| Title : The thiocarbamate-inducible Rhodococcus enzyme ThcF as a member of the family of alpha\/beta hydrolases with haloperoxidative side activity - De Mot_2003_FEMS.Microbiol.Lett_224_197 |
| Author(s) : De Mot R , De Schrijver A , Schoofs G , Parret AH |
| Ref : FEMS Microbiology Letters , 224 :197 , 2003 |
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Abstract :
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. |
| PubMedSearch : De Mot_2003_FEMS.Microbiol.Lett_224_197 |
| PubMedID: 12892883 |
| Gene_locus related to this paper: rhoer-thcf |
| Gene_locus | rhoer-thcf |
De Mot R, De Schrijver A, Schoofs G, Parret AH (2003)
The thiocarbamate-inducible Rhodococcus enzyme ThcF as a member of the family of alpha\/beta hydrolases with haloperoxidative side activity
FEMS Microbiology Letters
224 :197
De Mot R, De Schrijver A, Schoofs G, Parret AH (2003)
FEMS Microbiology Letters
224 :197