The reactivity of B12 cofactors: the proteins make a difference.
Determination 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.
Ludwig
M L
ML
Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor 48109-1055, USA.
Drennan
C L
CL
Matthews
R G
RG
D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001562:Benzimidazoles / Q000737:chemistry*; D003038:Cobamides / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry; D006639:Histidine / Q000378:metabolism; D006801:Humans; D008765:Methylmalonyl-CoA Mutase / Q000737:chemistry; D008780:Methyltransferases / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011424:Propionibacterium / Q000737:chemistry; D014805:Vitamin B 12 / Q000031:analogs & derivatives* / Q000737:chemistry
D001562:Benzimidazoles; D003038:Cobamides; D006639:Histidine; C015158:5,6-dimethylbenzimidazole; C019476:mecobalamin; D008780:Methyltransferases; D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide; D014805:Vitamin B 12