The enzyme catalyzes the conversion of of (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA. It is a homodimer that binds a divalent metal ion per subunit. Metal ions are coordinated at the interface of subunits (PMID11470438).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CO(not in PDB) 1 x | CO | cobalt | divalent cation (different per organism) | mononuclear | Coordinates substrate Electrostatic stabiliser Increases acidity |
*It refers to the MACiE reference pdb: 1jc5
| Metal/s Properties in Resting State | ||||||
| CO(not in PDB) 1 x | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | The metal ligands should be His12, Gln65, His91, Glu141 and two water molecules (residue numbers taken from 1JC5). | |||||
| References |
| -Armstrong RN Mechanistic diversity in a metalloenzyme superfamily. Biochemistry. 2000 Nov 14;39(45):13625-32.(MEDLINE:11076500) |
| - Some information have been also deduced from the MACiE mechanism model |