Inversion of the substrate specificity of yeast alcohol dehydrogenase
作者： D.W. Green , H.W. Sun , B.V. Plapp
DOI: 10.1016/S0021-9258(18)53028-3
关键词: Biochemistry 、 Alcohol dehydrogenase 、 Ethanol 、 Substrate (chemistry) 、 Stereochemistry 、 Binding site 、 Alcohol 、 Isozyme 、 Enzyme 、 Yeast 、 Chemistry
摘要: The relationship between the size of substrate binding pocket and catalytic reactivities with varied alcohols was studied Saccharomyces cerevisiae alcohol dehydrogenase I (ScADH) compared liver enzymes from horse (EqADH, EE isoenzyme) monkey (MmADH alpha, alpha-isoenzyme). yeast enzyme is most active ethanol, its activity decreases as increased, whereas activities increase larger alcohols. in ScADH enlarged by single substitutions Thr-48 to Ser (T48S), Trp-57 Met (W57M), Trp-93 Ala (W93A), a double change, T48S:W93A, triple, T48S:W57M:W93A. T48S has same pattern (V/K) wild-type for linear primary W57M have lowered reactivity secondary W93A T48S:W93A resemble MmADH alpha having an inverted specificity alcohols, being 3- 10-fold more on hexanol 350- 540-fold less are reactive long chain three Ala-93 also acquired weak branched cyclohexanol.
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