Taurocyamine kinase

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In enzymology, a taurocyamine kinase (EC 2.7.3.4) is an enzyme that catalyzes the chemical reaction

ATP + taurocyamine $\rightleftharpoons$ ADP + N-phosphotaurocyamine

Thus, the two substrates of this enzyme are ATP and taurocyamine, whereas its two products are ADP and N-phosphotaurocyamine.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:taurocyamine N-phosphotransferase. Other names in common use include taurocyamine phosphotransferase, and ATP:taurocyamine phosphotransferase. This enzyme participates in taurine and hypotaurine metabolism.

[edit] References

IUBMB entry for 2.7.3.4
BRENDA references for 2.7.3.4 (Recommended.)
PubMed references for 2.7.3.4
PubMed Central references for 2.7.3.4
Google Scholar references for 2.7.3.4
HOBSON GE, REES KR (1957). "The annelid phosphokinases". Biochem. J. 65: 305–7. PMID 13403909.
Kassab R, Pradel LA, Nguyen Van Thoai (1965). "[ATP:taurocyamine and ATP:lombricine phosphotransferases Purification and study of SH groups]". Biochim. Biophys. Acta. 99: 397–405. PMID 5840960.
Thoai NV (1957). "Sur la taurocyamine et la glycocyamine phosphokinase". Bull. Soc. Chim. Biol. 39: 197–208.
Thoai NV, Robin Y and Pradel L-A (1963). "Hypotaurocyamine phosphokinase comparison avec la taurocyamine phosphokinase". Biochim. Biophys. Acta 73: 437–444. doi:10.1016/0006-3002(63)90445-1.