| EC |
2.1.1.389 |
| Accepted name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]—tetrahydrofolate methyltransferase |
| Reaction: |
a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) quaternary-amine-specific corrinoid protein] |
| Other name(s): |
mtqA (gene name) (ambiguous); [methyl-Co(III) MtqC corrinoid protein]—tetrahydrofolate methyltransferase |
| Systematic name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]:tetrahydrofolate methyltransferase |
| Comments: |
The enzyme, characterized from the acetogenic gut bacterium Eubacterium limosum, participates in a pathway for the degradation of some quaternary amine compounds (L-proline betaine and L-carnitine). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (bacterial MtqC) to tetrahydrofolate. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697–13707. [DOI] [PMID: 31341018] |
| 2. |
Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971–11981. [DOI] [PMID: 32571881] |
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| [EC 2.1.1.389 created 2023] |
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