The thiocarbamate-inducible Rhodococcus enzyme ThcF as a member of the family of α/β hydrolases with haloperoxidative side activity

被引：8

作者：

De Mot, R ^{[1
]}

De Schrijver, A ^{[1
]}

Schoofs, G ^{[1
]}

Parret, AHA ^{[1
]}

机构：

[1] Catholic Univ Louvain, Dept Appl Platn Sci, Ctr Microbial & Plant Genet, B-3001 Heverlee, Belgium

来源：

FEMS MICROBIOLOGY LETTERS | 2003年 / 224卷 / 02期

关键词：

alpha/beta hydrolase; esterase; non-heme haloperoxidase; thiocarbamate herbicide; LAL regulator family; HASH family;

D O I：

10.1016/S0378-1097(03)00452-X

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Purified thiocarbamate-inducible ThcF of Rhodococcus erythropolis N186/21, overexpressed in Escherichia coli, displayed several characteristics of the HASH family of enzymes that groups prokaryotic proteins of the alp hydrolase superfamily possessing serine-dependent hydrolase and/or haloperoxidase activity. Kinetic analysis of bromination and ester hydrolysis revealed a low affinity of ThcF for model substrates. Sulfoxidation of thiocarbamates was demonstrated but probably represents a side activity due to peroxoacid generation by the enzyme. The thcF-linked thcG gene, encoding a LAL-type regulator, triggers expression of thcF in Rhodococcus. The tandem gene organization thcG-thcF is conserved in the thiocarbamate-degrading strain Rhodococcus sp. 1330. It is proposed that HASH enzymes may be involved in the metabolism of plant-derived compounds. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：197 / 203

页数：7

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