Hydrolysis of a thiopeptide by cadmium carboxypeptidase A
作者： William L. Mock , Jin-Tann Chen , Joseph W. Tsang
DOI: 10.1016/0006-291X(81)91533-3
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摘要: Abstract Substitution of the active site zinc ion carboxypeptidase A by cadmium yields an enzyme inactive towards ordinary peptide substrates. However, a substrate analog (BzGlyNHCH2CSPheOH) containing thioamide linkage at scissile position is cleaved to thioacid. The kinetic parameters and their pH dependencies are k cat K m = 5.04 × 10 4 min −1 M , decreasing with either acid or base (PKE1 5.64, pKE2 9.55), kcat 1.02 102 min−1, (pKES 6.61). thiopeptide less efficiently native (zinc) A. This cadmium-sulfur synergism supports mechanism wherein amide activated metal coordination its (thio) carbonyl.
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