Baeyer Villiger Monooxygenases
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. Investigação da seletividade de mono-oxigenases frente a substratos orgânicos de boro ou de selênio / Investigation on selectivity of mono-oxigenases in the presence of boron-containing or seleniun-containing organic compounds
Neste trabalho foi avaliada a seletividade (quimio ou enantiosseletividade) de quatro enzimas Baeyer-Villiger mono-oxigenases (BVMOs: PAMO, PAMO M446G, HAPMO e CHMO) frente a substratos contendo boro ou selênio. Inicialmente uma série de boro-acetofenonas foram submetidas à bio-oxidação catalisada por estas BVMOs. A enzima CHMO mostrou quimiosseletivida
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 25/05/2012
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2. High-throughput screening in enzyme assays for epoxide hydrolases and monooxygenases activity detection using whole cell / Triagem de alto desempenho para detecção de atividade de epoxido-hidrolases e monooxigenases utilizando celulas integras
Biocatalysis is a multidisciplinary area, where new technologies are developing rapidly in order to offer unique options and solutions to different organic chemistry problems, complementing the classical synthetic chemistry. Facing the need imposed by progress in this area, this project aims at the implementation of high-throughput screening (HTS) methodolog
Publicado em: 2006
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3. Multibiorreações e suas aplicações para as sinteses de compostos enantiomericamente puros / Multibioreactions applied to the syntheses of enantiomerically pure compounds
The utilization of enzymes for organic compound transformations is an alternative to classical syntheses. Enzymes are used as biocatalysts for the syntheses in vitro of asymmetric compounds because they are intrinsically chiral and result in high catalytic efficiency. In front of the biodiversity of existing microorganisms in Nature and of the necessity to d
Publicado em: 2006
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4. Crystal structure of a Baeyer–Villiger monooxygenase
Flavin-containing Baeyer–Villiger monooxygenases employ NADPH and molecular oxygen to catalyze the insertion of an oxygen atom into a carbon–carbon bond of a carbonylic substrate. These enzymes can potentially be exploited in a variety of biocatalytic applications given the wide use of Baeyer–Villiger reactions in synthetic organic chemistry. The catal
National Academy of Sciences.
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5. 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 simila
American Society for Microbiology.
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6. mRNA Differential Display in a Microbial Enrichment Culture: Simultaneous Identification of Three Cyclohexanone Monooxygenases from Three Species
mRNA differential display has been used to identify cyclohexanone oxidation genes in a mixed microbial community derived from a wastewater bioreactor. Thirteen DNA fragments randomly amplified from the total RNA of an enrichment subculture exposed to cyclohexanone corresponded to genes predicted to be involved in the degradation of cyclohexanone. Nine of the
American Society for Microbiology.
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7. Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453.
The oxygenating component of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453 was purified to homogeneity by a combination of ammonium sulfate fractionation and chromatography on DEAE-cellulose and polyanion SI-17 columns. It had an Mr of 78,000, bound one molecule of nonautooxidizable flavin mononucleotide (FMN), consisted of two subu
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8. Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-delta 3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida.
Previously, Pseudomonas putida was shown to degrade (+)-camphor, and cleavage of the first ring of the bicyclic structure involved two monooxygenases (a hydroxylase and a ring oxygen-inserting enzyme), a dehydrogenase, and spontaneous cleavage of an unstable oxygenation product (lactone). Cleavage of the second ring was not demonstrated but was assumed also