Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases
نویسندگان
چکیده
منابع مشابه
Identifying 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 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 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 Origin and Evolution of Baeyer—Villiger Monooxygenases (BVMOs): An Ancestral Family of Flavin Monooxygenases
The Baeyer-Villiger Monooxygenases (BVMOs) are enzymes belonging to the "Class B" of flavin monooxygenases and are capable of performing exquisite selective oxidations. These enzymes have been studied from a biotechnological perspective, but their physiological substrates and functional roles are widely unknown. Here, we investigated the origin, taxonomic distribution and evolutionary history o...
متن کاملExploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase.
Steroid monooxygenase (STMO) from Rhodococcus rhodochrous catalyzes the Baeyer-Villiger conversion of progesterone into progesterone acetate using FAD as prosthetic group and NADPH as reducing cofactor. The enzyme shares high sequence similarity with well characterized Baeyer-Villiger monooxygenases, including phenylacetone monooxygenase and cyclohexanone monooxygenase. The comparative biochemi...
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: European Journal of Biochemistry
سال: 2004
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.2004.04126.x