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ENZYME entry: EC 4.2.1.175

Accepted Name
(R)-3-(aryl)lactoyl-CoA dehydratase.
Alternative Name(s)
(R)-phenyllactoyl-CoA dehydratase.
Aryllactyl-CoA dehydratase.
Reaction catalysed
  • (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
Comment(s)
  • 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 2.8.3.17.
  • 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 5.6.1.9, 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.
Cross-references
BRENDA4.2.1.175
EC2PDB4.2.1.175
ExplorEnz4.2.1.175
PRIAM enzyme-specific profiles4.2.1.175
KEGG Ligand Database for Enzyme Nomenclature4.2.1.175
IUBMB Enzyme Nomenclature4.2.1.175
IntEnz4.2.1.175
MEDLINEFind literature relating to 4.2.1.175
MetaCyc4.2.1.175
Rhea expert-curated reactions4.2.1.175
UniProtKB/Swiss-Prot
Q93AL9, FLDB_CLOSG;  Q93AL8, FLDC_CLOSG;  

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