14289-45-3

Upstream product

• 33741-78-5 DL-2-Amino-2-(2-naphthyl)acetic acid 
• 21473-01-8 2-naphthalenylmagnesium bromide 

Downstream Products

• 66-99-9 β-naphthaldehyde 
• 43210-73-7 (R)-2-hydroxy-2-(2-naphthyl)acetic acid 
• 1236046-53-9 (naphthalen-2-yl)(2-(pyridin-2-yl)phenyl)methanone 
• 94300-93-3 N-(2-(2-naphthoyl)phenyl)acetamide 
• 1345669-05-7 N-allyl-N-benzyl-2-(naphthalen-2-yl)-2-oxoacetamide 
• 56048-51-2 2-(2-naphthyl)benzothiazole 
• 1422748-20-6 2-(2-(2-naphthoyl)-6-methoxyphenyl)-N,N-diethylacetamide 
• 1452841-78-9 2-(2-naphthoyl)-4-chlorophenyl dimethylcarbamate 
• 33741-78-5 DL-2-Amino-2-(2-naphthyl)acetic acid 
• 67363-82-0 N-(4-methylphenyl)-2-naphthamide 
• 1616778-90-5 C₁₉H₁₅FO 
• 144371-23-3 (S)-2-hydroxy-2-(naphthalen-2-yl)acetic acid 
• 28118-49-2 S-phenyl naphthalene-2-carbothioate 
• 4782-69-8 (E)-1-(naphthalen-2-yl)-3-phenylprop-2-en-1-one 

Relevant academic research and scientific papers

Diphenylparabanic acid as a synthon for the synthesis of α-diketones and α-ketocarboxylic acids

Diphenylparabanic acid was found to react with >2 equiv of organolithiums at -78 °C to effectively give the corresponding symmetrical α-diketones. However, upon treatment with 1 equiv of organolithium, the parabanic acid gave mainly 5-substituted 5-hydroxyimidazolidine-2,4-diones. On the other hand, Grignard reagents were less reactive toward the parabanic acid at low temperature, and selectively gave the corresponding 5- hydroxyimidazolidine-2,4-diones even if more than 1 equiv of the reagents was used. A tandem process in which the parabanic acid was first reacted with a Grignard reagent and then reacted in one-pot with an organolithium effectively gave the unsymmetrical α-diketone. 5-Substituted 5-hydroxyimidazolidine-2, 4-diones were useful as versatile precursors for preparing α- ketocarboxylic acids as well as unsymmetrical α-diketones.

Enzymatic conversion of unnatural amino acids by yeast D-amino acid oxidase

Unnatural amino acids, particularly synthetic α-amino acids, are becoming crucial tools for modern drug discovery research. In particular, this application requires enantiomerically pure isomers. In this work we report on the resolution of racemic mixtures of the amino acids D,L-naphthylalanine and D,L-naphthylglycine by using a natural enzyme, D-amino acid oxidase from the yeast Rhodotorula gracilis. A significant improvement of the bioconversion is obtained using a single-point mutant enzyme designed by a rational approach. With this D-amino acid oxidase variant the complete resolution of all the unnatural amino acids tested was obtained: in this case, the bioconversion requires a shorter time and a lower amount of biocatalyst compared to the wild-type enzyme. The simultaneous production of the corresponding α-keto acid, a possible precursor of the amino acid in the L-form, improves the significance of the procedure.