作者: W. N. Lipscomb , J. A. Hartsuck , F. A. Quiocho , G. N. Reeke
DOI: 10.1073/PNAS.64.1.28
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摘要: Abstract Several features of carboxypeptidase A (CPA) which were previously established by the X-ray diffraction structure studies have now been confirmed chemical sequence analysis. These results include number (307) amino acid residues in CPAα, identities (Arg 145, Glu 270, and Tyr 248) shown study to be involved substrate binding catalysis, existence a disulfide bond. The Zn ligands, 69, 72, 196 identified as His, Glx, either Glx or Lys, are proved Glu, respectively. No change is required our previous mechanistic deductions, here extended specific mechanism activation net charge on metal ion, suffers local dielectric constant when it covered substrate.