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  1. Article

    Open Access

    Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp, and ArgR

    The glutamate synthase operon (gltBDF) contributes to one of the two main pathways of ammonia assimilation in Escherichia coli. Of the seven most-global regulators, together affecting expression of about half of ...

    Ligi Paul, Pankaj K Mishra, Robert M Blumenthal, Rowena G Matthews in BMC Microbiology (2007)

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  2. No Access

    Article

    Effector regulation in a monomeric enzyme

    The monomeric B12-dependent ribonucleotide reductase from L. leichmannii has the central 10-stranded α/β-barrel found in all ribonucleotide reductases but incorporates two distinctive structural features, a novel...

    Martha L. Ludwig, Rowena G. Matthews in Nature Structural Biology (2002)

  3. No Access

    Article

    Domain alternation switches B12-dependent methionine synthase to the activation conformation

    B12-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain h...

    Vahe Bandarian, Katherine A. Pattridge, Brett W. Lennon… in Nature Structural Biology (2002)

  4. No Access

    Chapter

    Making Methionine: A Love Affair with Folate

    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...

    Rowena G. Matthews in Chemistry and Biology of Pteridines and Folates (2002)

  5. No Access

    Article

    The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia

    Elevated plasma homocysteine levels are associated with increased risk for cardiovascular disease and neural tube defects in humans. Folate treatment decreases homocysteine levels and dramatically reduces the ...

    Brian D. Guenther, Christal A. Sheppard, Pamela Tran… in Nature Structural Biology (1999)

  6. No Access

    Chapter

    Methylenetetrahydrofolate Reductase: Comparison of the Enzyme from Mammalian and Bacterial Sources

    Methylenetetrahydrofolate reductase catalyzes the reduction of methylenetetrahydrofolate to methyl-tetrahydrofolate, which serves as the methyl donor for the conversion of homocysteine to methionine in the rea...

    Christal A. Sheppard, James S. Sumner… in Homocysteine Metabolism: From Basic Scienc… (1997)

  7. No Access

    Article

    Human methylenetetrahydrofolate reductase: isolation of cDNA, map** and mutation identification

    Methylenetetrahydrofolate reductase (MTHFR) catalyses the reduction of methylenetetrahydrofolate to methyltetrahydrofolate, a cofactor for homocysteine methylation to methionine. MTHFR deficiency, an autosomal...

    Philippe Goyette, James S. Sumner, Renate Milos, Alessandra M.V. Duncan… in Nature Genetics (1994)

  8. No Access

    Chapter

    Cobalamin-Dependent and Cobalamin-Independent Methionine Synthases in Escherichia coli: Two Solutions to the Same Chemical Problem

    Two genes encoding proteins with methionine synthase activity are found in Escherichia coli. Both enzymes use methyltetrahydrofolate as a methyl donor to catalyze the conversion of homocysteine to methionine, as ...

    James T. Drummond, Rowena G. Matthews in Chemistry and Biology of Pteridines and Folates (1993)

  9. No Access

    Chapter

    The Role of Folylpolyglutamates in the Regulation of Folate Metabolism

    Folylpolyglutamates have been shown to function as potent inhibitors, relative to the corresponding monoglutamates, of two enzymes involves in the metabolism of methylenetetrahydrofolate (CH2-H4folate) in mammali...

    Rowena G. Matthews, Jonathan Ross, Charles M. Baugh… in Folyl and Antifolyl Polyglutamates (1983)

  10. No Access

    Chapter

    Interactions of adenosylmethionine with methylenetetrahydrofolate reductase

    Commercial preparations of AdoMet are isolated from yeast, and the AdoMet has the configuration of the natural diastereoisomer at both the sulfonium pole and the methionyl substituent. However, such preparatio...

    S Colette Creveling, Elisa C Krapf… in Biochemistry of S-Adenosylmethionine and R… (1982)

  11. No Access

    Chapter

    A New Intermediate in TPNH-Linked Flavoproteins

    The early studies of Michaelis et. al. (1) clearly indicated that partial reduction of the flavin coenzymes led to the production of colored radical intermediates. Except for the catio-nic radical, which is produ...

    Vincent Massey, Rowena G. Matthews… in Pyridine Nucleotide-Dependent Dehydrogenas… (1970)