TAILIEUCHUNG - Báo cáo Y học: Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family

A new NADP(H)-dependent alcohol dehydrogenase (the YCR105Wgene product, ADHVII) has been identified in Saccharomyces cerevisiae. The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of –. ADHVII shows a broad sub-strate specificity similar to the recently characterized ADHVI (64% identity), although they show some differ-ences in kinetic properties. ADHVI and ADHVII are the onlymembersof the cinnamyl alcohol dehydrogenase family inyeast. SimultaneousdeletionofADH6andADH7wasnot lethal for the yeast | Eur. J. Biochem. 269 5738-5745 2002 FEBS 2002 doi Characterization of a Saccharomyces cerevisiae NADP H -dependent alcohol dehydrogenase ADHVII a member of the cinnamyl alcohol dehydrogenase family Carol Larroy Xavier Pares and Josep A. Biosca Department of Biochemistry and Molecular Biology Universitat Autonoma de Barcelona Barcelona Spain A new NADP H -dependent alcohol dehydrogenase the YCR105W gene product ADHVII has been identified in Saccharomyces cerevisiae. The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of . ADHVII shows a broad substrate specificity similar to the recently characterized ADHVI 64 identity although they show some differences in kinetic properties. ADHVI and ADHVII are the only members of the cinnamyl alcohol dehydrogenase family in yeast. Simultaneous deletion of ADH6 and ADH7 was not lethal for the yeast. Both enzymes could participate in the synthesis of fusel alcohols ligninolysis and NADP H homeostasis. Keywords cinnamyl alcohol dehydrogenase fusel alcohols NADP H homeostasis ligninolysis. The current version of the Yeast Proteome Database http lists approximately 260 oxido-reductases 160 of them have been characterized experimentally and the rest predicted by sequence similarity or by other analysis 1 . Our group is interested in the identification and characterization of novel alcohol dehydrogenase ADH gene products from Saccharomyces cerevisiae 2 3 . ADHs are oxidoreductases that catalyze the reversible oxidation of alcohols to aldehydes or ketones with the corresponding reduction of NAD or NADP. ADHs constitute a large group of enzymes that can be subdivided into at least three distinct enzyme superfamilies medium-chain and short-chain dehydrogenases reductases and iron-activated alcohol dehydrogenases 4 5 . The medium-chain dehydrogenase reductase MDR superfamily consists of enzymes with a subunit size of approximately 350 .

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