Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes.
Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes.
复制标题
微粒体和可溶性环氧化物水解酶是同一 C-X 键水解酶家族的成员。
DOI：
10.1021/tx00038a001
复制
发表时间：
1994
影响因子：
4.1
通讯作者：
Armstrong,RN
中科院分区：
文献类型：
--
作者：
Lacourciere,GM;Armstrong,RN
Sequence alignments of mammalian microsomal (MEH) and soluble epoxide hydrolases (SEH) with bacterial haloalkanedehalogenase (HAD) and haloacetate dehalogenase (HAcD) together with structural and functional evidence suggest that these four enzymes are structurally and mechanistically related. The catalytic mechanism of HAD and MEH have been recently shown to involve an ester intermediate formed by alkylation of an active site carboxyl group. Very pronounced sequence similarities of regions of MEH, SEH, and HAcD with the activesite of HAD suggest that all four enzymes belong tothe same family of CX bond hydrolases which involve an alkyl-enzyme intermediate. The catalytic triads (nucleophile-base-acid) of MEH and SEH are proposed to be Asp226-His431-Asp352 and Asp333-His523-Asp495, respectively, on the basis of sequence alignments with HAD. Althoughcompelling arguments, through sequence alignments, can be made for the assignment of the nucleophile-basepair of the triad, the identity ofthe acid residue (eg, Asp352 and Asp495) is more speculative. The threedimensional structures of both MEH and SEH are suggested to contain structural elements of the/ß hydrolase fold.
