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The reactivity of B12 cofactors: the proteins make a difference Ludwig ML; Drennan CL; Matthews RGStructure 1996[May]; 4 (5): 505-12Determination of the structure of intact methylmalonyl-CoA mutase from Propionibacterium shermanii, and comparisons with the structure of the cobalamin-binding fragment of methionine synthase from Escherichia coli, afford a first glimpse at the similarities and distinctions between the two principal classes of B12-dependent enzymes: the mutases and the methyltransferases.|5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Benzimidazoles/*chemistry[MESH]|Cobamides/*chemistry[MESH]|Escherichia coli/chemistry[MESH]|Histidine/metabolism[MESH]|Humans[MESH]|Methylmalonyl-CoA Mutase/chemistry[MESH]|Methyltransferases/metabolism[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Propionibacterium/chemistry[MESH]|Vitamin B 12/*analogs & derivatives/chemistry[MESH] |
