The enzyme catalyzes the reversible rearrangement of succinyl-CoA into methylmalonyl-CoA by a free-radical mechanism (PMID8805541). It uses coenzyme B12 (adenosylcobalamin) as a cofactor which contains a cobalt ion (PMID8805541).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| B12 800 A | CO | cobalt | cobalt | cobalamin | Promotes homolysis |
*It refers to the MACiE reference pdb: 1req
| Metal/s Properties in Resting State | ||||||
| B12 800 A | Resting state enzyme (3req) | |||||
| Oxidation State | 3 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -Mansoorabadi SO, Padmakumar R, Fazliddinova N, Vlasie M, Banerjee R, Reed GH Characterization of a succinyl-CoA radical-cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase. Biochemistry. 2005 Mar 8;44(9):3153-8.(MEDLINE:15736925) |