Enoyl-CoA hydratase (EC 4.2.1.17) (ECH) [1] and D3,D2-enoyl-CoA isomerase
(EC 5.3.3.8) (ECI) [2] are two enzymes involved in fatty acid metabolism. ECH
catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA and ECI
shifts the 3- double bond of the intermediates of unsaturated fatty acid
oxidation to the 2-trans position.
Most eukaryotic cells have two fatty-acid β-oxidation systems, one located
in mitochondria and the other in peroxisomes. In mitochondria, ECH and ECI are
separate yet structurally related monofunctional enzymes. Peroxisomes contain
a trifunctional enzyme [3] consisting of an N-terminal domain that bears both
ECH and ECI activity, and a C-terminal domain responsible for 3-hydroxyacyl-CoA dehydrogenase (HCDH) activity.
In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA), ECH and ECI
are also part of a multifunctional enzyme which contains both a HCDH and a
3-hydroxybutyryl-CoA epimerase domain [4].
A number of other proteins have been found to be evolutionary related to the
ECH/ECI enzymes or domains:
3-hydroxbutyryl-coa dehydratase (EC 4.2.1.55) (crotonase), a bacterial
enzyme involved in the butyrate/butanol-producing pathway.
Naphthoate synthase (EC 4.1.3.36) (DHNA synthase) (gene menB) [5], a
bacterial enzyme involved in the biosynthesis of menaquinone (vitamin K2).
DHNA synthase converts O-succinyl-benzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
naphthoic acid (DHNA).
4-chlorobenzoate dehalogenase (EC 3.8.1.6) [6], a Pseudomonas enzyme which
catalyzes the conversion of 4-chlorobenzoate-CoA to 4-hydroxybenzoate-CoA.
A Rhodobacter capsulatus protein of unknown function (ORF257) [7].
Bacillus subtilis putative polyketide biosynthesis proteins pksH and pksI.
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References
1
Authors
Minami-Ishii N. Taketani S. Osumi T. Hashimoto T.
Source
Eur. J. Biochem. 185:73-78(1989).
2
Authors
Mueller-Newen G. Stoffel W.
Source
Biol. Chem. Hoppe-Seyler 372:613-624(1991).
3
Authors
Palosaari P.M. Hiltunen J.K.
Title
Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities.
Babbitt P.C. Kenyon G.L. Martin B.M. Charest H. Slyvestre M. Scholten J.D. Chang K.-H. Liang P.-H. Dunaway-Mariano D.
Title
Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases.
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