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  • Coenzyme specificity in fungal 17ß-hydroxysteroid dehydrogenase
    Kristan, Katja, 1975- ...
    The 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus is an NADP(H)-dependent member of the short-chain dehydrogenase/reductase superfamily (SDR) that belongs to the cP1 ... classical subfamily. Here, we have created several mutants by sitedirected mutagenesis, and through these we havestudied the amino acid residues that are responsible for coenzyme binding and specificity. The Thr202Val and Thr202Ile mutants were inactive, thus confirming the importance ofThr202 for the appropriate orientation ofthe coenzyme that enables the hydride transfer. The Ala50Arg and Asn51 Arg mutantshad increased rates of NADPH dissociation, and thus an enhanced substrate oxidation with NADP+, while the Asn51Arg mutant also showed an increased rate of NADP+ dissociation, and thus an enhanced substrate reductionwith NADPH. Addition of a negatively-charged amino acid residue at the first position afrer the second beta-strand (Tyr49Asp) affected the coenzyme specificity and turned the enzyme into an NAD+-dependent oxidase resembling the cD1d subfamily members.
    Vir: Molecular and cellular endocrinology. - ISSN 0303-7207 (Letn. 241, 2005, str. 80-87)
    Vrsta gradiva - članek, sestavni del
    Leto - 2005
    Jezik - angleški
    COBISS.SI-ID - 19811289