57079-18-2

Upstream product

• 108-31-6 maleic anhydride 
• 63-91-2 L-phenylalanine 
• 50997-19-8 maleic acic-(L)-phenylalanine methyl ester 
• 124455-81-8 (Z)-3-[(S)-1-(4-Nitro-benzyloxycarbonyl)-2-phenyl-ethylcarbamoyl]-acrylic acid 
• 50997-20-1 (Z)-3-((S)-1-Ethoxycarbonyl-2-phenyl-ethylcarbamoyl)-acrylic acid 

Downstream Products

• 62205-63-4 methyl N,N-maleoyl-L-phenylalaninate 
• 172960-26-8 ethyl N,N-maleoyl-L-phenylalaninate 
• 55750-54-4 N,N-maleoyl-L-phenylalanine 

Relevant academic research and scientific papers

Synthesis and properties of chiral N,N-maleoyl derivatives and Diels-Alder reactions with cyclopentadiene

Maleyl amino acid derivatives were prepared from maleic anhydride and cyclized by reaction with ZnCl2 and hexamethyldisilazane yielding maleoyl derivatives. These derivatives were used as dienophiles in cycloadditions with cyclopentadiene. The

Nucleophile specificity in trypsin-catalyzed acyl transfer using non-specific acyl donors

The S'-subsite specificity of trypsin has been studied by comparing the non-specific acyl donors Mal-Phe-OCam (Mal = maleyl, OCam = carboxamidomethyl ester), Mal-Gly-Phe-OCam and Mal-Phe-OMe (OMe = methyl ester) with the specific substrate Bz-Arg-OEt (Bz = benzoyl, OEt = ethyl ester). Various nucleophilic amino components were chosen to determine S'1-P'1 interactions depending on the acyl donor used. The data obtained underline that there are no significant differences in the nucleophile specificity for specific and non-specific acyl donors, but with the latter a slightly better acceptance of the nucleophiles was found. Independent of the acyl donor used, a preference for methionine and arginine in the S'1-subsite of trypsin could be established. The results provide evidence that the binding site of the non-specific substrates in the active site of trypsin is not different to that of Bz-Arg-OEt.

SPECIFIC WATER-SOLUBLE SUBSTRATES FOR CHYMOTRYPSIN: ATTEMPTS FOR COMPENSATING DIMINISHED P1-S1 INTERACTION

N-Maleyl-L-amino acid and peptide esters were synthesized and employed as substrates for α-chymotrypsin.From the kcat/KM values can be suggested that benzyl esters are significantly better substrates than the appropriate methyl esters.Further improvement in the substrate properties results from the introduction of the p-nitrobenzyl ester moiety.The choline ester of benzyloxycarbonyl-L-phenylalanine with the highest kcat/KM value confirmed the P'1 leaving group specifity for positively charged residues.From the kinetic data can be concluded that acyl donors with high kcat/KM values, which are useful in kinetically controlled enzymatic peptide synthesis, need not contain aromatic amino acid residue in the P1 position.