Open AccessIdentification of a novel B aeyer‐ V illiger monooxygenase from A cinetobacter radioresistens : close relationship to the M ycobacterium tuberculosis prodrug activator EtaA
Author(s) -
Minerdi Daniela,
Zgrablic Ivan,
Sadeghi Sheila J.,
Gilardi Gianfranco
Publication year - 2012
Publication title -
microbial biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.287
H-Index - 74
ISSN - 1751-7915
DOI - 10.1111/j.1751-7915.2012.00356.x
Subject(s) - chemistry , in silico , ethionamide , biochemistry , biology , gene , antibiotics , rifampicin , ethambutol
Summary This work demonstrates that A cinetobacter radioresistens strain S 13 during the growth on medium supplemented with long‐chain alkanes as the sole energy source expresses alm A gene coding for a B aeyer‐ V illiger monooxygenase ( BVMO ) involved in alkanes subterminal oxidation. Phylogenetic analysis placed the sequence of this novel BVMO in the same clade of the prodrug activator ethionamide monooxygenase ( EtaA ) and it bears only a distant relation to the other known class I BVMO proteins. In silico analysis of the 3 D model of the S 13 BVMO generated by homology modelling also supports the similarities with EtaA by binding ethionamide to the active site. In vitro experiments carried out with the purified enzyme confirm that this novel BVMO is indeed capable of typical B aeyer‐ V illiger reactions as well as oxidation of the prodrug ethionamide.