54865-22-4Relevant articles and documents
Native subtilisin Karlsberg and modified subtilisin 72 as effective catalysts of peptide bond formation in organic media
Anikina,Semashko,Oksenoit,Lysogorskaya,Filippova
, p. 116 - 121 (2006)
The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z-Ala-Ala-Leu-pNA and Glp-Ala-Ala-Leu-pNA by the subtilisins were determined. It was found that the subtilisin Karlsberg complex with SDS in anhydrous organic solvents is an effective catalyst of peptide synthesis with multifunctional amino acids in positions P1 and P′1 (Glu, Arg, and Asp) containing unprotected side ionogenic groups. Pleiades Publishing, Inc., 2006.
Synthesis of peptide aldehydes via enzymatic acylation of amino aldehyde derivatives
Voyushina, Tatiana L.,Potetinova, Joanna V.,Milgotina, Ekaterina I.,Stepanov, Valentin M.
, p. 2953 - 2959 (2007/10/03)
Two ways for semi-enzymatic preparation of the peptide aldehydes are proposed: (1) enzymatic acylation of amino alcohols with acyl peptide esters and subsequent chemical oxidation of the resulting peptide alcohols with DMSO/acetic anhydride mixture or (2) enzymatic acylation of the preliminarily obtained by a chemical route amino aldehyde semicarbazones. Subtilisin 72, serine proteinase with a broad specificity, distributed over macroporous silica, was used as a catalyst in both cases. Due to the practical absence of water in the reaction mixtures the yields of the products in both enzymatic reactions were nearly quantitative. The second way seems to be more attractive because all chemical stages were carried out with amino acid derivatives, far less valuable compounds than peptide ones. A series of peptide aldehydes of general formula Z-Ala-Ala-Xaa-al (where Xaa-al=leucinal, phenylalaninal, alaninal, valinal) was obtained. The inhibition parameters for these compounds, in the hydrolysis reactions of corresponding chromogenic substrates for subtilisin and α-chymotrypsin, were determined. Copyright (C) 1999 Elsevier Science Ltd.
