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Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase
- 1.0326968 - ÚOCHB 2010 RIV US eng J - Journal Article
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
R&D Projects: GA MŠMT 1M0508
Grant - others:GA MŠk(CZ) LC06077; NIH(US) R01TW0052501
Program: LC
Institutional research plan: CEZ:AV0Z40550506
Keywords : BHMT * betain * homocysteine * methionine * inhibitor
Subject RIV: CE - Biochemistry
Impact factor: 4.802, year: 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.
Permanent Link: http://hdl.handle.net/11104/0173885
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