Jinge zhu (3 risultati)

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  • Lingua: Inglese

    Editore: VDM Verlag Dr. Müller, 2009

    3639165152 / 9783639165159

    • Brossura

    Da: preigu, Osnabrück, Germaniapreigu

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    Condizione: Nuovo

    EUR 66,50

    EUR 70,00 spedizione 
    Spedito da Germania a U.S.A.

    Quantità: 5 disponibili

    Taschenbuch. Condizione: Neu. Characterization of S-Ribosylhomocysteinase (LuxS) | Mechanism and Inhibition | Jinge Zhu | Taschenbuch | Englisch | VDM Verlag Dr. Müller | EAN 9783639165159 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. …

  • Lingua: Inglese

    Editore: VDM Verlag Dr. Müller, 2009

    3639165152 / 9783639165159

    • Brossura
    • Print on Demand

    Da: moluna, Greven, Germaniamoluna

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    Condizione: Nuovo

    EUR 60,51

    EUR 48,99 spedizione 
    Spedito da Germania a U.S.A.

    Quantità: Più di 20 disponibili

    Kartoniert / Broschiert. Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Zhu JingeJinge ZhunPh.D., Biochemistry, The Ohio State University, Columbus, OH (2005)nResearch Associate, University of Wisconsin - Madison.S-Ribosylhomocysteinase (LuxS) catalyzes the cleavageof the thioether bond in S-ribosyl. …

  • Lingua: Inglese

    Editore: VDM Verlag Dr. Müller, 2009

    3639165152 / 9783639165159

    • Brossura
    • Print on Demand

    Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH

    Venditore con 5 stelle
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    Condizione: Nuovo

    EUR 84,50

    EUR 35,00 spedizione 
    Spedito da Germania a U.S.A.

    Quantità: 2 disponibili

    Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - S-Ribosylhomocysteinase (LuxS) catalyzes the cleavageof the thioether bond in S-ribosylhomocysteine to produce L-homocysteine and 4,5-dihydroxy-2,3-pentanedione,the precursor of type II bacterial quorum sensingautoinducer. This work carried out extensive mechanistic studiesof the LuxS reaction. The native metal cofactor of LuxS wasidentified as ferrous ion, instead of previously reported zinc ion, with apotential catalytic role. Substantial evidence was provided for theinternal redox reaction, which comprised two consecutive carbonylmigration steps followed by -elimination. Three LuxS activity assays were developed and greatlyfacilitated the mechanistic investigations of LuxS. Two classes ofLuxS inhibitors were designed based on metal chelation and catalyticmechanism, respectively. They encouraged future development ofLuxS inhibitors as novel antibacterial agents and helped probe thecatalytic mechanism of LuxS.…