Diketocamphane enantiomer-specific "Baeyer-Villiger" monooxygenases from camphor-grown Pseudomonas putida ATCC 17453
نویسندگان
چکیده
منابع مشابه
Flavin-Dependent Redox Transfers by the Two-Component Diketocamphane Monooxygenases of Camphor-Grown Pseudomonas putida NCIMB 10007
The progressive titres of key monooxygenases and their requisite native donors of reducing power were used to assess the relative contribution of various camphor plasmid (CAM plasmid)- and chromosome-coded activities to biodegradation of (rac)-camphor at successive stages throughout growth of Pseudomonas putida NCIMB 10007 on the bicylic monoterpenoid. A number of different flavin reductases (F...
متن کاملConversion of Furans by Baeyer-Villiger Monooxygenases
Various furans are considered as valuable platform chemicals as they can be derived from plant biomass. Yet, for their exploitation, follow-up chemistry is required. Here we demonstrate that Baeyer-Villiger monooxygenases (BVMOs) can be used as biocatalysts for the selective oxidation of several furans, including 5-(hydroxymethyl) furfural (HMF) and furfural. A total of 15 different BVMOs were ...
متن کاملIdentifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases.
The Baeyer-Villiger monooxygenase (BVMO), 4-hydroxyacetophenone monooxygenase (HAPMO), uses NADPH and O(2) to oxidize a variety of aromatic ketones and sulfides. The FAD-containing enzyme has a 700-fold preference for NADPH over NADH. Sequence alignment with other BVMOs, which are all known to be selective for NADPH, revealed three conserved basic residues, which could account for the observed ...
متن کاملBaeyer-Villiger monooxygenases, an emerging family of flavin-dependent biocatalysts
Baeyer-Villiger monooxygenases (BVMO) are flavoenzymes that catalyze a remarkably wide variety of oxidative reactions such as regioand enantioselective Baeyer-Villiger oxidations and sulfoxidations. Several of these conversions are difficult to achieve using chemical approaches. Due to their selectivity and catalytic efficiency, BVMOs are highly valuable biocatalysts for synthesis of a broad ra...
متن کاملThe oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase
The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1993
ISSN: 0022-1287
DOI: 10.1099/00221287-139-4-797