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Why does the yeast ADH enzyme is so much less effective in catalysing the oxidation of...

Why does the yeast ADH enzyme is so much less effective in catalysing the oxidation of the other alcohols? Refer to the structural features of the alcohols and enzyme to answer this question.

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Answer #1

The yeast ADH enzyme has a binding site is composed of many large hydrophobic residues like Tryptophan at positions 54 and 92, methionine at position 270 and tyrosine at position 294 together forms a small cavity or binding pocket which is unable to accommodate most of the alcohols other than ethanol. Especially the secondary alcohols, and longer chain alcohols and branched alcohols are tough to be accommodated in this cavity or binding pocket of ADH because of this structural challenge. And even if it does the catalysis and turn over is very poor.

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