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- Title
Unique Double-Barreled Enzyme Makes Methionine the Hard Way.
- Authors
R., Pejchal; M.L., Ludwig
- Abstract
The article informs that each reaction is catalyzed by a specific enzyme, whose uniquely shaped active site not only binds reactants, but, by forming weak and temporary bonds, coaxes them into new orientations with new partners, thus creating the products. Researchers elucidate the structure of cobalamin-independent methionine synthase from the bacterium Thermotoga maritima , and describe how it catalyzes the formation of the amino acid methionine. Methionine synthases actually come in two forms, which use somewhat different mechanisms to accomplish the same task: transfer of a methyl group from methyltetrahydrofolate to the terminal sulfur of homocysteine.
- Publication
PLoS Biology, 2005, Vol 3, Issue 2, p1
- ISSN
1544-9173
- Publication type
Academic Journal
- DOI
10.1371/journal.pbio.0030031