Paper Report for: De Mot_2003_FEMS.Microbiol.Lett_224_197
Reference
Title: The thiocarbamate-inducible Rhodococcus enzyme ThcF as a member of the family of alpha/beta hydrolases with haloperoxidative side activity De Mot R, De Schrijver A, Schoofs G, Parret AH Ref: FEMS Microbiology Letters, 224:197, 2003 : PubMed
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.
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 Letters224: 197-203
De Mot R, De Schrijver A, Schoofs G, Parret AH (2003) FEMS Microbiology Letters224: 197-203