EC 1.3.1.74 - 2-alkenal reductase [NAD(P)+]

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IntEnz Enzyme Nomenclature
EC 1.3.1.74

Names

Accepted name:
2-alkenal reductase [NAD(P)+]
Other names:
NAD(P)H-dependent alkenal/one oxidoreductase
NADPH:2-alkenal α,β-hydrogenase
2-alkenal reductase
Systematic name:
n-alkanal:NAD(P)+ 2-oxidoreductase

Reaction

Comments:

Highly specific for 4-hydroxynon-2-enal and non-2-enal. Alk-2-enals of shorter chain have lower affinities. Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one. Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid. Involved in the detoxication of α,β-unsaturated aldehydes and ketones [cf. EC 1.3.1.102, 2-alkenal reductase (NADP+)].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0032440
CAS Registry Numbers: 137367-20-5 57406-74-3 9032-20-6
UniProtKB/Swiss-Prot:

References

  1. Mano, J., Torii, Y., Hayashi, S., Takimoto, K., Matsui, K., Nakamura, K., Inzé, D., Babiychuk, E., Kushnir, S. and Asada, K.
    The NADPH:quinone oxidoreductase P1-ζ-crystallin in Arabidopsis catalyzes the α,β-hydrogenation of 2-alkenals: detoxication of the lipid peroxide-derived reactive aldehydes.
    Plant Cell Physiol. 43: 1445-1455 (2002). [PMID: 12514241]
  2. Dick, R.A., Kwak, M.K., Sutter, T.R. and Kensler, T.W.
    Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase.
    J. Biol. Chem. 276: 40803-40810 (2001). [PMID: 11524419]

[EC 1.3.1.74 created 2003, modified 2014]