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Structure-Activity Study of New Inhibitors of Human Betaine-Homocysteine S-Methyltransferase

Publikace na Přírodovědecká fakulta |
2009

Tento text není v aktuálním jazyce dostupný. Zobrazuje se verze "en".Abstrakt

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.