Binding of mercury(II) to protein thiol groups: a study of proteinase K and carboxypeptidase Y.
Chemically modified enzymes have been prepared by incorporating an -Hg-L group into proteinase K and carboxypeptidase Y at the thiol groups of Cys-73 and Cys-341, respectively (L = CN- or I-). The -S-Hg-13CN group has been applied as a spectroscopic label for carbon-13 NMR spectroscopy.
Bagger
S
S
Chemistry Department A, Technical University of Denmark, Lyngby.
Breddam
K
K
Byberg
B R
BR
D000838:Anions; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D043402:Cathepsin A; D019286:Endopeptidase K; D004789:Enzyme Activation; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008628:Mercury / Q000378:metabolism* / Q000494:pharmacology; D003904:Mitosporic Fungi / Q000201:enzymology; D011193:Potassium Iodide / Q000494:pharmacology; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors; D013438:Sulfhydryl Compounds
D000838:Anions; D029701:Saccharomyces cerevisiae Proteins; D015842:Serine Proteinase Inhibitors; D013438:Sulfhydryl Compounds; D011193:Potassium Iodide; D002268:Carboxypeptidases; D043402:Cathepsin A; C499283:PRC1 protein, S cerevisiae; C022633:serine carboxypeptidase; D012697:Serine Endopeptidases; D019286:Endopeptidase K; D008628:Mercury