Identification of histidine residues that act as zinc ligands in beta-lactamase II by differential tritium exchange.
1. Four histidine-containing peptides have been isolated from a tryptic digest of the Zn2+-requiring beta-lactamase II from Bacillus cereus. One of these peptides probably contains two histidine residues. 2. The presence of one equivalent of Zn2+ substantially decreases the rate of exchange of the C-2 proton in at least two and probably three of the histidine residues of these peptides for solvent 3H. 3. It is concluded that peptides containing at least two of the three histidine residues acting as Zn2+ ligands at the tighter Zn2+-binding site of beta-lactamase II have been identified.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002510:Cephalosporinase / Q000378:metabolism*; D006639:Histidine / Q000032:analysis*; D008024:Ligands; D010446:Peptide Fragments / Q000032:analysis; D014316:Tritium; D014357:Trypsin; D015032:Zinc / Q000378:metabolism*; D001618:beta-Lactamases / Q000378:metabolism*
D000596:Amino Acids; D008024:Ligands; D010446:Peptide Fragments; D014316:Tritium; D006639:Histidine; D014357:Trypsin; D002510:Cephalosporinase; D001618:beta-Lactamases; D015032:Zinc