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Literature summary for 2.1.1.13 extracted from

  • Liptak, M.D.; Datta, S.; Matthews, R.G.; Brunold, T.C.
    Spectroscopic study of the cobalamin-dependent methionine synthase in the activation conformation: effects of the Y1139 residue and S-adenosylmethionine on the B12 cofactor (2008), J. Am. Chem. Soc., 130, 16374-16381.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzymes I690C/G743C and I690C/G743C/Y1139 are expressed in Escherichia coli Hms174(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
I690C/G743C the variant of a C-terminal fragment of MetH locks the enzyme into the activation conformation without perturbing any of the residues in the vicinity of the active site Escherichia coli
I690C/G743C/Y1139F the I690C/G743C MetH variant is trapped in the activation conformation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Hi-Trap column chromatography and MonoQ column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N5-methyltetrahydropteroylmonoglutamate + L-homocysteine
-
Escherichia coli tetrahydropteroylmonoglutamate + L-methionine
-
?

Synonyms

Synonyms Comment Organism
MetH
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
vitamin B12 dependent on Escherichia coli