Title: Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y Jung G, Ueno H, Hayashi R, Liao TH Ref: Protein Science, 4:2433, 1995 : PubMed
The essential histidine residue of carboxypeptidase Y (CPY) was modified by a site-specific reagent, a chloromethylketone derivative of benzyloxycarbonyl-L-phenylalanine. The single modified histidine residue was converted to N tau-carboxy-methyl histidine (cmHis) upon performic acid oxidation. A peptide containing cmHis was isolated from the tryptic-thermolytic digest. Based on the amino acid composition and sequence analysis, the peptide is shown to be Val-Phe-Asp-Gly-Gly-cmHis-MetO2-Val-Pro, which was derived from CPY cleaved by trypsin at Arg 391 and thermolysin at Phe 401, and thus His 397 was modified. This histidine residue has been implicated previously by X-ray analysis to participate in the charge-relay system of CPY.
Jung G, Ueno H, Hayashi R, Liao TH (1995) Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y Protein Science4: 2433-5
