Lombricine kinase

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In enzymology, a lombricine kinase (EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction

ATP + lombricine $\rightleftharpoons$ ADP + N-phospholombricine

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

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:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.

[edit] References

IUBMB entry for 2.7.3.5
BRENDA references for 2.7.3.5 (Recommended.)
PubMed references for 2.7.3.5
PubMed Central references for 2.7.3.5
Google Scholar references for 2.7.3.5
Gaffney TJ, Rosenberg H, Ennor AH (1964). "The purification and properties of adenosine triphosphate-lombricine phosphotransferase". Biochem. J. 90: 170–6. PMID 5832288.
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.
Pant R (1959). "Isolation of lombricine and its enzymatic phosphorylation". Biochem. J. 73: 30–33.
van Thoai N, Robin Y, Guillou Y (1972). "A new phosphagen, N'-phosphorylguanidinoethylphospho-O-( -N,N-dimethyl)serine (phosphothalassemine)". Biochemistry. 11: 3890–5. doi:10.1021/bi00771a009. PMID 5079888.