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Literature summary for 2.5.1.6 extracted from

  • Taylor, J.C.; Markham, G.D.
    The bifunctional active site of S-adenosylmethionine synthetase. Roles of the active site aspartates (1999), J. Biol. Chem., 274, 32909-32914.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ cannot be replaced by Ca2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A817 XL1-Blue strain
-
Escherichia coli XL1-Blue P0A817 XL1-Blue strain
-

Purification (Commentary)

Purification (Comment) Organism
method that includes ammonium sulfate fraction, phenyl-Sepharose HR chromatographies and amminohexyl-Sepharose anion exchange Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants Escherichia coli ?
-
?
additional information S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants Escherichia coli XL1-Blue ?
-
?

Subunits

Subunits Comment Organism
tetramer native polyacrylamide gel electrophoresis Escherichia coli