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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F09%3A00326968" target="_blank" >RIV/61388963:_____/09:00326968 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/09:10109553

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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 andinhibitors.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/1M0508" target="_blank" >1M0508: New Antivirals and Antineoplastics</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2009

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Medicinal Chemistry

ISSN

0022-2623

e-ISSN

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Volume of the periodical

52

Issue of the periodical within the volume

12

Country of publishing house

US - UNITED STATES

Number of pages

14

Pages from-to

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UT code for WoS article

000267180600006

EID of the result in the Scopus database

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