PROSITE documentation PDOC00150Enoyl-CoA hydratase/isomerase signature
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.
- Escherichia coli carnitine racemase (gene caiD) [8].
- Escherichia coli hypothetical protein ygfG.
- Yeast hypothetical protein YDR036c.
As a signature pattern for these enzymes, we selected a conserved region rich in glycine and hydrophobic residues.
Expert(s) to contact by email: Last update:December 2004 / Pattern and text revised.
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| 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. | |
| Source | J. Biol. Chem. 265:2446-2449(1990). | |
| PubMed ID | 2303409 |
| 4 | Authors | Nakahigashi K. Inokuchi H. |
| Title | Nucleotide sequence of the fadA and fadB genes from Escherichia coli. | |
| Source | Nucleic Acids Res. 18:4937-4937(1990). | |
| PubMed ID | 2204034 |
| 5 | Authors | Driscoll J.R. Taber H.W. |
| Title | Sequence organization and regulation of the Bacillus subtilis menBE operon. | |
| Source | J. Bacteriol. 174:5063-5071(1992). | |
| PubMed ID | 1629163 |
| 6 | Authors | 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. | |
| Source | Biochemistry 31:5594-5604(1992). | |
| PubMed ID | 1351742 |
| 7 | Authors | Beckman D.L. Kranz R.G. |
| Title | A bacterial homolog to the mitochondrial enoyl-CoA hydratase. | |
| Source | Gene 107:171-172(1991). | |
| PubMed ID | 1743516 |
| 8 | Authors | Eichler K. Bourgis F. Buchet A. Kleber H.-P. Mandrand-Berthelot M.-A. |
| Title | Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. | |
| Source | Mol. Microbiol. 13:775-786(1994). | |
| PubMed ID | 7815937 |
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