| EC |
1.3.1.74 |
| Accepted name: |
2-alkenal reductase [NAD(P)+] |
| Reaction: |
a n-alkanal + NAD(P)+ = an alk-2-enal + NAD(P)H + H+ |
| Other name(s): |
NAD(P)H-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase; 2-alkenal reductase |
| Systematic name: |
n-alkanal:NAD(P)+ 2-oxidoreductase |
| 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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 52227-95-9 |
| 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 (2002) 1445–1455. [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 (2001) 40803–40810. [DOI] [PMID: 11524419] |
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| [EC 1.3.1.74 created 2003, modified 2014] |
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