Jump to content

Lombricine kinase

From Wikipedia, the free encyclopedia
lombricine kinase
Identifiers
EC no.2.7.3.5
CAS no.9026-53-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

ATP + lombricine ADP + N-phospholombricine

The two substrates of this enzyme are ATP and lombricine, and the 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

[edit]
  • 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.
  • 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. doi:10.1016/s0926-6593(65)80194-1. 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.