Kinetic Parameter Values Used in the Model

SUPPLEMENTAL DATA

Kinetic parameter values used in the model

(Km in µM, Vmax in µM/hr)

References

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2.D'Ari, L., and J. C. Rabinowitz. 1991. Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli. J Biol Chem 266:23953-8.

3.Dalal, F. R., and J. S. Gots. 1967. Purification of 5,10-methylenetetrahydrofolate dehydrogenase from Salmonella typhimurium and its inhibition by purine nucleotides. J Biol Chem 242:3636-40.

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8.Graziani, S., Y. Xia, J. R. Gurnon, J. L. Van Etten, D. Leduc, S. Skouloubris, H. Myllykallio, and U. Liebl. 2004. Functional analysis of FAD-dependent thymidylate synthase ThyX from Paramecium bursaria Chlorella virus-1. J Biol Chem 279:54340-7.

9.Guenther, B. D., C. A. Sheppard, P. Tran, R. Rozen, R. G. Matthews, and M. L. Ludwig. 1999. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat Struct Biol 6:359-65.

10.Inglese, J., D. L. Johnson, A. Shiau, J. M. Smith, and S. J. Benkovic. 1990. Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. Biochemistry 29:1436-43.

11.Mahdavian, E., H. T. Spencer, and R. B. Dunlap. 1999. Kinetic studies on drug-resistant variants of Escherichia coli thymidylate synthase: functional effects of amino acid substitutions at residue 4. Arch Biochem Biophys 368:257-64.

12.Nagy, P. L., A. Marolewski, S. J. Benkovic, and H. Zalkin. 1995. Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli. J Bacteriol 177:1292-8.

13.Phan, J., E. Mahdavian, M. C. Nivens, W. Minor, S. Berger, H. T. Spencer, R. B. Dunlap, and L. Lebioda. 2000. Catalytic cysteine of thymidylate synthase is activated upon substrate binding. Biochemistry 39:6969-78.

14.Pomper, B. K., J. A. Vorholt, L. Chistoserdova, M. E. Lidstrom, and R. K. Thauer. 1999. A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1. Eur J Biochem 261:475-80.

15.Schirch, V., S. Hopkins, E. Villar, and S. Angelaccio. 1985. Serine hydroxymethyltransferase from Escherichia coli: purification and properties. J Bacteriol 163:1-7.

16.Shaw, D., J. D. Odom, and R. B. Dunlap. 1999. High expression and steady-state kinetic characterization of methionine site-directed mutants of Escherichia coli methionyl- and selenomethionyl-dihydrofolate reductase. Biochim Biophys Acta 1429:401-10.

17.Taylor, R., and H. Weissbach. 1973. The Enzymes, 3rd Ed. (Boyer, P.D., ed.) 12:121-165.

18.Taylor, R., and H. Weissbach. 1971. Methods Enzymol 17B:379-388.

19.Trimmer, E. E., D. P. Ballou, M. L. Ludwig, and R. G. Matthews. 2001. Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry 40:6216-26.

20.Wilquet, V., M. Van de Casteele, D. Gigot, C. Legrain, and N. Glansdorff. 2004. Dihydropteridine reductase as an alternative to dihydrofolate reductase for synthesis of tetrahydrofolate in Thermus thermophilus. J Bacteriol 186:351-5.

21.Zhou, Z. S., A. E. Smith, and R. G. Matthews. 2000. L-Selenohomocysteine: one-step synthesis from L-selenomethionine and kinetic analysis as substrate for methionine synthases. Bioorg Med Chem Lett 10:2471-5.

[1] If the reference is not indicated, the values where collected from BRENDA database.