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Gene Review

ECs3818  -  methionine adenosyltransferase

Escherichia coli O157:H7 str. Sakai

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  1. S-Adenosylmethionine synthetase from Escherichia coli. Markham, G.D., Hafner, E.W., Tabor, C.W., Tabor, H. J. Biol. Chem. (1980) [Pubmed]
  2. Cloning expression and characterization of methionine adenosyltransferase in Leishmania infantum promastigotes. Reguera, R.M., Balaña-Fouce, R., Pérez-Pertejo, Y., Fernández, F.J., García-Estrada, C., Cubría, J.C., Ordóñez, C., Ordóñez, D. J. Biol. Chem. (2002) [Pubmed]
  3. The bifunctional active site of S-adenosylmethionine synthetase. Roles of the basic residues. Taylor, J.C., Markham, G.D. J. Biol. Chem. (2000) [Pubmed]
  4. Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition. McQueney, M.S., Markham, G.D. J. Biol. Chem. (1995) [Pubmed]
  5. Identification of the reactive sulfhydryl groups of S-adenosylmethionine synthetase. Markham, G.D., Satishchandran, C. J. Biol. Chem. (1988) [Pubmed]
  6. The bifunctional active site of s-adenosylmethionine synthetase. Roles of the active site aspartates. Taylor, J.C., Markham, G.D. J. Biol. Chem. (1999) [Pubmed]
  7. The conformations of a substrate and a product bound to the active site of S-adenosylmethionine synthetase. Schalk-Hihi, C., Markham, G.D. Biochemistry (1999) [Pubmed]
  8. The active-site arginine of S-adenosylmethionine synthetase orients the reaction intermediate. Reczkowski, R.S., Taylor, J.C., Markham, G.D. Biochemistry (1998) [Pubmed]
  9. Isolation of a metK mutant with a temperature-sensitive S-adenosylmethionine synthetase. Hafner, E.W., Tabor, C.W., Tabor, H. J. Bacteriol. (1977) [Pubmed]
  10. Refolding and characterization of rat liver methionine adenosyltransferase from Escherichia coli inclusion bodies. López-Vara, M.C., Gasset, M., Pajares, M.A. Protein Expr. Purif. (2000) [Pubmed]
  11. Expression of the cloned genes encoding the putrescine biosynthetic enzymes and methionine adenosyltransferase of Escherichia coli (speA, speB, speC and metK). Boyle, S.M., Markham, G.D., Hafner, E.W., Wright, J.M., Tabor, H., Tabor, C.W. Gene (1984) [Pubmed]
  12. Multiple forms of lysyl-transfer ribonucleic acid synthetase in Escherichia coli. Hirshfield, I.N., Bloch, P.L., Van Bogelen, R.A., Neidhardt, F.C. J. Bacteriol. (1981) [Pubmed]
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