EC 1.3.1.102 - 2-alkenal reductase (NADP+)

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IntEnz Enzyme Nomenclature
EC 1.3.1.102

Names

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

Reaction

Comments:

Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde [3]. Involved in the detoxication of α,β-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Hirata, T., Tamura, Y., Yokobatake, N., Shimoda, K., Ashida, Y.
    A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum.
    Phytochemistry 55 : 297-303 (2000). [PMID: 11117876]
  2. Matsushima, A., Sato, Y., Otsuka, M., Watanabe, T., Yamamoto, H., Hirata, T.
    An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins.
    Bioorg. Chem. 36 : 23-28 (2008). [PMID: 17945329]
  3. Mansell, D.J., Toogood, H.S., Waller, J., Hughes, J.M.X., Levy, C.W., Gardiner, J.M., and Scrutton, N.S.
    Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum.
    ACS Catal. 3 : 370-379 (2013).

[EC 1.3.1.102 created 2013]