Molecular recognition of cobalt(III)-ligated peptides by serine proteases: the role of electrostatic effects.
A series of peptides with a positively charged cobalt(III)-complex group attached to the carboxylate terminal was synthesized. The behavior of these metallopeptides as acceptor nucleophiles in acyl transfer reactions catalyzed by the three serine proteases bovine pancreatic alpha-chymotrypsin, porcine pancreatic trypsin, and proteinase K from Tritirachium album was examined. The efficiency of the substrates was assessed by kinetic measurement of the partition between aminolysis and hydrolysis. The results are discussed with special reference to coulombic interactions between the metal-ligated substrates and charged residues on the enzyme surfaces. The idea of using the metallopeptides in practical enzymatic peptide synthesis is put forward.
Bagger
S
S
Department of Chemistry, Technical University of Denmark, Lyngby. sb@kemi.dtu.dk
Wagner
K
K
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003035:Cobalt; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D055672:Static Electricity
D008667:Metalloproteins; D003035:Cobalt; D012697:Serine Endopeptidases