\rightleftharpoons$ ADP + O-phosphocholine

Thus, the two substrates of this enzyme are ATP and choline, whereas its two products are ADP and O-phosphocholine.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The first detailed investigation of the enzyme was conducted by McCamen in 1962, where it was shown that the brain is the richest source of the enzyme in mammalian tissue. A related enzyme, ethanolamine kinase tends to co-purify with choline kinase leading to a suggestion that the two activities are mediated by two distinct active sites on a single protein ^[1] . The systematic name of this enzyme class is ATP:choline phosphotransferase. These enzymes participate in glycine, serine and threonine metabolism and glycerophospholipid metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1NW1, 2CKO, 2CKP, 2CKQ, 2I7Q, and 2IG7.

[edit] References

^ Spanner, S. & Ansell, G.B. (1978). "Choline kinase and ethanolamine kinase activity in the cytosol of nerve endings from rat forebrain. 178, 753-760

IUBMB entry for 2.7.1.32
BRENDA references for 2.7.1.32 (Recommended.)
PubMed references for 2.7.1.32
PubMed Central references for 2.7.1.32
Google Scholar references for 2.7.1.32
Hayashi SI, Lin EC (1967). "Purification and properties of glycerol kinase from Escherichia coli". J. Biol. Chem. 242: 1030–5. PMID 5335908.
Wittenberg J and Kornberg A (1953). "Choline phosphokinase". J. Biol. Chem. 202: 431–444.