EC 1 - Oxidoreductases
EC 1.2 - Acting on the aldehyde or oxo group of donors
EC 1.2.1 - With NAD+ or NADP+ as acceptor
EC 1.2.1.19 - Aminobutyraldehyde dehydrogenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.2.1.19
Names
Accepted name:
aminobutyraldehyde dehydrogenase
Other
names:
4-aminobutanal dehydrogenase
4-aminobutyraldehyde dehydrogenase
γ-aminobutyraldehyde dehydroganase
γ-guanidinobutyraldehyde dehydrogenase [ambiguous]
ABAL dehydrogenase
1-pyrroline dehydrogenase
ABALDH
YdcW
4-aminobutyraldehyde dehydrogenase
γ-aminobutyraldehyde dehydroganase
γ-guanidinobutyraldehyde dehydrogenase [ambiguous]
ABAL dehydrogenase
1-pyrroline dehydrogenase
ABALDH
YdcW
Systematic name:
4-aminobutanal:NAD+ 1-oxidoreductase
Reaction
- 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00068
Gene Ontology:
GO:0033737
,
GO:0019145
CAS Registry Number:
9028-98-2
References
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Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species.J. Biol. Chem. 249 : 1737-1741 (1974). [PMID: 4817964]
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Aldehyde dehydrogenase.In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 7 , Academic Press , New York , 1963 , 203-221
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Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase.J. Biol. Chem. 234 : 2145-2150 (1959). [PMID: 13673029]
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γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves.Plant Physiol. 76 : 654-657 (1984). [PMID: 16663901]
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4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida.Agric. Biol. Chem. 50 : 2009-2016 (1986).
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A pathway for putrescine catabolism in Escherichia coli.Biochim. Biophys. Acta 880 : 242-244 (1986). [PMID: 3510672]
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Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli.Biochimie 69 : 1161-1168 (1987). [PMID: 3129020]
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Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase.FEBS Lett. 579 : 4107-4112 (2005). [PMID: 16023116]
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Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase.J. Mol. Biol. 343 : 29-41 (2004). [PMID: 1538141]
[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]