Acetylglutamate kinase

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acetylglutamate kinase
Identifiers
EC number 2.7.2.8
CAS number 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 / EGO

In enzymology, an acetylglutamate kinase (EC 2.7.2.8) is an enzyme that catalyzes the chemical reaction:

ATP + N-acetyl-L-glutamate \rightleftharpoons 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: 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 and McLellan WL (1970). "N-Acetyl-gamma-glutamokinase (Escherichia coli)". Methods Enzymol. 17A: 251–255. doi:10.1016/0076-6879(71)17190-x.