Publication: Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. Implication for the potential catalytic mechanism of enzymatic epoxide hydrolysis
Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. Implication for the potential catalytic mechanism of enzymatic epoxide hydrolysis
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Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., & Hammock, B. D. (1994). Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. Implication for the potential catalytic mechanism of enzymatic epoxide hydrolysis. FEBS Letters, 338, 251–256. https://doi.org/10.1016/0014-5793(94)80278-5
Abstract
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Abstract
Direct comparison of the amino acid sequences of microsomal and soluble epoxide hydrolase superficially indicates that these enzymes are unrelated. Both proteins, however, share significant sequence similarity to a bacterial haloalkane dehalogenase that has earlier been shown to belong to the alpha/beta hydrolase fold family of enzymes. The catalytic mechanism for the dehalogenase has been elucidated in detail [Verschueren et al. (1993) Nature 363, 693-698] and proceeds via an ester intermediate where the substrate is covalently bound
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- Arand, Michael
- Grant, D F
- Beetham, J K
- Friedberg, T
- Oesch, F
- Hammock, B D
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Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., & Hammock, B. D. (1994). Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. Implication for the potential catalytic mechanism of enzymatic epoxide hydrolysis. FEBS Letters, 338, 251–256. https://doi.org/10.1016/0014-5793(94)80278-5
