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

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Identifiers
EC number 2.1.1.258
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase (EC 2.1.1.258, 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

[Methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate 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.

References

  1. ↑ Roberts DL, Zhao S, Doukov T, Ragsdale SW (October 1994). "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. doi:10.1128/jb.176.19.6127-6130.1994. PMC 196833. PMID 7928975.
  2. ↑ Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW (August 2000). "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase". Structure. 8 (8): 817–30. doi:10.1016/s0969-2126(00)00172-6. PMID 10997901.
  3. ↑ Doukov TI, Hemmi H, Drennan CL, Ragsdale SW (March 2007). "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. doi:10.1074/jbc.m609828200. PMC 3966722. PMID 17172470.
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