5-Methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase explained

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Ec Number:	2.1.1.258

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase (acsE (gene)) is an enzyme with systematic name 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase.^{[1] [2] [3]} This enzyme catalyses the following chemical reaction

\rightleftharpoons a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate

This enzyme catalyses the transfer of a methyl group from the N⁵ position of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein, containing a corrin ring similar to that in cobalamin.

Notes and References

1. Roberts DL, Zhao S, Doukov T, Ragsdale SW . The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum . Journal of Bacteriology . 176 . 19 . 6127–30 . October 1994 . 7928975 . 196833 . 10.1128/jb.176.19.6127-6130.1994 .
2. Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW . Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase . Structure . 8 . 8 . 817–30 . August 2000 . 10997901 . 10.1016/s0969-2126(00)00172-6 . free .
3. Doukov TI, Hemmi H, Drennan CL, Ragsdale SW . Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases . The Journal of Biological Chemistry . 282 . 9 . 6609–6618 . March 2007 . 17172470 . 3966722 . 10.1074/jbc.m609828200 . free .