Previous work has demonstrated that the ADH of yeast contains 4 moles of zinc per mole of protein as a structural part of the protein molecule (l-3). The metal has a direct relationship to the catalytic activity of ADH, as shown by (a) the concomitant increase of zinc-protein and activity-protein ratios during purification of ADH, (b) the inhibition of ADH activity by agents forming stable complexes with zinc, (c) the restoration of activity on their removal by dialysis, and (d) the prevention or reversal of the action of such inhibitors by Zn++. Mechanisms for the role of zinc in ADH activity have been suggested (3). The kinetics of the inhibition by OP, which forms complexes with zinc, and the effect of DPN on this inhibition have been studied to elucidate the participation of the metal in ADH activity. The data indicate that OP competes with DPN for an enzymatically active site of ADH and that each zinc atom of ADH binds a DPN molecule.

• PMID: 13345837
• PubMed
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Reference Type

Journal Article

Authors

HOCH FL, VALLEE BL

Primary Lit For

Additional Lit For

ADH5 | ADH4 | ADH3 | ADH2 | ADH1

Review For