Acetylglutamate kinase
From Wikipedia, the free encyclopedia
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. 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. This enzyme participates in urea cycle and metabolism of amino groups.
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[edit] Structural studies
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.
[edit] References
- IUBMB entry for 2.7.2.8
- BRENDA references for 2.7.2.8 (Recommended.)
- PubMed references for 2.7.2.8
- PubMed Central references for 2.7.2.8
- Google Scholar references for 2.7.2.8
- 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. 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: 6–18. PMID 6040410.
- Vogel HJ and McLellan WL (1970). "N-Acetyl-gamma-glutamokinase (Escherichia coli)". Methods Enzymol. 17A: 251–255.
[edit] External links
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- The CAS registry number for this enzyme class is 9027-58-1.