Bifunctional activity labels for selection of filamentous bacteriophages displaying enzymes

• Published in: Bioorganic & medicinal chemistry Vol. 3; no. 7; pp. 907 - 915
• Main Authors: Vanwetswinkel, Sophie, Touillaux, Roland, Fastrez, Jacques, Marchand-Brynaert, Jacqueline
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.07.1995
• Subjects: activity label; Bacterial Proteins; Bacteriophages - genetics; beta-Lactamase Inhibitors; beta-Lactamases - analysis; beta-Lactamases - genetics; Biotin - analogs & derivatives; Biotin - chemical synthesis; biotinyl spacer; Carrier Proteins - analysis; Carrier Proteins - antagonists & inhibitors; Carrier Proteins - genetics; Cross-Linking Reagents - chemical synthesis; d-carboxypeptidase; enzyme inhibition; Enzyme Inhibitors - chemical synthesis; Hexosyltransferases; Muramoylpentapeptide Carboxypeptidase - analysis; Muramoylpentapeptide Carboxypeptidase - antagonists & inhibitors; Muramoylpentapeptide Carboxypeptidase - genetics; Penicillanic Acid - analogs & derivatives; Penicillanic Acid - chemical synthesis; Penicillin-Binding Proteins; Peptidyl Transferases; Phage enzyme; Recombinant Proteins - analysis; β-lactamase; activity label; d; enzyme inhibition; β-lactamase; d-carboxypeptidase; biotinyl spacer; Phage enzyme

Two bifunctional activity labels of β-lactamases or penicillin binding proteins have been prepared. They feature a penicillin sulfone derivative, i.e. a suicide substrate of serine β-lactamases, or a penicillin derivative connected to a biotin moiety through a spacer containing a disulfide bridge. T...