4-Hydroxyacetophenone monooxygenase fromPseudomonas fluorescensACB
نویسندگان
چکیده
منابع مشابه
Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenase.
The 4-hydroxyacetophenone monooxygenase (HAPMO) from Pseudomonas fluorescens ACB catalyzes NADPH- and oxygen-dependent Baeyer-Villiger oxidation of 4-hydroxyacetophenone to the corresponding acetate ester. Using the purified enzyme from recombinant Escherichia coli, we found that a broad range of carbonylic compounds that are structurally more or less similar to 4-hydroxyacetophenone are also s...
متن کاملCoenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase.
The NADPH-dependent dimeric flavoenzyme 4-hydroxyacetophenone monooxygenase (HAPMO) catalyzes Baeyer-Villiger oxidations of a wide range of ketones, thereby generating esters or lactones. In the current work, we probed HAPMO-coenzyme complexes present during the enzyme catalytic cycle with the aim to gain mechanistic insight. Moreover, we investigated the structural role of the nicotinamide coe...
متن کاملCloning, expression, characterization, and biocatalytic investigation of the 4-hydroxyacetophenone monooxygenase from Pseudomonas putida JD1.
While the number of available recombinant Baeyer-Villiger monooxygenases (BVMOs) has grown significantly over the last few years, there is still the demand for other BVMOs to expand the biocatalytic diversity. Most BVMOs that have been described are dedicated to convert efficiently cyclohexanone and related cyclic aliphatic ketones. To cover a broader range of substrate types and enantio- and/o...
متن کاملConversion of 4-hydroxyacetophenone into 4-phenyl acetate by a flavin adenine dinucleotide-containing Baeyer-Villiger-type monooxygenase.
An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monom...
متن کاملOxygen reaction of 4-hydroxybenzoate monooxygenase.
Among monooxygenases the flavin containing enzymes were the first being purified and crystallized since they consist of only one single protein in contrast to the multienzyme structure of the metal containing monooxygenases. Flavin plays a dual role in these enzymes acting as electron acceptor and oxygen activating site simultaneously. Kinetic measurements by NAKAMURA et al.1 on the 4-hydroxybe...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2001
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2001.02137.x