Abstract
I am deeply honored to be chosen as the Frederick Gowland Hopkins lecturer by my friends and colleagues. The honor is particularly special for me because my father traveled from New York to Cambridge to do his Ph.D. dissertation research in Hopkins laboratory. My father received his Ph.D. in 1934, at a time when biochemistry in the States was in its infancy. Hopkins’ brilliant research on vitamins and cofactors, and on cellular metabolism, made his laboratory the place to study biochemistry.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Taylor R.T., Weissbach H. Escherichia coli B N5-methyltetrahydrofolate-homocysteine methytransferase: Sequential formation of bound methylcobalamin with S-adenosyl-L-methionine and N5-methyltetrahydrofolate. Arch. Biochem. Biophys. 129: 728–744, 1969.
Fujii K., Huennekens F.M. Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system. J. Biol. Chem. 249: 6745–6753, 1974.
Taylor R.T., Weissbach H. Escherichia coli B N5-methyltetrahydrofolate-homocysteine vitamin-B12 transmethylase: formation and photolability of a methylcobalamin enzyme. Arch. Biochem. Biophys. 123: 109–126, 1968.
Doukov T., Seravelli J., Stezowski J.J., Ragsdale S.W. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyl transferase. Structure. 8: 817–830, 2000.
Smith A.E., Matthews R.G. 2000. The protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase. Biochemistry. 39:13880–13890.
Drummond J.T., Huang S., Blumenthal R.M., Matthews R.G. Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli. Biochemistry. 32: 9290–9295, 1993.
Goulding C.W., Matthews R.G. Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry. 36: 15749–15757, 1997.
Goulding C.W., Postigo D., Matthews R.G. Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry. 36: 8082–8091, 1997.
Taylor R.T. Methylcobalamin as a substrate at a separate site on Escherichia coli B N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase. Arch. Biochem. Biophys. 144:352–362, 1971.
Roberts D.L., Zhao S., Doukov T., Ragsdale S.W. The reductive acetyl-CoA pathway: sequence and heterologous expression of active CH3-H4 folatexorrinoid/iron sulfur protein methyltransferase from Clostridium thermoaceticum. J. Bacteriol. 176: 6127–6130, 1994.
Goulding C.W., Matthews R.G. Cobalamin-dependent methionine synthase from Escherichia coli: zinc is required for methyl transfer from methylcobalamin to homocysteine. Biochemistry. 36: 15749–15757, 1997.
Drennan C. L., Huang S., Drummond J.T., Matthews R.G. Ludwig M.L. How a protein binds B12: A 3.0 Å x-ray structure of the B12 binding domains of methionine synthase. Science. 266: 1669–1674, 1994.
Jarrett J.T., Choi C.Y., Matthews R.G. Changes in protonation associated with substrate binding and cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry. 36: 15739–15748, 1997.
Drummond J.T., Matthews R.G. Nitrous oxide degradation by cobalamin-dependent methionine synthase: characterization of the reactants and products in the inactivation reaction. Biochemistry. 33: 3732–3741, 1994.
Drummond J.T., Matthews R.G. “Cobalamin-dependent methionine synthase: dissection of a large protein into functional and structural domains.” In B. Golden (ed.), Proceedings of the Conference on Organic Reactivity: Physical and Biological Aspects. Royal Society of Chemistry, Cambridge, pp. 58–72, 1993.
Hall D.E., Jordan-Starck T.C., Loo R.O., Ludwig M.L., Matthews R.G. Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemisty. 39: 10711–10719, 2000.
Jarrett J. T., Drennan C. L., Amaratunga M., Schölten J.D., Ludwig M.L., Matthews R.G. A protein radical cage slows photolysis of methylcobalamin in methionine synthase from Escherichia coli. J. Bioorgan. Med. Chem. 4: 1237–1246, 1996.
Bandarian V., Matthews R.G. Quantitation of rate enhancements attained by the binding of cobalamin to methionine synthase. Biochemistry. 40: 5056–5064, 2001.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media New York
About this chapter
Cite this chapter
Matthews, R.G. (2002). Making Methionine: A Love Affair with Folate. In: Milstien, S., Kapatos, G., Levine, R.A., Shane, B. (eds) Chemistry and Biology of Pteridines and Folates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0945-5_1
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0945-5_1
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5317-1
Online ISBN: 978-1-4615-0945-5
eBook Packages: Springer Book Archive