Abstract

Formaldehyde and NADH are formed from methanol and NAD in the reaction catalyzed by horse liver ADH and yeast ADH. In this reaction the above enzymes resemble closely human liver ADH, which has been known for some time to catalyze methanol dehydrogenation. The formation of formaldehyde from melhanol has been followed by chromatography of 2:4-DNPH derivatives of the reaction products and quantitation by the highly specific chromotropic acid method. Kinetic results have shown that turnover numbers × sec −1 × active site −1 are very similar for all three enzymes. The specificity of all three enzymes with respect to methanol is therefore identical. Human liver ADH, however, has the lowest K m for methanol, and on this basis only may be considered to be the best catalyst of this reaction.

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