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Albalat et al., 1992, FEBS Lett. 308(3): 235--239

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Albalat et al., 1992, FEBS Lett. 308(3): 235--239
FlyBase Identifier FBrf0056069
FlyBase URL http://flybase.org/reports/FBrf0056069.html
Publication Type paper
Publication Year 1992
PubMed ID 1505661
PubMed URL http://www.ncbi.nlm.nih.gov/pubmed/1505661

Title

Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme.

Abstract

Drosophila alcohol dehydrogenase is the most studied member of the family of short-chain alcohol dehydrogenases, although its tridimensional structure still remains unknown. We have engineered a Drosophila alcohol dehydrogenase in which tyrosine-152, an invariant residue in all members of the family, has been substituted by phenylalanine. The mutated gene has been expressed in yeast and pure mutant enzyme has been prepared by a one-step FPLC chromatographic procedure. Drosophila alcohol dehydrogenase-phenylalanine-152 shows no enzymatic activity. This result suggests not only that tyrosine-152 could constitute an essential building block of the active site but also that its hydroxyl group is directly involved in the redox reaction catalyzed by the enzyme.

Genes from Reference

Gene(s) Dmel\Adh
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