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

Class of enzymes

Class of enzymes

FieldValue
Name5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
EC_number2.1.1.258

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase (, acsE (gene)) is an enzyme with systematic name 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase. 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 carbon atom and associated hydrogen atoms 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. Although called a methyl transferase, the net transfer is of one carbon atom and two hydrogen atomsthe methyltetrahydrofolate contains only two hydrogen atoms more than the tetrahydrofolate. The cobalt atom is able to change oxidation state by obtaining electrons from the 4Fe-4S complex in the protein.

References

References

  1. (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.
  2. (August 2000). "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase". Structure.
  3. (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.
  4. Stephen Ragsdale and Elizabeth Pierce. (December 2008). "Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics.
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ec-2.1.1
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