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

This is an abbreviated version!
For detailed information about 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase, go to the full flat file.

Reaction

a [methyl-Co(III) corrinoid Fe-S protein]
+
tetrahydrofolate
=
a [Co(I) corrinoid Fe-S protein]
+
5-methyltetrahydrofolate

Synonyms

acsE, methyltetrahydrofo1ate:corrinoid/iron-sulfur protein methyltransferase, methyltetrahydrofolate corrinoid-iron sulfur protein methyltransferase, methyltetrahydrofolate, corrinoid iron–sulfur protein methyltransferase, methyltetrahydrofolate- and corrinoid-dependent methyltransferase, methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase, methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase MeTr, MeTr

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.258 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase

Reference

Reference on EC 2.1.1.258 - 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seravalli, J.; Zhao, S.; Ragsdale, S.W.
Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis
Biochemistry
38
5728-5735
1999
Moorella thermoacetica
Manually annotated by BRENDA team
Zhao, S.; Roberts, D.; Ragsdale, S.
Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: Origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein
Biochemistry
34
15075-15083
1995
Moorella thermoacetica
Manually annotated by BRENDA team
Zhao, S.; Ragsdale, S.
A conformational change in the methyltransferase from Clostridium thermoaceticum facilitates the methyl transfer from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein in the acetyl-CoA pathway
Biochemistry
35
2476-2481
1996
Moorella thermoacetica
Manually annotated by BRENDA team
Roberts, D.; Zhao, S.; Doukov, T.; Ragsdale, S.
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
1994
Moorella thermoacetica (Q46389)
Manually annotated by BRENDA team
Doukov, T.; Hemmi, H.; Drennan, C.; Ragsdale, S.
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
2007
Moorella thermoacetica
Manually annotated by BRENDA team
Alonso, H.; Cummins, P.; Gready, J.
Methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr): Protonation state of the ligand and active-site residues
J. Phys. Chem. B
113
14787-14796
2009
Moorella thermoacetica (Q46389)
Manually annotated by BRENDA team
Zhu, X.; Gu, X.; Zhang, S.; Liu, Y.; Huang, Z.; Tan, X.
Efficient expression and purification of methyltransferase in acetyl-coenzyme a synthesis pathway of the human pathogen Clostridium difficile
Protein Expr. Purif.
78
86-93
2011
Clostridioides difficile, Clostridioides difficile 630
Manually annotated by BRENDA team
Doukov, T.; Seravalli, J.; Stezowski, J.; Ragsdale, S.
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase
Structure
8
817-830
2000
Moorella thermoacetica (Q46389), Moorella thermoacetica
Manually annotated by BRENDA team
Zhu, X.; Li, T.; Gu, X.; Zhang, S.; Liu, Y.; Wang, Y.; Tan, X.
Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile
Metallomics
5
551-558
2013
Clostridioides difficile, Clostridioides difficile 630
Manually annotated by BRENDA team