5-Methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
| 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 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 atoms – the methyltetrahydrofolate contains only two hydrogen atoms more than the tetrahydrofolate. The cobalt atom is able to change oxidation state by obtaining electrons frpm the 4Fe-4S complex in the protein.[4]
References
[edit]- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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. 1784 (12): 1873–1898. doi:10.1016/j.bbapap.2008.08.012. PMC 2646786. PMID 18801467.
External links
[edit]- 5-methyltetrahydrofolate:corrinoid/iron-sulfur+protein+Co-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
