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 \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.

References

  1. Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. (1994). "The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum". J. Bacteriol. 176: 6127–6130. PMID 7928975.
  2. Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. (2000). "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase". Structure 8: 817–830. doi:10.1016/s0969-2126(00)00172-6. PMID 10997901.
  3. Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. (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". J. Biol. Chem. 282: 6609–6618. doi:10.1074/jbc.m609828200. PMID 17172470.

External links

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