Glutamate-5-semialdehyde dehydrogenase
| 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 | ||||||||
| |||||||||
In enzymology, glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction
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
- ^ Enzyme 1.2.1.41 at KEGG Pathway Database.
- ^ 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.