Počet záznamů: 1

Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase

  1. 1.
    0326968 - UOCHB-X 2010 RIV US eng J - Článek v odborném periodiku
    Vaněk, Václav - Buděšínský, Miloš - Kabeleová, Petra - Šanda, Miloslav - Kožíšek, Milan - Hančlová, Ivona - Mládková, Jana - Brynda, Jiří - Rosenberg, Ivan - Koutmos, M. - Garrow, T. A. - Jiráček, Jiří
    Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase.
    Journal of Medicinal Chemistry. Roč. 52, č. 12 (2009), s. 3652-3665 ISSN 0022-2623
    Grant CEP: GA MŠk 1M0508
    Grant ostatní: GA MŠk(CZ) LC06077; NIH(US) R01TW0052501
    Výzkumný záměr: CEZ:AV0Z40550506
    Klíčová slova: BHMT * betain * homocysteine * methionine * inhibitor
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 4.802, rok: 2009

    In this study, we prepared a new series of betaine-homocysteine S-methyltransferase (BHMT) inhibitors. The inhibitors were designed to mimic the hypothetical transition state of BHMT substrates, betaine and homocysteine, and consisted of analogues with NH, N(CH3), or N(CH3)2 groups separated from the homocysteine sulfur atom by a methylene, ethylene, or a propylene spacer. The inhibition results evoke questions about putative conformational changes of BHMT upon the binding of the substrates/products and inhibitors.
    Trvalý link: http://hdl.handle.net/11104/0173885