MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Candida albicans SC5314: D-specific enoyl-CoA hydratase: FOX2
Cucumis sativus: very-long-chain 3-hydroxyacyl-CoA dehydratase
Homo sapiens: peroxisomal multifunctional enzyme type 2: HSD17B4
Pseudomonas oleovorans: (R)-specific enoyl-CoA hydratase: phaJ1
Rattus norvegicus: 3-hydroxyacyl-CoA dehydraseInferred from experiment
Saccharomyces cerevisiae: peroxisomal multifunctional enzyme type 2: FOX2

In Pathway: stearate biosynthesis I (animals and fungi)

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: enoyl-CoA hydratase 2

Enzyme Commission Synonyms: 2-enoyl-CoA hydratase 2, AtECH2, ECH2, MaoC, MFE-2, PhaJAc, D-3-hydroxyacyl-CoA hydro-lyase, D-specific 2-trans-enoyl-CoA hydratase

Standard Gibbs Free Energy (ΔrG): 2.1629639 kcal/molInferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
This enzyme catalyses a hydration step in peroxisomal β-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units [Koski05]. The enzymes from Aeromonas caviae [Hisano01] and Arabidopsis thaliana [Goepfert06] are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 [Koski03].

Citations: [Fukui98, Engeland91 ]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R07760

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Engeland91: Engeland K, Kindl H (1991). "Evidence for a peroxisomal fatty acid beta-oxidation involving D-3-hydroxyacyl-CoAs. Characterization of two forms of hydro-lyase that convert D-(-)-3-hydroxyacyl-CoA into 2-trans-enoyl-CoA." Eur J Biochem 200(1);171-8. PMID: 1879422

Fukui98: Fukui T, Shiomi N, Doi Y (1998). "Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae." J Bacteriol 180(3);667-73. PMID: 9457873

Goepfert06: Goepfert S, Hiltunen JK, Poirier Y (2006). "Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana." J Biol Chem 281(47);35894-903. PMID: 16982622

Hisano01: Hisano T, Fukui T, Iwata T, Doi Y (2001). "Crystallization and preliminary X-ray analysis of (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis." Acta Crystallogr D Biol Crystallogr 57(Pt 1);145-7. PMID: 11134939

Koski03: Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T (2003). "Crystallization and preliminary crystallographic data of 2-enoyl-CoA hydratase 2 domain of Candida tropicalis peroxisomal multifunctional enzyme type 2." Acta Crystallogr D Biol Crystallogr 59(Pt 7);1302-5. PMID: 12832794

Koski05: Koski KM, Haapalainen AM, Hiltunen JK, Glumoff T (2005). "Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2." J Mol Biol 345(5);1157-69. PMID: 15644212

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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