| glutamate 5-kinase | |||||||||
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Glutamate 5-kinase tetramer, Burkholderia thailandensis
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| Identifiers | |||||||||
| EC number | 2.7.2.11 | ||||||||
| CAS number | 54596-30-4 | ||||||||
| 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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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
In enzymology, a glutamate 5-kinase (EC 2.7.2.11) is an enzyme that catalyzes the chemical reaction
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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AKO, 2J5T, and 2J5V.