Open AccessThe thiocarbamate‐inducible Rhodococcus enzyme ThcF as a member of the family of α/β hydrolases with haloperoxidative side activity
Author(s) -
Mot René,
Schrijver Adinda,
Schoofs Geert,
Parret Annabel H.A
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00452-x
Subject(s) - thiocarbamate , chemistry , biochemistry , enzyme , rhodococcus , organic chemistry
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 α/β 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.