EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
2.1.1.258 | 718824 |
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 |
8652591 |
2.1.1.258 | 721068 |
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase |
Structure |
8 |
817-830 |
2000 |
Moorella thermoacetica |
10997901 |
2.1.1.258 | 720970 |
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 |
21324365 |
2.1.1.258 | 720970 |
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 630 |
21324365 |
2.1.1.258 | 717236 |
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 |
10231523 |
2.1.1.258 | 718823 |
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 |
7578120 |
2.1.1.258 | 720305 |
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 |
19827815 |
2.1.1.258 | 728242 |
Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile |
Metallomics |
5 |
551-558 |
2013 |
Clostridioides difficile |
23599026 |
2.1.1.258 | 728242 |
Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile |
Metallomics |
5 |
551-558 |
2013 |
Clostridioides difficile 630 |
23599026 |
2.1.1.258 | 719846 |
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 |
17172470 |