Residue 345 of dibenzothiophene (DBT) sulfone monooxygenase is involved in C-S bond cleavage specificity of alkylated DBT sulfones.
Biotechnol Lett
; 25(14): 1199-202, 2003 Jul.
Article
em En
| MEDLINE
| ID: mdl-12967013
ABSTRACT
Rhodococcus erythropolis IGTS8 that possesses dibenzothiophene sulfone monooxygenase mutated at residue 345 (Q345A), can degrade octyl sulfide on which the wild strain cannot grow. Residue 345 and the neighbouring residues were changed by site-directed mutagenesis. Only DszA changed at residue 345 gave an altered C-S bond cleavage pattern of 3-methyl DBT sulfone. This residue is therefore involved in C-S bond cleavage specifically for alkylated DBT sulfone.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Oxigenases
/
Enxofre
/
Tiofenos
/
Rhodococcus
Idioma:
En
Revista:
Biotechnol Lett
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Japão