126434-65-9

Upstream product

• 133179-10-9 (2S,6S)-6-Benzyl-2-methyl-[1,3]dioxepan-4-one 
• 55262-02-7 3-benzyl-cyclobutanone 
• 16720-76-6 4-(phenylmethyl)-2(5H)-furanone 
• 22530-98-9 4-benzyl-dihydro-furan-2-one 
• 25226-98-6 trans-cinnamaldehyde diethylacetal 
• 75332-40-0 C₂₇H₂₈O₈S₂ 
• 1021647-08-4 (2S)-2-benzyl-4-nitrobutan-1-ol 
• 100-58-3 phenylmagnesium bromide 
• 184838-77-5 (+)-(1R,5S)-ethyl 2-oxo-3-oxabicyclo[3.1.0]hexane-1-carboxylate 
• 147725-25-5 (4S)-3-<1-oxo-3-(1,3-dithian-2-ylidene)-2-benzylpropyl>-4-(1-methylethyl)-2-oxazolidinone 
• 607375-36-0 acrylic acid 2-benzyl-allyl ester 
• 171007-71-9 3-phenyl-1-propyl diazoacetate 
• 147725-39-1 (2S)-2-benzyl-3-(1,3-dithian-2-ylidene)propanol 
• 374717-36-9 propyl 3-benzyl-4-hydroxybutanoate 

Relevant academic research and scientific papers

Spontaneous Nanobelt Formation by Self-Assembly of β-Benzyl GABA

We present the formation of a nanobelt by self-assembly of β-benzyl GABA (γ-aminobutyric acid). This simple γ-amino acid building block self-assembled to form a well-defined nanobelt in chloroform. The nanobelt showed distinct optical properties due to π–π interactions. This new-generation self-assembled single amino acid may serve as a template for functional nanomaterials.

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.

Self-sufficient Baeyer-Villiger monooxygenases: Effective coenzyme regeneration for biooxygenation by fusion engineering

(Chemical Presented) Two-in-one biocatalysts were engineered by the covalent fusion of NADPH-dependent Baeyer-Villiger monooxygenases to a phosphite dehydrogenase for coenzyme regeneration (see scheme). Not only the purified fusion proteins, but also whole cells and crude cell extracts containing the enzyme conjugates, could be used to catalyze biotransformations with high efficiency. NADP+=nicotinamide adenine dinucleotide phosphate.

Peptide catalyzed asymmetric conjugate addition reactions of aldehydes to nitroethylene - A convenient entry into γ2-amino acids

The peptide H-d-Pro-Pro-Glu-NH2 is a highly effective catalyst for conjugate addition reactions between aldehydes and nitroethylene. Only 1 mol % of H-d-Pro-Pro-Glu-NH2 and a 1.5-fold excess of aldehyde with respect to nitroethylene suffice to obtain γ-nitroaldehydes and, after reduction, monosubstituted γ-nitroalcohols in excellent yields and optical purities. The products can be readily converted into γ2-amino acids, thereby opening an effective direct entry into this important class of compounds. Copyright

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.

An approach to β-substituted γ-butyrolactones and its application to the synthesis of lignans

Copper-catalyzed reaction of 4-cyclopentene-1,3-diol monoacetate with ArCH2MgCl afforded 4-arylmethyl-2-cyclopenten-1-ols regioselectively. Subsequent cleavage of the cyclopentene ring followed by functional group manipulation provided the key β-arylmethyl-γ-butyrolactones for the synthesis of lignans. In addition, synthesis of the rolipram lactone intermediate was accomplished.

Catalytic enantioselective conjugate reduction of lactones and lactams

A dramatic acceleration of the enantioselective copper-catalyzed conjugate reduction of α,β-unsaturated lactones, lactams, and esters is reported upon addition of alcohol additives. Good to excellent yields and enantioselectivities were realized using a catalyst generated in situ from CuCl2·H2O, t-BuONa, p-tol-BINAP, and PMHS, and this methodology was applied to the synthesis of (-)-Paroxetine.

Synthesis of optically active β-benzyl-γ-butyrolactone through lipase-catalyzed kinetic resolution

The lipase-catalyzed kinetic resolution of the racemic γ-hydroxy ester 2, coupled with subsequent acid-mediated cyclization, is an effective method for the synthesis of both enantiomers of β-benzyl-γ-butyrolactone 1. This enzymatic process affords the pro

First attempts at differential diastereoselection in catalytic reactions of N-chirally substituted dirhodium(II) tetrakis[methyl 2-oxoimidazolidine-4(S)-carboxylates] with diazoacetates

Chiral attachments on 2-oxoimidazolidine-4(S)-carboxylate ligands for dirhodium(II) can provide differential diastereoselection in catalytic reactions of diazo compounds. The synthesis of these heterocyclic ligands from the readily available amino acid as