N-acetyl-gamma-glutamyl-phosphate reductase

From Wikipedia, the free encyclopedia

In enzymology, a N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) is an enzyme that catalyzes the chemical reaction

N-acetyl-L-glutamate 5-semialdehyde + NADP⁺ + phosphate $\rightleftharpoons$ N-acetyl-L-glutamyl 5-phosphate + NADPH + H⁺

The 3 substrates of this enzyme are N-acetyl-L-glutamate 5-semialdehyde, NADP⁺, and phosphate, whereas its 3 products are N-acetyl-L-glutamyl 5-phosphate, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include reductase, acetyl-gamma-glutamyl phosphate, N-acetylglutamate 5-semialdehyde dehydrogenase, N-acetylglutamic gamma-semialdehyde dehydrogenase, N-acetyl-L-glutamate gamma-semialdehyde:NADP+ oxidoreductase, and (phosphorylating). This enzyme participates in urea cycle and metabolism of amino groups.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1VKN, 2CVO, 2G17, 2I3A, 2I3G, 2NQT, 2OZP, and 2Q49.

[edit] References

IUBMB entry for 1.2.1.38
BRENDA references for 1.2.1.38 (Recommended.)
PubMed references for 1.2.1.38
PubMed Central references for 1.2.1.38
Google Scholar references for 1.2.1.38
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.
Glansdorff N and Sand G (1965). "Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12". Biochim. Biophys. Acta 108: 308–311.