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Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway.

Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Research Abstract Details 

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  • Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Abstract Text:

    takashi yamamotoTakashi Yamamoto,tadashi eguchiTadashi Eguchi,takashi yamamotoTakashi Yamamoto,tadashi eguchiTadashi Eguchi,

    Homoisocitrate dehydrogenase is involved in the alpha-aminoadipate pathway of l-lysine biosynthesis in higher fungi such as yeast and human pathogenic fungi. This enzyme catalyzes the oxidative decarboxylation of (2R,3S)-homoisocitrate into 2-ketoadipate using NAD(+) as a coenzyme. A series of aza-, oxa-, and thia-analogues of homoisocitrate was designed and synthesized as an inhibitor for homoisocitrate dehydrogenase. Among them, thia-analogue showed strong competitive inhibitory activity as K(i)=97nM toward homoisocitrate dehydrogenase derived from Saccharomyces cerevisiae. Kinetic studies suggested that the formation of the enolate intermediate played an important role in inhibition.

    Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Publishing Authors By Initials

    t yamamotoT Yamamoto,t eguchiT Eguchi,t yamamotoT Yamamoto,t eguchiT Eguchi,

    For similar abstracts research abstracts see: abstracts research

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    Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Bioorganic & medicinal chemistry

    VOLUME: 16

    Page Numbers: 3372-6

    Journal Abbreviation:

    ISSN: 1464-3391

    DAY: 8

    MONTH: 12

    YEAR: 2007

    Thiahomoisocitrate: A highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Information

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    LANGUAGE: eng

    NlmUniqueID: 9413298

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    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Bioorg Med Chem

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