Continued from EC 3.2.2 and EC 3.2.3
EC 3.3.1 Thioether and trialkylsulfonium hydrolases
EC 3.3.2 Ether Hydrolases
Accepted name: adenosylhomocysteinase
Reaction: S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
For diagram click here.
Other name(s): S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase
Systematic name: S-adenosyl-L-homocysteine hydrolase
Comments: The enzyme contains one tightly bound NAD+ per subunit. This appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond [2] (for mechanism click here), cf. EC 5.5.1.4, inositol-3-phosphate synthase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-54-1
References:
1. de la Haba, G. and Cantoni, G.L. The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine. J. Biol. Chem. 234 (1959) 603-608. [PMID: 13641268]
2. Palmer, J.L. and Abeles, R.H. The mechanism of action of S-adenosylhomocysteinase. J. Biol. Chem. 254 (1979) 1217-1226. [PMID: 762125]
Accepted name: adenosylmethionine hydrolase
Reaction: S-adenosyl-L-methionine + H2O = L-homoserine + methylthioadenosine
Other name(s): S-adenosylmethionine cleaving enzyme; methylmethionine-sulfonium-salt hydrolase; adenosylmethionine lyase
Systematic name: S-adenosyl-L-methionine hydrolase
Comments: Also hydrolyses methylmethionine sulfonium salt to dimethyl sulfide and homoserine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-62-3
References:
1. Mazelis, M., Levin, B. and Mallinson, N. Decomposition of methyl methionine sulfonium salts by a bacterial enzyme. Biochim. Biophys. Acta 105 (1965) 106-114. [PMID: 5849106]
[EC 3.3.1.3 Transferred entry: now EC 3.2.1.148 ribosylhomocysteinase (EC 3.3.1.3 created 1972, deleted 2001)]
Accepted name: isochorismatase
Reaction: isochorismate + H2O = 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
For diagram of reaction, click here.
Other name(s): 2,3-dihydro-2,3-dihydroxybenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoic synthase
Systematic name: isochorismate pyruvate-hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-64-5
References:
1. Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401-411. [PMID: 4306838]
Accepted name: alkenylglycerophosphocholine hydrolase
Reaction: 1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine
Other name(s): lysoplasmalogenase
Systematic name: 1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-65-6
References:
1. Arthur, G., Page, L., Mock, T. and Choy, P.C. The catabolism of plasmenylcholine in the guinea pig heart. Biochem. J. 236 (1986) 475-480. [PMID: 3753461]
2. Ellingson, J.S. and Lands, W.E.M. Phospholipid reactivation of plasmalogen metabolism. Lipids 3 (1968) 111-120.
3. Warner, H.R. and Lands, W.E.M. The metabolism of plasmalogen: enzymatic hydrolysis of the vinyl ether. J. Biol. Chem. 236 (1961) 2404-2409.
