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
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
收藏
页码:197 / 203
页数:7
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