ENZYME entry: EC 188.8.131.52
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- (R)-3-(phenyl)lactoyl-CoA <=> (E)-cinnamoyl-CoA + H(2)O
- (R)-3-(4-hydroxyphenyl)lactoyl-CoA <=> (E)-4-coumaroyl-CoA + H(2)O
- (R)-3-(indol-3-yl)lactoyl-CoA <=> 3-(indol-3-yl)acryloyl-CoA + H(2)O
- The enzyme, found in some amino acid-fermenting anaerobic bacteria,
participates in the fermentation pathways of L-phenylalanine,
L-tyrosine, and L-tryptophan.
- It is a heterodimeric protein consisting of the FldB and
FldC polypeptides, both of which contain an [4Fe-4S] cluster,
and forms a complex with EC 184.108.40.206.
- In order to catalyze the reaction, the enzyme requires one high-
energy electron that transiently reduces the electrophilic thiol
ester carbonyl of the substrate to a nucleophilic ketyl radical
anion, facilitating the elimination of the hydroxyl group.
- This electron, which is provided by by EC 220.127.116.11, needs to be
supplied only once, before the first reaction takes place, as it is
regenerated at the end of each reaction cycle.
- The enzyme acts on (R)-3-(aryl)lactoyl-CoAs produced by FldA,
and regenerates the CoA donors used by that enzyme.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|Rhea expert-curated reactions||184.108.40.206|
entries corresponding to 4.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-