JBC Transcription and Nuclear Factor Monoclonals

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The Role of Cobamides in Methionine Synthesis

ENZYMATIC FORMATION OF HOLOENZYME

Nathan Brot 1 and Herbert Weissbach 1

From the 1 From the Laboratory of Clinical Biochemistry, National Heart Institute, and Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20014

An enzyme has been obtained from extracts of Escherichia coli which catalyzes the synthesis of N5-methyltetrahydrofolate-homocysteine methyltransferase holoenzyme from apoenzyme and 5,6-dimethylbenzimidazolylcobamide deoxyadenosyl in the presence of a reduced pyridine nucleotide. In addition to holoenzyme formation, this system supplies the reducing power for the synthesis of methionine from N5-methyl-H4-folate. It is suggested that this enzyme system functions by reducing the cobamide prosthetic group, and that it may be the natural reducing system required for methionine synthesis in E. coli.

Submitted on January 3, 1966


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 Proc. Natl. Acad. Sci. USAHome page
K. Yamada, R. A. Gravel, T. Toraya, and R. G. Matthews
Human methionine synthase reductase is a molecular chaperone for human methionine synthase
PNAS, June 20, 2006; 103(25): 9476 - 9481.
[Abstract] [Full Text] [PDF]


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