76763-88-7Relevant academic research and scientific papers
Type II flavin-containing monooxygenases: A new class of biocatalysts that harbors baeyer-villiger monooxygenases with a relaxed coenzyme specificity
Riebel, Anette,Fink, Michael J.,Mihovilovic, Marko D.,Fraaije, Marco W.
, p. 1112 - 1117 (2014/05/06)
Within a newly identified set of flavin-containing monooxygenases (FMOs) from Rhodococcus jostii RHA1, we have identified three monooxygenases (FMO-E, FMO-F, and FMO-G) that are effective in catalyzing Baeyer-Villiger oxidations. These type II FMOs display relaxed coenzyme specificity by accepting both NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) and NADH (reduced form of nicotinamide adenine dinucleotide), as a coenzyme, which is a novel and attractive feature among biocatalysts capable of conducting Baeyer-Villiger oxidations. We purified FMO-E and determined that the Michaelis constants for both coenzymes were in the micromolar range, whereas the activity was highest for NADH. By using the stopped-flow technique, formation of a peroxyflavin-enzyme intermediate was observed, which indicated that type II FMOs follow a catalytic mechanism similar to that of other class B flavoprotein monooxygenases. A set of cyclobutanones and cyclohexanones were used to probe the regio- and enantioselectivity of all three recombinant monooxygenases. The biocatalysts readily accepted small cyclic ketones, which enabled the conversion of previously poorly accepted substrates by other monooxygenases (especially norcamphor), and exhibited excellent and unique regio- and enantioselectivities. Sequence analysis revealed that type II FMOs that act as Baeyer-Villiger monooxygenases contain a unique N-terminal domain. Sequence conservation in this protein domain can be used to identify new NADH-dependent Baeyer-Villiger monooxygenases, which would facilitate future biocatalyst discovery efforts. New kid on the block: Members of a newly recognized group of sequence-related flavin-containing monooxygenases can perform Baeyer-Villiger oxidations. Their coenzyme indifference and unique specificity make them attractive biocatalysts.
Comparing the stereoselective biooxidation of cyclobutanones by recombinant strains expressing bacterial baeyer - Villiger monooxygenases
Rudroff, Florian,Rydz, Joanna,Ogink, Freek H.,Fink, Michael,Mihovilovic, Marko D.
, p. 1436 - 1444 (2008/09/17)
Microbial Baeyer - Villiger oxidation of representative prochiral ketones with a cyclobutanone structural motif was investigated using a collection of eight monooxygenases of different bacterial origin. This platform of enzymes is able to perform stereoselective biotransformations on an array of structurally diverse substrates. With several ketone precursors, biooxidations yielded enantiocomplementary butyrolactones as key intermediates for the synthesis of natural products and bioactive compounds. The microbial Baeyer - Villiger oxidation allows a facile and rapid entry to several compound classes in a desymmetrization reaction upon de novo generation of chirality.
Total Synthesis of Homochiral Kadsurin Having the Natural Configuration
Ohshima, Toshihiro,Tanaka, Masahide,Mitsuhashi, Hiroshi,Maruno, Masao,Wakamatsu, Takeshi
, p. 139 - 146 (2007/10/02)
The total synthesis of kadsurin was achieved in a stereoselective manner.The stereoselective hydrogenation of the homochiral enone (12), obtained from the known tetracyclic lactone (7), afforded known ketone (13), the conversion of which into kadsurin has
A SIMPLE PREPARATION OF (R)-(+)-β-(3,4,5-TRIMETHOXYBENZYL)-BUTANOLIDE, AND ITS USE IN THE TOTAL SYNTHESES OF NATURALLY OCCURRING DIBENZYLBUTANOLIDE LIGNANS
Lalami, Khalid,Dhal, Robert,Brown, Eric
, p. 1131 - 1134 (2007/10/02)
Resolution of methyl α-(3,4,5-trimethoxybenzyl)hemisuccinate by means of (-)-ephedrine, followed by calcium borohydride reduction, afforded (R)-(+)-β-(3,4,5-trimethoxybenzyl)butanolide.This lactone was used as a starting material for the optically active
