University of Aquila, Laquila
Kluyveromyces lactis alcohol dehydrogenase studied, kinetics revealed
Published in Physician Law Weekly, February 23rd, 2005
"By computer modelling and protein engineering we have investigated changes in two amino acid residues located in the coenzyme pocket of the yeast K. lactis mitochondrial alcohol dehydrogenase III. These two residues, Gly 225 and Ala 274, were hypothesized to be involved in the enzyme discrimination between NAD(H) and NADP(H).
"Upon changing Gly-225 to Ala we produced an enzyme (mutant G225A) showing very little difference...
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Source: Physician Law Weekly (2005-02-23)
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