Literature summary for 2.1.1.13 extracted from

Datta, S.; Koutmos, M.; Pattridge, K.A.; Ludwig, M.L.; Matthews, R.G.
A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor (2008), Proc. Natl. Acad. Sci. USA, 105, 4115-4120.

Search for more literature for 2.1.1.13

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli Hms174(DE3) cells	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
the 65-kDa I690C/G743C MetH fragment is crystallized by the microbatch method, using 0.2 M potassium nitrate and 20% (w/v) PEG3350	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
I690C/G743C	the mutant is locked in the reactivation conformation and found in both His-on and -off states	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P13009	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-charged HiTrap chelating column chromatography and Mono Q 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
B12-dependent methionine synthase	-	Escherichia coli
MetH	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
vitamin B12	-	Escherichia coli

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Release 2023.1 (January 2023)