The enzyme catalyzes the cobalamin-dependent transfer of a methyl group from N5-methyltetrahydrofolate to homocysteine, producing tetrahydrofolate and methionine
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| COB 122 A | CO | cobalt | cobalt | cobalamin | Promotes heterolysis Electron pair acceptor Coordinates substrate One electron donor Electron pair donor |
*It refers to the MACiE reference pdb: 1bmt
| Metal/s Properties in Resting State | ||||||
| COB 122 A | Resting state enzyme (1bmt) | |||||
| Oxidation State | 3 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -Datta S, Pattridge KA, Smith JL, Matthews RG Insights into the reactivation of cobalamin-dependent methionine synthase. Proc Natl Acad Sci U S A. 2009 Nov 3;106(44):18527-32. Epub 2009 Oct 21.(MEDLINE:19846791) |
| -Matthews RG Protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase. Biochemistry. 2000 Nov 14;39(45):13880-90.(MEDLINE:11076529) |