In enzymology, N-acetyl-gamma-glutamyl-phosphate reductase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are N-acetyl-L-ó-glutamyl phosphate, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and a proton. Its products are 2-acetamido-5-oxopentanoic acid, oxidised NADP<sup>+</sup>, and inorganic phosphate (P<sub>i</sub>).
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.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .