127357-85-1

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 107-14-2 chloroacetonitrile 

Downstream Products

• 1333389-26-6 PheLysAlaAcm 
• 5956-81-0 (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate 
• 1333389-11-9 (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-5-((bis(4-methoxyphenyl)(phenyl)methoxy)methyl)-4-hydroxytetrahydrofuran-3-yl 2-((tert-butoxycarbonyl)amino)-3-phenylpropanoate 

Relevant academic research and scientific papers

Methods of modifying N-termini of a peptide or protein using transferases

The invention includes a selective method of modifying the N-terminus of a protein using an aminoacyl tRNA transferase. In certain embodiments, the method comprises contacting a solution of the protein or peptide with a transferase and a derivative of a molecule, whereby the N-terminus of the protein or peptide is derivatized with the molecule.

N-terminal protein modification using simple aminoacyl transferase substrates

Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

Enzymes as synthetic catalysts: Mechanistic and active-site considerations of natural and modified chymotrypsin

This paper describes the mechanistic investigation of α-chymotrypsin and [Met192-sulfoxide]-α-chymotrypsin-catalyzed peptide synthesis in a kinetically controlled process (i.e., aminolysis) and the relative stabilities of both enzymes in differ