174417-69-7

Upstream product

• 374064-15-0 3-[(4-methoxyphenyl)methyl]cyclobutanone 
• 63559-26-2 2-(p-methoxybenzyl)propane-1,3-diol 
• 824-94-2 p-methoxybenzyl chloride 
• 123-11-5 4-methoxy-benzaldehyde 
• 174417-68-6 Acetic acid (R)-3-cyano-2-(4-methoxy-benzyl)-propyl ester 
• 6335-37-1 2-(4-methoxybenzyl)malonic acid diethyl ester 
• 174417-67-5 Acetic acid (S)-2-methanesulfonyloxymethyl-3-(4-methoxy-phenyl)-propyl ester 
• 174417-66-4 (R)-3-hydroxy-2-(p-methoxybenzyl)propyl acetate 

Downstream Products

• 174417-70-0 ethyl (R)-4-chloro-3-(p-methoxybenzyl)butylate 
• 1316843-77-2 (3R,4R)-3-(4-benzyloxy-3-methoxybenzyl)-4-(4-methoxybenzyl)dihydrofuran-2(3H)-one 
• 72150-17-5 eptazocine hydrobromide 
• 174417-71-1 (R)-3-{[(2-Ethoxycarbonyl-ethyl)-methyl-amino]-methyl}-4-(4-methoxy-phenyl)-butyric acid ethyl ester 
• 174417-72-2 (R)-1-methyl-3-(p-methoxybenzyl)-5-oxo-2,3,4,5,6,7-hexahydro-1H-azepine 

Relevant academic research and scientific papers

Chiral aluminum complexes as catalysts in asymmetric Baeyer-Villiger reactions of cyclobutanones

BINOL-aluminum complexes were successfully employed as mediators and catalysts in asymmetric Baeyer-Villiger rearrangements of cyclobutanones. Good enantioselectivies were achieved with only 15 mol% of the chosen chiral Lewis acid. The enantiomeric excesses obtained have never been reached before in such metal-catalyzed Baeyer-Villiger reactions.

Synthesis and pharmacological characterisation of arctigenin analogues as antagonists of AMPA and kainate receptors

(-)-Arctigenin and a series of new analogues have been synthesised and then tested for their potential as AMPA and kainate receptor antagonists of human homomeric GluA1 and GluK2 receptors expressed in HEK293 cells using a Ca2+ influx assay. In general, these compounds showed antagonist activity at both receptors with greater activity evident at AMPARs. Schild analysis indicates that a spirocyclic analogue 6c acts as a non-competitive antagonist. Molecular docking studies in which 6c was docked into the X-ray crystal structure of the GluA2 tetramer suggest that (-)-arctigenin and its analogues bind in the transmembrane domain in a similar manner to the known AMPA receptor non-competitive antagonists GYKI53655 and the antiepileptic drug perampanel. The arctigenin derivatives described herein may serve as novel leads for the development of drugs for the treatment of epilepsy. This journal is

First chemo-enzymatic synthesis of the (R)-Taniguchi lactone and substrate profiles of CAMO and OTEMO, two new Baeyer–Villiger monooxygenases

Abstract: This study investigates the substrate profile of cycloalkanone monooxygenase and 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase, two recently discovered enzymes of the Baeyer–Villiger monooxygenase family, used as whole-cell biocatalysts. Biooxidations of a diverse set of ketones were performed on analytical scale: desymmetrization of substituted prochiral cyclobutanones and cyclohexanones, regiodivergent oxidation of terpenones and bicyclic ketones, as well as kinetic resolution of racemic cycloketones. We demonstrated the applicability of the title enzymes in the enantioselective synthesis of (R)-(?)-Taniguchi lactone, a building block for the preparation of various natural product analogs such as ent-quinine. Graphical abstract: [Figure not available: see fulltext.]

Type II flavin-containing monooxygenases: A new class of biocatalysts that harbors baeyer-villiger monooxygenases with a relaxed coenzyme specificity

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

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.

Novel chemo-enzymatic process for the preparation of opticaly enriched beta-benzyl-gamma-butyrolactones

The present invention relates to a novel process for the preparation of optically enriched substituted R(+)β-benzyl-γ-butyrolactones of the general formula 1, 1wherein, R1 and R2 independently represent the following groups, R1=R2=H, OH, —OCnH2n+1 (n=1 to 8), NH2, and/or CF3, R1 and R2 together represents —O(CH2)mO— where m=2 to 4.

Asymmetric synthesis of (+)- and (-)-eptazocine via an enzymatic reaction

Starting from (R)-3-hydroxy-2-(p-methoxybenzyl)propyl acetate (R-(+)-4) prepared by enzymatic monoacetylation of 2-(p-methoxybenzyl)propane-1,3-diol (3) with lipase PS in the presence of vinyl acetate as an acetyl donor, lactones ( (+)- and (-)-6) were ob