Stereo- and sequence specificity of serine proteases in peptide synthesis.
The sequence- and stereospecificity of the S1- and S' i-subsites (i = 1-3) of bovine alpha-chymotrypsin and trypsin, proteinase K and penicillin amidase from E. coli and A. viscosus has been determined by hydrolysis and kinetically controlled peptide synthesis using different substrates. The data are compared with results for other serine proteases and the thiol protease papain. The stereospecificities differ by orders of magnitude, decreased when the enzyme was immobilized and were influenced when organic solvent molecules were bound to the enzyme.
Kasche
V
V
AB Biotechnologie II, TU Hamburg-Harburg, F.R.G.
Michaelis
G
G
Wiesemann
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D007700:Kinetics; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D013237:Stereoisomerism; D013379:Substrate Specificity
D010455:Peptides; D012697:Serine Endopeptidases