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Functional and structural comparisons of cysteine residues in the Val108 wild type and Met108 variant of human soluble catechol O-methyltransferase

Authors
Yan LiXiaofeng Yang장민선James D. YagerRichard B. van BreemenJudy L. Bolton
Issue Date
Apr-2005
Publisher
Elsevier
Keywords
COMT; gene polymorphism; estrogen replacement therapy; 4-hydroxyequilenin
Citation
Chemico Biological Interactions, v.152, no.2-3, pp.151 - 163
Journal Title
Chemico Biological Interactions
Volume
152
Number
2-3
Start Page
151
End Page
163
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/148792
DOI
10.1016/j.cbi.2005.03.001
ISSN
0009-2797
Abstract
Catechol O-methyltransferase (COMT) plays an important role in the inactivation of biologically active and toxic catechols. This enzyme is genetically polymorphic with a wild type and a variant form. Numerous epidemiological studies have shown that the variant form is associated with an increased risk of developing estrogen-associated cancers and a wide spectrum of mental disorders. There are seven cysteine residues in human S-COMT, all of which exist as free thiols and are susceptible to electrophilic attack and/or oxidative damage leading to enzyme inactivation. Here, the seven cysteine residues were systematically replaced by alanine residues by means of site-directed mutagenesis. The native forms and cysteine/alanine mutants were assayed for enzymatic activity, thermal stability, methylation regioselectivity, and reactivity of cysteine residues to thiol reagent. Our data showed that although there is only one encoding base difference between these two COMT forms, this difference might induce structural changes in the local area surrounding some cysteine residue, which might further contribute to the different roles they might play in enzymatic activity, and to the different susceptibility to enzyme inactivation, (c) 2005 Elsevier Ireland Ltd. All rights reserved.
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