Biology:Glutamate 5-kinase
| Glutamate 5-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glutamate 5-kinase tetramer, Burkholderia thailandensis | |||||||||
| 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 | ||||||||
| |||||||||
Glutamate 5-kinase (EC 2.7.2.11) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme characterised from Escherichia coli, converts L-glutamic acid, to L-γ-glutamyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the biosynthesis of the amino acid, proline.[1]
The product can spontaneously cyclise to (S)-pyroglutamic acid by loss of the phosphate group (Pi):[2]
- REDIRECT Template:Chemical reaction
This enzyme is a transferase, specifically one 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.[2]
Structural studies
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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