96096-69-4

Upstream product

• 89321-71-1 (2S,3S)-3-propyl-2-oxiranemethanol 

Downstream Products

• 100992-81-2 Methyl (2R,3S)-(-)-3-propyloxirane-2-carboxylate 
• 244239-98-3 (2R,3S)-3-Propyl-oxirane-2-carboxylic acid (2-hydroxy-phenyl)-amide 
• 244239-99-4 (2R,3S)-3-Propyl-oxirane-2-carboxylic acid (2-hydroxy-5-methyl-phenyl)-amide 
• 244240-01-5 (2R,3S)-3-Propyl-oxirane-2-carboxylic acid (5-chloro-2-hydroxy-phenyl)-amide 
• 226565-78-2 (2-Methoxymethoxy-phenyl)-((2R,3S)-3-propyl-oxiranyl)-methanone 
• 226565-81-7 (2-Methoxymethoxy-5-methyl-phenyl)-((2R,3S)-3-propyl-oxiranyl)-methanone 
• 226565-84-0 (5-Methoxy-2-methoxymethoxy-phenyl)-((2R,3S)-3-propyl-oxiranyl)-methanone 
• 107796-99-6 Methyl (2S,3R)-(+)-3-propyloxirane-2-carboxylate 
• 117709-02-1 3-propylepoxyethane-2-carboxylic acid methyl ester 

Relevant academic research and scientific papers

New chiral amino alcohol ligands for catalytic enantioselective addition of diethylzincs to aldehydes

A study aimed at the synthesis and structure optimization of new, efficient, optically active β-amino alcohol ligands with a structure suitable for immobilization on magnetite nanoparticles has been carried out. The optimized homogeneous amino alcohol catalysts 13a and 13b, the chirality of which arises from the Sharpless epoxidation of suitable allyl alcohols, were tested by employing the well-established enantioselective amino alcohol-promoted addition of diethylzinc to benzaldehyde, giving the corresponding benzyl alcohol with nearly quantitative yield and ee = 95%. Then, their broad applicability as chiral catalysts was evaluated by carrying out the same reaction on a family of aldehydes, including variously substituted aromatic ones as well as an aliphatic analogue. The results have confirmed the validity of the fine-tuning process performed on ligands 13a and 13b. In fact, both exhibited excellent catalytic activity as demonstrated by the chemical yields and ee obtained from all the tested aldehydes, almost independent of the position and type of substitution in the aromatic ring.

Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes

Here, we report a new experimental approach utilizing an amide ligation reaction for the characterization of acyl carrier protein (ACP)-bound reaction intermediates, which are otherwise difficult to analyze by traditional biochemical methods. To explore fatty acid tailoring enzymes of the calcium-dependent antibiotic (CDA) biosynthetic pathway, this strategy enabled the transformation of modified fatty acids, covalently bound as thioesters to an ACP, into amide ligation products that can be directly analyzed and compared to synthetic standards by HPLC-MS. The driving force of the amide formation is the thermodynamic activation inherent to thioester-bound compounds. Using this novel method, we were able to characterize the ACP-mediated biosynthesis of the unique 2,3-epoxyhexanoyl moiety of CDA, revealing a new type of FAD-dependent oxidase HxcO with intrinsic enoyl-ACP epoxidase activity, as well as a second enoyl-ACP epoxidase, HcmO. In general, our approach should be widely applicable for the in vitro characterization of other biosynthetic systems acting on carrier proteins, such as integrated enzymes from NRPS and PKS assembly lines or tailoring enzymes of fatty and amino acid precursor synthesis.