4101-35-3

Upstream product

• 64-18-6 formic acid 
• 73-32-5 DL-isoleucine 
• 319-78-8 D-Isoleucine 
• 319-78-8 isoleucine 
• 73-32-5 L-isoleucine 
• 959215-79-3 (2RS,3S)-2-amino-3-methylpentanoic acid 
• 3107-04-8 DL-alloisoleucine 

Downstream Products

• 319-78-8 D-Isoleucine 
• 90821-99-1 Cyclo(Ile-Ala-) 
• 935399-25-0 N-alanyl-isoleucine 
• 1115-24-8 N-chloroacetyl-isoleucine 
• 73-32-5 L-isoleucine 
• 102609-71-2 N-phenylcarbamoyl-D-alloisoleucine 
• 102609-71-2 N-phenylcarbamoyl-L-alloisoleucine 
• 1509-35-9 D-alloisoleucine 
• 1509-34-8 D-allo-isoleucine 

Relevant academic research and scientific papers

ANTIFOULING AGENT FOR UNDERWATER ADHERING ORGANISMS HAVING AMINO ACID ISONITRILE SKELETON

PROBLEM TO BE SOLVED: To provide a novel antifouling agent for underwater adhering organisms having excellent characteristics compared with well-known antifouling agents. SOLUTION: An antifouling agent for underwater adhering organisms comprises a compound represented by formula (I) or salt thereof, or solvate thereof, as an active ingredient. COPYRIGHT: (C)2015,JPO&INPIT

Formylation of amines and alcohols using aminopropylated mesoporous SBA-15 silica (APMS) as an efficient and recyclable catalyst

Aminopropylated mesoporous SBA-15 silica (APMS) is introduced as a new, recyclable and efficient catalyst for the formylation of a variety of amines and alcohols by using readily available formic acid under solvent-free conditions.

Chemo-enzymatic approach to D-allo-isoleucine

A mixture of D-alloisoleucine and L-isoleucine derivatives are selectively hydrolysed by enzymatic catalysis (alcalase) allowing the recovery of the D-allo stereoisomer in excellent d.e. and yields. Thus, N-formyl-D-allo- isoleucine benzylester is obtained after enzymatic hydrolysis of the diastereoisomeric mixture or by a crystallisation procedure.

Remote binding energy in antibody catalysis: Studies of a catalytically unoptimized specificity pocket

Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system. We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes. We have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes favorable simultaneous interactions between the side chain and binding pocket along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-pocket interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (kcat) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8·hapten complex has allowed for the identification of differences between the active sites of 17E8 and several proteases. The identified differences give insight to the sources of the inefficient use of binding energy.

REAGENTS AND SYNTHETIC METHODS. 30. PRACTICAL AND IMPROVED METHOD FOR FORMYLATING AMINO COMPOUNDS BY MEANS OF FORMIC ACID-DIMETHYLFORMAMIDE SYSTEM.

Several amino compounds were formylated in high yields by means of formic acid-dimethylformamide, specially D,L-amino acids.The influence of this solvent was also briefly discussed.