[EC 3.3.2.3 Transferred entry: epoxide hydrolase. Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10). (EC 3.3.2.3 created 1978, modified 1999, deleted 2006)]
Accepted name: trans-epoxysuccinate hydrolase
Reaction: trans-2,3-epoxysuccinate + H2O = meso-tartrate
Other name(s): trans-epoxysuccinate hydratase; tartrate epoxydase
Systematic name: trans-2,3-epoxysuccinate hydrolase
Comments: Acts on both optical isomers of the substrate. Formerly EC 4.2.1.37.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-73-6
References:
1. Allen, R.H. and Jakoby, W.B. Tartaric acid metabolism. IX. Synthesis with tartrate epoxidase. J. Biol. Chem. 244 (1969) 2078-2084. [PMID: 5782001]
Accepted name: alkenylglycerophosphoethanolamine hydrolase
Reaction: 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = an aldehyde + sn-glycero-3-phosphoethanolamine
Systematic name: 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine aldehydohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78413-08-8
References:
1. Gunawan, J. and Debuch, H. Liberation of free aldehyde from 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) by rat liver microsomes. Hoppe-Seyler's Z. Physiol. Chem. 362 (1981) 445-452. [PMID: 7239443]
Accepted name: leukotriene-A4 hydrolase
Reaction: leukotriene A4 + H2O = leukotriene B4
Glossary: leukotriene A4 = (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate
leukotriene B4 = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
Other name(s): LTA4 hydrolase; LTA4H; leukotriene A4 hydrolase
Systematic name: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate hydrolase
Comments: This is a bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities [4,6]. It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates [6] (see EC 3.4.11.6, aminopeptidase B). It also converts leukotriene A4 into leukotriene B4, unlike EC 3.3.2.10, soluble epoxide hydrolase, which converts leukotriene A4 into 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid [3,4]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol-5,6-oxide hydrolase) [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 90119-07-6
References:
1. Evans, J.F., Dupuis, P. and Ford-Hutchinson, A.W. Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils. Biochim. Biophys. Acta 840 (1985) 43-50. [PMID: 3995081]
2. Minami, M., Ohno, S., Kawasaki, H., Raadmark, O., Samuelsson, B., Jörnvall, H., Shimizu, T., Seyama, Y. and Suzuki, K. Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase - complete primary structure of an enzyme involved in eicosanoid synthesis. J. Biol. Chem. 262 (1987) 13873-13876. [PMID: 3654641]
3. Haeggström, J., Meijer, J. and Radmark, O. Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase. J. Biol. Chem. 261 (1986) 6332-6337. [PMID: 3009453]
4. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]
5. Fretland, A.J. and Omiecinski, C.J. Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 (2000) 41-59. [PMID: 11154734]
6. Orning, L., Gierse, J.K. and Fitzpatrick, F.A. The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity. J. Biol. Chem. 269 (1994) 11269-11267. [PMID: 8157657]
7. Ohishi, N., Izumi, T., Minami, M., Kitamura, S., Seyama, Y., Ohkawa, S., Terao, S., Yotsumoto, H., Takaku, F. and Shimizu, T. Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers. J. Biol. Chem. 262 (1987) 10200-10205. [PMID: 3038871]
Accepted name: hepoxilin-epoxide hydrolase
Reaction: hepoxilin A3 + H2O = trioxilin A3
Glossary: hepoxilin A3 = (5Z,9E,14Z)-(8ξ,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoate
trioxilin A3 = (5Z,9E,14Z)-(8ξ,11ξ,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate
Other name(s): hepoxilin epoxide hydrolase; hepoxylin hydrolase; hepoxilin A3 hydrolase
Systematic name: (5Z,9E,14Z)-(8ξ,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoate hydrolase
Comments: Converts hepoxilin A3 into trioxilin A3. Highly specific for the substrate, having only slight activity with other epoxides such as leukotriene A4 and styrene oxide [2]. Hepoxilin A3 is an hydroxy-epoxide derivative of arachidonic acid that is formed via the 12-lipoxygenase pathway [2]. It is probable that this enzyme plays a modulatory role in inflammation, vascular physiology, systemic glucose metabolism and neurological function [4]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122096-98-4
References:
1. Pace-Asciak, C.R. Formation and metabolism of hepoxilin A3 by the rat brain. Biochem. Biophys. Res. Commun. 151 (1988) 493-498. [PMID: 3348791]
2. Pace-Asciak, C.R. and Lee, W.-S. Purification of hepoxilin epoxide hydrolase from rat liver. J. Biol. Chem. 264 (1989) 9310-9313. [PMID: 2722835]
3. Fretland, A.J. and Omiecinski, C.J. Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 (2000) 41-59. [PMID: 11154734]
4. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]
Accepted name: limonene-1,2-epoxide hydrolase
Reaction: limonene-1,2-epoxide + H2O = limonene-1,2-diol
For diagram of reaction click here.
