Literature summary extracted from
Brooks, A.J.; Fox, C.C.; Marsh, E.N.; Vlasie, M.; Banerjee, R.; Brunold, T.C.
Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase (2005), Biochemistry, 44, 15167-15181.
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.4.99.1 |
Clostridium cochlearium |
- |
expression in Escherichia coli as fusion protein |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
5.4.99.1 |
L-threo-3-methylaspartate = L-glutamate |
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals |
Clostridium cochlearium |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
5.4.99.1 |
adenosylcobalamin |
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals |
Clostridium cochlearium |
|