Literature summary extracted from
Bandarian, V.; Pattridge, K.A.; Lennon, B.W.; Huddler, D.P.; Matthews, R.G.; Ludwig, M.L.
Domain alteration switches B12-dependent methionine synthase to the activation conformation (2002), Nat. Struct. Biol., 9, 53-56.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.1.1.13 |
S-adenosyl-L-methionine |
required |
Escherichia coli |
|
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.1.1.13 |
3.0 A structure of a 65000 Da C-terminal fragment of methionine synthase that spans the cobalamin- and the S-adenosylmethionine-binding domains, arranged in a conformation suitable for the methyl transfer from S-adenosylmethionine to cobalamin that occurs during activation |
Escherichia coli |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.13 |
Escherichia coli |
P13009 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.1.1.13 |
vitamin B12 |
dependent |
Escherichia coli |
|