Differences in folate-protein interactions result in differing inhibition of native rat liver and recombinant glycine N-methyltransferase by 5-methyltetrahydrofolate

Article ID	Journal	Published Year	Pages	File Type
10536852	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics	2012	6 Pages	PDF

Abstract

âº We crystallized rat liver glycine N-methyltransferase with folate inhibitors. âº We compared structures of these complexes with that formed by recombinant protein. âº Folates establish more hydrogen bonds with native liver protein. âº This explains more efficient inhibition of liver glycine N-methyltransferase.

Keywords

AdoMet S-adenosylhomocysteine GNMT AdoHcy S-adenosylmethionine Inhibition Crystal structure Folate glycine N-methyltransferase

Related Topics

Physical Sciences and Engineering Chemistry Analytical Chemistry

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Differences in folate-protein interactions result in differing inhibition of native rat liver and recombinant glycine N-methyltransferase by 5-methyltetrahydrofolate

Authors

Zigmund Luka, Svetlana Pakhomova, Lioudmila V. Loukachevitch, Marcia E. Newcomer, Conrad Wagner,