65671-47-8

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 41089-47-8 L-glutamic acid α-methyl γ-benzyl diester hydrochloride 
• 2578-33-8 D-glutamic acid-5-benzyl ester 
• 3392-05-0 Boc-Ala-O-N-hydroxysuccinimide 
• 53759-36-7 γ-benzyl tert-butoxycarbonyl-L-alanyl-D-glutamate 
• 18107-18-1 diazomethyl-trimethyl-silane 
• 57584-59-5 γ-OBzl-L-Glu-α-OMe 
• 1676-73-9 L-glutamic acid γ-benzyl ester 
• 100-51-6 benzyl alcohol 

Downstream Products

• 77303-04-9 (S)-2-[(S)-2-((S)-4-Benzyloxycarbonyl-2-{(S)-2-[((S)-1-tert-butoxycarbonyl-pyrrolidine-2-carbonyl)-amino]-4-methyl-pentanoylamino}-butyrylamino)-propionylamino]-pentanedioic acid 5-benzyl ester 1-methyl ester 
• 77303-05-0 (S)-2-{(S)-2-[(S)-4-Benzyloxycarbonyl-2-((S)-2-tert-butoxycarbonylamino-4-methyl-pentanoylamino)-butyrylamino]-propionylamino}-pentanedioic acid 5-benzyl ester 1-methyl ester 
• 77303-03-8 (S)-2-[(S)-2-((S)-4-Benzyloxycarbonyl-2-tert-butoxycarbonylamino-butyrylamino)-propionylamino]-pentanedioic acid 5-benzyl ester 1-methyl ester 
• 65671-48-9 (S)-2-((S)-2-Amino-propionylamino)-pentanedioic acid 5-benzyl ester 1-methyl ester; hydrochloride 

Relevant academic research and scientific papers

Tetrapeptide Copper Catalysts Capable Of Oxidizing Hydrocarbons At Room Temperature

The present invention relates to peptide copper catalysts capable of oxidizing hydrocarbons at room temperature.

Transpeptidase-mediated incorporation of d-amino acids into bacterial peptidoglycan

The β-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse d-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical d-amino acids can be introduced into the bacterial cell wall.

Synthesis of Peptide Analogues of Prothrombin Precursor Sequence 5-9. Substrate Specificity of Vitamin K Dependent Carboxylase

Thirty-five analogues of Phe-Leu-Glu-Glu-Leu, the pentapeptide sequence 5-9 of bovine prothrombin precursor, were synthesized and assayed as potential substrates or inhibitors of rat liver vitamin K dependent carboxylase.Carboxylation of substrate was determined by measuring the incorporation of carbon-14 labeled bicarbonate into product.Changes in substrate carboxylation produced by changing peptide chain length, amino acid chirality, or the distance seperating the peptide chain backbone from the carboxyl group were measured.The data suggest that the carboxylase carboxylates L-glutamic acid residues and does not carboxylate L-aspartic acid, L-homoglutamic acid, glutamine, or D-glutamic acid residues; tri- through pentapeptides are better substrates than mono- or bis(amino acid) derivatives, and hydrophobic groups added to the N-terminus can produce better substrates for the enzyme.None of the synthetic substrates is carboxylated as effectively as the endogenous protein substrates for the enzyme.The effect of structure on additional parameters affecting carboxylation is discussed.