EC - Aminobutyraldehyde dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
aminobutyraldehyde dehydrogenase
Other names:
4-aminobutanal dehydrogenase
4-aminobutyraldehyde dehydrogenase
γ-aminobutyraldehyde dehydroganase
γ-guanidinobutyraldehyde dehydrogenase [ambiguous]
ABAL dehydrogenase
1-pyrroline dehydrogenase
Systematic name:
4-aminobutanal:NAD+ 1-oxidoreductase



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 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
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033737 , GO:0019145
CAS Registry Number: 9028-98-2
UniProtKB/Swiss-Prot: (63) [show] [UniProt]


  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 : 1737-1741 (1974). [PMID: 4817964]
  2. Jakoby, W.B.
    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
  3. Jakoby, W.B. and Fredericks, J.
    Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase.
    J. Biol. Chem. 234 : 2145-2150 (1959). [PMID: 13673029]
  4. Matsuda, H. and Suzuki, Y.
    γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves.
    Plant Physiol. 76 : 654-657 (1984). [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 : 2009-2016 (1986).
  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 : 242-244 (1986). [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 : 1161-1168 (1987). [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 : 4107-4112 (2005). [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 : 29-41 (2004). [PMID: 1538141]

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