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MetaCyc Reaction: 4.2.1.119

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

EC Number: 4.2.1.119

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:4.2.1.119, ENZYME:EC:4.2.1.119, IUBMB-ExplorEnz:EC:4.2.1.119


References

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."


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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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