N-acetyl-gamma-glutamyl-phosphate reductase

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N-acetyl-gamma-glutamyl-phosphate reductase
Identifiers
EC no. 1.2.1.38
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

 
 
H+
Pi
N-acetyl-gamma-glutamyl-phosphate reductase
H+
Pi
 
 

The three substrates of this enzyme are N-acetyl-L-γ-glutamyl phosphate, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and a proton. Its products are 2-acetamido-5-oxopentanoic acid, oxidised NADP+, and inorganic phosphate (Pi). [1] [2] [3]

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

  1. Enzyme 1.2.1.38 at KEGG Pathway Database.
  2. 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 (6): 491–6. Bibcode:1962BBRC....7..491B. doi:10.1016/0006-291X(62)90342-X. PMID   13863980.
  3. 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.