View source for 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

{{enzyme
| Name = 2-enoate reductase
| EC_number = 1.3.1.31
| CAS_number = 70712-51-5
| IUBMB_EC_number = 1/3/1/31
| GO_code = 0047540
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''2-enoate reductase''' ({{EC number|1.3.1.31}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:butanoate + NAD<sup>+</sup> <math>\rightleftharpoons</math> 2-butenoate + NADH + H<sup>+</sup>

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[butanoate]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[2-butenoate]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor.  The systematic name of this enzyme class is '''butanoate:NAD+ Delta2-oxidoreductase'''. This enzyme is also called '''enoate reductase'''.  This enzyme participates in [[phenylalanine metabolism]].  It has 4 [[cofactor (biochemistry)|cofactors]]: [[FAD]], [[Iron]], [[Sulfur]],  and [[Iron-sulfur]].  

==References==
{{reflist|1}}
* {{cite journal | author = Tischer W, Bader J, Simon H | date = 1979 | title = Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of alpha, beta-unsaturated carboxylate anions | journal = Eur. J. Biochem.  | volume = 97 | pages = 103&ndash;12  | pmid = 477658 | doi = 10.1111/j.1432-1033.1979.tb13090.x | issue = 1 }}

{{1.3-enzyme-stub}}

[[Category:EC 1.3.1]]
[[Category:NADH-dependent enzymes]]
[[Category:Flavin enzymes]]
[[Category:Iron enzymes]]
[[Category:Sulfur enzymes]]
[[Category:Iron-sulfur enzymes]]
[[Category:Enzymes of unknown structure]]