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Glutamate 5-kinase

From Wikipedia, the free encyclopedia
glutamate 5-kinase
Glutamate 5-kinase tetramer, Burkholderia thailandensis
Identifiers
EC no.2.7.2.11
CAS no.54596-30-4
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 glutamate 5-kinase (EC 2.7.2.11) is an enzyme that catalyzes the chemical reaction

ATP + L-glutamate ADP + L-glutamate 5-phosphate

Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and L-glutamate 5-phosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 5-phosphotransferase. Other names in common use include ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, gamma-glutamate kinase, gamma-glutamyl kinase, and glutamate kinase. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

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As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AKO, 2J5T, and 2J5V.

References

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  • Baich A (December 1969). "Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase". Biochimica et Biophysica Acta (BBA) - General Subjects. 192 (3): 462–7. doi:10.1016/0304-4165(69)90395-x. PMID 4904678.