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Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase
- 1.0326968 - ÚOCHB 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. E-ISSN 1520-4804
Grant CEP: GA MŠMT 1M0508
Grant ostatní: GA MŠk(CZ) LC06077; NIH(US) R01TW0052501
Program: LC
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
Number of the records: 1