Aminobutyraldehyde dehydrogenase
| aminobutyraldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.19 | ||||||||
| CAS no. | 9028-98-2 | ||||||||
| 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, aminobutyraldehyde dehydrogenase (EC 1.2.1.19) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are 4-aminobutanal, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are γ-aminobutyric acid, reduced NADH, and a proton.[1][2][3][4][5]
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 4-aminobutanal:NAD+ 1-oxidoreductase. Other names in common use include gamma-guanidinobutyraldehyde dehydrogenase (ambiguous), ABAL dehydrogenase, 4-aminobutyraldehyde dehydrogenase, 4-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydrogenase, 1-pyrroline dehydrogenase, ABALDH, and YdcW. This enzyme participates in the urea cycle and the metabolism of amino groups and beta-alanine.[6]
References
- ^ Enzyme 1.2.1.19 at KEGG Pathway Database.
- ^ Matsuda H, Suzuki Y (1984). "gamma-Guanidinobutyraldehyde Dehydrogenase of Vicia faba Leaves". Plant Physiol. 76 (3): 654–657. doi:10.1104/pp.76.3.654. PMC 1064350. PMID 16663901.
- ^ Yorifuji T, Koike K, Sakurai T, Yokoyama K (1986). "4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida". Agric. Biol. Chem. 50 (8): 2009–2016. doi:10.1271/bbb1961.50.2009.
- ^ A; Martín-Checa, J; Balaña-Fouce, R; Garrido-Pertierra, A (1986). "A pathway for putrescine catabolism in Escherichia coli". Biochim. Biophys. Acta. 880 (2–3): 242–4. doi:10.1016/0304-4165(86)90085-1. PMID 3510672.
- ^ Prieto MI, Martin J, Balana-Fouce R, Garrido-Pertierra A (1987). "Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli". Biochimie. 69 (11–12): 1161–8. doi:10.1016/0300-9084(87)90142-8. PMID 3129020.
- ^ Samsonova NN, Smirnov SV, Novikova AE, Ptitsyn LR (2005). "Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase". FEBS Lett. 579 (19): 4107–12. Bibcode:2005FEBSL.579.4107S. doi:10.1016/j.febslet.2005.06.038. PMID 16023116.