Acetylglutamate kinase
| acetylglutamate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.2.8 | ||||||||
| CAS no. | 9027-58-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an acetylglutamate kinase (EC 2.7.2.8) is an enzyme that catalyzes the chemical reaction:
- ATP + N-acetyl-L-glutamate ADP + N-acetyl-L-glutamyl 5-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-L-glutamate, whereas its two products are ADP and N-acetyl-L-glutamyl 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. This enzyme participates in urea cycle and metabolism of amino groups.
Nomenclature
[edit]The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include:
- N-acetylglutamate 5-phosphotransferase,
- acetylglutamate phosphokinase,
- N-acetylglutamate phosphokinase,
- N-acetylglutamate kinase, and
- N-acetylglutamic 5-phosphotransferase.
Structural studies
[edit]As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1GS5, 1GSJ, 1OH9, 1OHA, 1OHB, 2AP9, 2BTY, 2BUF, and 2RD5.
References
[edit]- Baich A, Vogel HJ (1962). "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli". Biochem. Biophys. Res. Commun. 7 (6): 491–6. doi:10.1016/0006-291X(62)90342-X. PMID 13863980.
- Farago A, Denes G (1967). "Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway". Biochim. Biophys. Acta. 136 (1): 6–18. doi:10.1016/0304-4165(67)90315-7. PMID 6040410.
- Vogel HJ, McLellan WL (1970). "[24b] N-acetyl-γ-glutamokinase (Escherichia coli)". N-Acetyl-gamma-glutamokinase (Escherichia coli). Methods Enzymol. Vol. 17A. pp. 251–255. doi:10.1016/0076-6879(71)17190-x. ISBN 978-0-12-181874-6.
