lombricine kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.3.5 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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In enzymology, a lombricine kinase (EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction
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.
A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).
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