Chymotrypsin-catalyzed peptide synthesis in ice: Use of unprotected amino acids as acyl acceptors

Kinetically controlled chymotrypsin-catalyzed peptide syntheses are carried out using unprotected amino acids as amino components. The reactions are performed in frozen aqueous solutions. A gram scale dipeptide synthesis is described. Graphic

Saved in:
Bibliographic Details
Published inTetrahedron letters Vol. 34; no. 36; pp. 5701 - 5702
Main Authors Schuster, M., Ullmann, G., Ullmann, U., Jakubke, H.-D.
Format Journal Article
LanguageEnglish
Published OXFORD Elsevier Ltd 03.09.1993
Elsevier
Subjects
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Chemistry
Chemistry, Organic
enzymatic peptide synthesis
Exact sciences and technology
frozen aqueous reaction medium
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Organic chemistry
Peptides
Physical Sciences
Preparations and properties
protease
Science & Technology
protease
enzymatic peptide synthesis
frozen aqueous reaction medium
FROZEN AQUEOUS REACTION MEDIUM
ENZYMATIC PEPTIDE SYNTHESIS
PROTEASE
Dipeptides
Temperature effect
Enzymatic catalysis
Peptide synthesis
Glycine
Online AccessGet full text

Cover

More Information
Summary:Kinetically controlled chymotrypsin-catalyzed peptide syntheses are carried out using unprotected amino acids as amino components. The reactions are performed in frozen aqueous solutions. A gram scale dipeptide synthesis is described. Graphic
ISSN:0040-4039
1873-3581
DOI:10.1016/S0040-4039(00)73837-8