Biology:N-acetyl-gamma-glutamyl-phosphate reductase
| N-acetyl-gamma-glutamyl-phosphate reductase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.2.1.38 | ||||||||
| CAS number | 37251-00-6 | ||||||||
| 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 / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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.
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
- "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli". Biochem. Biophys. Res. Commun. 7 (6): 491–6. 1962. doi:10.1016/0006-291X(62)90342-X. PMID 13863980.
- Glansdorff N; Sand G (1965). "Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12". Biochim. Biophys. Acta 108 (2): 308–311. doi:10.1016/0005-2787(65)90016-x. PMID 5325238.
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