ExplorEnz: EC 1.2.1.19

Your query returned 1 entry. Printable version

1.2.1.19

Accepted name:

aminobutyraldehyde dehydrogenase

Reaction:

4-aminobutanal + NAD⁺ + H₂O = 4-aminobutanoate + NADH + 2 H⁺

For diagram of arginine catabolism, click here

Glossary:

4-aminobutanoate = γ-aminobutyrate = GABA

Other name(s):

γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW

Systematic name:

4-aminobutanal:NAD⁺ 1-oxidoreductase

Comments:

The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9028-98-2

References:

1.	Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737–1741. [PMID: 4817964]
2.	Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
3.	Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145–2150. [PMID: 13673029]
4.	Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654–657. [PMID: 16663901]
5.	Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016.
6.	Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672]
7.	Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161–1168. [DOI] [PMID: 3129020]
8.	Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116]
9.	Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29–41. [DOI] [PMID: 15381418]

[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]