Formation of peptide bonds by carboxypeptidase c from orange leaves.
Carboxypeptidase c partially purified from orange leaves was studied as a catalyst for enzymatic peptide synthesis. Various N-protected ester- and nucleophile compounds were evaluated in order to determine the substrate specificity. For further characterization of the synthetic reaction, optimum pH and the influence of the N-terminal protecting group were studied. Kinetic investigations revealed considerable differences in Km and Vmax for the nucleophile when the N-terminal protecting group of the substrate was varied.
Institut für Enzymtechnologie, Heinrich Heine Universität Düsseldorf, Jülich, FRG.
D
D
Steinke
A
A
Schwarz
C
C
Wandrey
M R
MR
Kula
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004151:Dipeptides / Q000138:chemical synthesis; D007202:Indicators and Reagents; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis; D010455:Peptides / Q000138:chemical synthesis*; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
D004151:Dipeptides; D007202:Indicators and Reagents; D009842:Oligopeptides; D010455:Peptides; D002268:Carboxypeptidases; C022633:serine carboxypeptidase