Abstract
Tyr 152 and Lys 156 may be functionally important residues in Drosophila ADH as they are conserved in the genus and in all short-chain dehydrogenases. In addition, unaltered Gly positions could have a crucial role in the building of the structural framework. We have modified Drosophila ADH and expressed the mutant forms in E. coli. Mutation of Tyr 152 to Glu or Gin, Lys 156 to Ile, Gly 184 to Leu, and the double mutant Gly 130 to Cys and Gly 133 to Ile, all rendered, with different substrates and at different pHs, an inactive enzyme. Results suggest that Tyr 152 and Lys 156are involved in catalysis and that Gly 130, Gly 133 and Gly 184 contribute substantially to the structure of the active form.
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