Aminobutyraldehyde dehydrogenase
This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations. (December 2021) |
aminobutyraldehyde dehydrogenase | |||||||||
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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 | ||||||||
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In enzymology, an aminobutyraldehyde dehydrogenase (EC 1.2.1.19) is an enzyme that catalyzes the chemical reaction
- 4-aminobutanal + NAD+ + H2O 4-aminobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-aminobutanal, NAD+, and H2O, whereas its 3 products are 4-aminobutanoate, NADH, 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 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.
References
[edit]- Callewaert, Denis M.; Rosemblatt, Mario S.; Tchen, T. T. (1974-03-25). "Purification and Properties of 4-Aminobutanal Dehydrogenase from a Pseudomonas Species". Journal of Biological Chemistry. 249 (6): 1737–1741. ISSN 0021-9258. PMID 4817964. Retrieved 2019-04-08.
- Boyer, P.D.; Lardy, H.; Myrback, K., eds. (1963). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 203–221.
- Jakoby, William B.; Fredericks, Joan (1959-08-01). "Pyrrolidine and Putrescine Metabolism: γ-Aminobutyraldehyde Dehydrogenase". Journal of Biological Chemistry. 234 (8): 2145–2150. ISSN 0021-9258. PMID 13673029. Retrieved 2019-04-08.
- 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. doi:10.1016/j.febslet.2005.06.038. PMID 16023116.