EC number:1.3.1.31

Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.1 With NAD+ or NADP+ as acceptor
ID:1.3.1.31
Description:2-enoate reductase.
Alternative Name: Enoate reductase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.1.31
BRENDA Enzyme Link: BRENDA 1.3.1.31
KEGG Enzyme Link: KEGG1.3.1.31
BioCyc Enzyme Link: BioCyc 1.3.1.31
ExPASy Enzyme Link: ExPASy1.3.1.31
EC2PDB Enzyme Link: EC2PDB 1.3.1.31
ExplorEnz Enzyme Link: ExplorEnz 1.3.1.31
PRIAM enzyme-specific profiles Link: PRIAM 1.3.1.31
IntEnz Enzyme Link: IntEnz 1.3.1.31
MEDLINE Enzyme Link: MEDLINE 1.3.1.31

EC number:1.3.1.31

MSA:

1.3.1.31;
Phylogenetic Tree:

1.3.1.31;
Uniprot:
M-CSA:
RHEA:10200 butanoate + NAD(+) = (2E)-2-butenoate + H(+) + NADH
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
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References

TitleAuthorsDatePubMed ID
On the kinetics and mechanism of enoate reductase.Bühler M, Simon H1982 Jun7106707
Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of alpha, beta-unsaturated carboxylate anions.Tischer W, Bader J, Simon H1979 Jun477658