De Mot René, De Schrijver Adinda, Schoofs Geert, Parret Annabel H A
Department of Applied Plant Sciences, Catholic University of Leuven, Kasteelpark Arenberg 20, B-3001 Heverlee, Belgium.
FEMS Microbiol Lett. 2003 Jul 29;224(2):197-203. doi: 10.1016/S0378-1097(03)00452-X.
Purified thiocarbamate-inducible ThcF of Rhodococcus erythropolis NI86/21, overexpressed in Escherichia coli, displayed several characteristics of the HASH family of enzymes that groups prokaryotic proteins of the alpha/beta 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. B30. It is proposed that HASH enzymes may be involved in the metabolism of plant-derived compounds.
在大肠杆菌中过表达的红平红球菌NI86/21纯化的硫代氨基甲酸盐诱导型ThcF，表现出HASH酶家族的几个特征，该家族将具有丝氨酸依赖性水解酶和/或卤过氧化物酶活性的α/β水解酶超家族的原核蛋白归为一类。溴化和酯水解的动力学分析表明，ThcF对模型底物的亲和力较低。硫代氨基甲酸盐的硫氧化已得到证实，但这可能是由于该酶产生过氧酸而导致的一种副活性。编码LAL型调节因子的thcF连锁thcG基因可触发红球菌中thcF的表达。硫代氨基甲酸盐降解菌株红球菌B30中thcG-thcF串联基因组织是保守的。有人提出，HASH酶可能参与植物衍生化合物的代谢。
