Lombricine kinase
| lombricine kinase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 2.7.3.5 | ||||||
| CAS number | 9026-53-3 | ||||||
| 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 / EGO | ||||||
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In enzymology, a lombricine kinase (EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction
- ATP + lombricine
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.
References
- Gaffney TJ, Rosenberg H, Ennor AH (1964). "The purification and properties of adenosine triphosphate-lombricine phosphotransferase". Biochem. J. 90 (1): 170–6. PMC 1202539. PMID 5832288. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1202539.
- Kassab R, Pradel LA, Nguyen Van Thoai (1965). "[ATP:taurocyamine and ATP:lombricine phosphotransferases Purification and study of SH groups]". Biochim. Biophys. Acta. 99 (3): 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 (21): 3890–5. doi:10.1021/bi00771a009. PMID 5079888.