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

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5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Identifiers
EC no.2.1.1.258
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IntEnzIntEnz view
BRENDABRENDA entry
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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, D.L.; Zhao, S.; Doukov, T.; 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.; 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.; 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)