N-acetyl-gamma-glutamyl-phosphate reductase

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 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

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.

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.