Glossary:
limonene = mentha-1,8-diene
limonene-1,2-epoxide = 1,2-epoxymenth-8-ene
limonene-1,2-diol = menth-8-ene-1,2-diol
Other name(s): limonene oxide hydrolase
Systematic name: limonene-1,2-epoxide hydrolase
Comment: Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. Enzyme hydrolyses several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. It differs from the previously described epoxide hydrolases [EC 3.3.2.4 (trans-epoxysuccinate hydrolase), EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase) and EC 3.3.2.10 (soluble epoxide hydrolase)] as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl dicarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 216503-88-7
References:
1. van der Werf, M.J., Overkamp, K.M. and de Bont, J.A.M. Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolases. J. Bacteriol. 180 (1998) 5052-5057. [PMID: 9748436]
2. Barbirato, F., Verdoes, J.C., de Bont, J.A.M. and van der Werf, M.J. The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases. FEBS Lett. 438 (1998) 293-296. [PMID: 9827564]
Accepted name: microsomal epoxide hydrolase
Reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol
Other name(s): epoxide hydratase (ambiguous); microsomal epoxide hydratase; epoxide hydrase; microsomal epoxide hydrase; arene-oxide hydratase (ambiguous); benzo[a]pyrene-4,5-oxide hydratase; benzo(a)pyrene-4,5-epoxide hydratase; aryl epoxide hydrase (ambiguous); cis-epoxide hydrolase; mEH
Systematic name: cis-stilbene-oxide hydrolase
Comments: This is a key hepatic enzyme that is involved in the metabolism of numerous xenobiotics, such as 1,3-butadiene oxide, styrene oxide and the polycyclic aromatic hydrocarbon benzo[a]pyrene 4,5-oxide [5—7]. In a series of oxiranes with a lipophilic substituent of sufficient size (styrene oxides), monosubstituted as well as 1,1- and cis-1,2-disubstituted oxiranes serve as substrates or inhibitors of the enzyme. However, trans-1,2-disubstituted, tri-and tetra-substituted oxiranes are not substrates [9]. The reaction involves the formation of an hydroxyalkyl—enzyme intermediate [10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol-5,6-oxide hydrolase) [7].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Jakoby, W.B. and Fjellstedt, T.A. Epoxidases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 7, Academic Press, New York, 1972, pp. 199-212.
2. Lu, A.Y., Ryan, D., Jerina, D.M., Daly, J.W. and Levin, W. Liver microsomal expoxide hydrase. Solubilization, purification, and characterization. J. Biol. Chem. 250 (1975) 8283-8288. [PMID: 240858]
3. Oesch, F. Purification and specificity of a human microsomal epoxide hydratase. Biochem. J. 139 (1974) 77-88. [PMID: 4463951]
4. Oesch, F. and Daly, J. Solubilization, purification, and properties of a hepatic epoxide hydrase. Biochim. Biophys. Acta 227 (1971) 692-697.
5. Bellucci, G., Chiappe, C. and Ingrosso, G. Kinetics and stereochemistry of the microsomal epoxide hydrolase-catalyzed hydrolysis of cis-stilbene oxides. Chirality 6 (1994) 577-582. [PMID: 7986671]
6. Morisseau, C. and Hammock, B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-333. [PMID: 15822179]
7. Fretland, A.J. and Omiecinski, C.J. Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 (2000) 41-59. [PMID: 11154734]
8. Oesch, F. Mammalian epoxide hydrases: inducible enzymes catalysing the inactivation of carcinogenic and cytotoxic metabolites derived from aromatic and olefinic compounds. Xenobiotica 3 (1973) 305-340. [PMID: 4584115]
9. Lacourciere, G.M. and Armstrong, R.N. Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes. Chem. Res. Toxicol. 7 (1994) 121-124. [PMID: 8199297]
10. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]
Accepted name: soluble epoxide hydrolase
Reaction: an epoxide + H2O = a glycol
Other name(s): epoxide hydrase (ambiguous); epoxide hydratase (ambiguous); arene-oxide hydratase (ambiguous); aryl epoxide hydrase (ambiguous); trans-stilbene oxide hydrolase; sEH; cytosolic epoxide hydrolase
