Glutamate-5-semialdehyde dehydrogenase

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glutamate-5-semialdehyde dehydrogenase
Identifiers
EC no. 1.2.1.41
CAS no. 54596-29-1
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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PMC articles
PubMed articles
NCBI proteins

In enzymology, glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction

 
 
Pi
H+
Glutamate-5-semialdehyde dehydrogenase
Pi
H+
 
 

The three substrates of this enzyme are L-glutamate-5-semialdehyde, oxidised nicotinamide adenine dinucleotide phosphate (NADP+) and phosphate (Pi). Its products are L-γ-glutamyl phosphate, reduced NADPH, and a proton. [1] [2]

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 L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1O20, 1VLU, and 2H5G.

References

  1. Enzyme 1.2.1.41 at KEGG Pathway Database.
  2. Baich A (July 1971). "The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate -semialdehyde dehydrogenase (NADP), the second enzyme in the pathway". Biochimica et Biophysica Acta. 244 (1): 129–34. doi:10.1016/0304-4165(71)90129-2. PMID   4399189.