Systematic name: epoxide hydrolase
Comments: Catalyses the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism [7]. It is involved in the metabolism of arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic acid epoxides. The EETs, which are endogenous chemical mediators, act at the vascular, renal and cardiac levels to regulate blood pressure [4,5]. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate phosphatase [1,2]. Like EC 3.3.2.9, microsomal epoxide hydrolase, it is probable that the reaction involves the formation of an hydroxyalkyl—enzyme intermediate [4,6]. The enzyme can also use leukotriene A4, the substrate of EC 3.3.2.6, leukotriene-A4 hydrolase, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B4 as the product [9,10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [7].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9048-63-9
References:
1. Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA 100 (2003) 1558-1563. [PMID: 12574510]
2. Cronin, A., Mowbray, S., Durk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc. Natl. Acad. Sci. USA 100 (2003) 1552-1557. [PMID: 12574508]
3. Oesch, F. Mammalian epoxide hydrases: inducible enzymes catalysing the inactivation of carcinogenic and cytotoxic metabolites derived from aromatic and olefinic compounds. Xenobiotica 3 (1973) 305-340. [PMID: 4584115]
4. Morisseau, C. and Hammock, B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-333. [PMID: 15822179]
5. Yu, Z., Xu, F., Huse, L.M., Morisseau, C., Draper, A.J., Newman, J.W., Parker, C., Graham, L., Engler, M.M., Hammock, B.D., Zeldin, D.C. and Kroetz, D.L. Soluble epoxide hydrolase regulates hydrolysis of vasoactive epoxyeicosatrienoic acids. Circ. Res. 87 (2000) 992-998. [PMID: 11090543]
6. Lacourciere, G.M. and Armstrong, R.N. The catalytic mechanism of microsomal epoxide hydrolase involves an ester intermediate. J. Am. Chem. Soc. 115 (1993) 10466-10456.
7. Fretland, A.J. and Omiecinski, C.J. Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 (2000) 41-59. [PMID: 11154734]
8. Zeldin, D.C., Wei, S., Falck, J.R., Hammock, B.D., Snapper, J.R. and Capdevila, J.H. Metabolism of epoxyeicosatrienoic acids by cytosolic epoxide hydrolase: substrate structural determinants of asymmetric catalysis. Arch. Biochem. Biophys. 316 (1995) 443-451. [PMID: 7840649]
9. Haeggström, J., Meijer, J. and Radmark, O. Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase. J. Biol. Chem. 261 (1986) 6332-6337. [PMID: 3009453]
10. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]
Accepted name: cholesterol-5,6-oxide hydrolase
Reaction: (1) 5,6α-epoxy-5α-cholestan-3β-ol + H2O = 5α-cholestane-3β,5α,6β-triol
(2) 5,6β-epoxy-5β-cholestan-3β-ol + H2O = 5α-cholestane-3β,5α,6β-triol
For diagram click here.
Glossary: cholesterol = cholest-5-en-3β-ol
Other name(s): cholesterol-epoxide hydrolase; ChEH
Systematic name: 5,6α-epoxy-5α-cholestan-3β-ol hydrolase
Comments: The enzyme appears to work equally well with either epoxide as substrate [3]. The product is a competitive inhibitor of the reaction. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Levin, W., Michaud, D.P., Thomas, P.E. and Jerina, D.M. Distinct rat hepatic microsomal epoxide hydrolases catalyze the hydration of cholesterol 5,6 α-oxide and certain xenobiotic alkene and arene oxides. Arch. Biochem. Biophys. 220 (1983) 485-494. [PMID: 6401984]
2. Oesch, F., Timms, C.W., Walker, C.H., Guenthner, T.M., Sparrow, A., Watabe, T. and Wolf, C.R. Existence of multiple forms of microsomal epoxide hydrolases with radically different substrate specificities. Carcinogenesis 5 (1984) 7-9. [PMID: 6690087]
3. Sevanian, A. and McLeod, L.L. Catalytic properties and inhibition of hepatic cholesterol-epoxide hydrolase. J. Biol. Chem. 261 (1986) 54-59. [PMID: 3941086]
4. Fretland, A.J. and Omiecinski, C.J. Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 (2000) 41-59. [PMID: 11154734]
5. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]