EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
2.1.1.184 | 705957 |
Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions |
Nucleic Acids Res. |
31 |
4941-4949 |
2003 |
Bacillus subtilis |
12907737 |
2.1.1.184 | 705957 |
Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions |
Nucleic Acids Res. |
31 |
4941-4949 |
2003 |
Bacillus subtilis BD1167 |
12907737 |
2.1.1.184 | 485441 |
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria |
Biochemistry |
37 |
7103-7112 |
1998 |
Bacillus subtilis |
9585521 |
2.1.1.184 | 702189 |
Dubnau, D.: Binding of Bacillus subtilis ermC' methyltransferase to 23S rRNA |
Biochemistry |
29 |
6033-6042 |
1990 |
Bacillus subtilis |
2116903 |
2.1.1.184 | 734477 |
Evolved Escherichia coli strains for amplified, functional expression of membrane proteins |
J. Mol. Biol. |
426 |
136-149 |
2014 |
Escherichia coli |
24041572 |
2.1.1.184 | 704243 |
Induction of ermC methylase in the absence of macrolide antibiotics and by pseudomonic acid A |
J. Bacteriol. |
171 |
4518-4520 |
1989 |
Bacillus subtilis |
2502538 |
2.1.1.184 | 705109 |
Kavanaugh, T.J.; Abad-Zapatero, C.: The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism |
J. Mol. Biol. |
289 |
277-291 |
1999 |
Bacillus subtilis |
10366505 |
2.1.1.184 | 485438 |
Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase |
J. Biol. Chem. |
264 |
2615-2624 |
1989 |
Bacillus subtilis |
2492520 |
2.1.1.184 | 485438 |
Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase |
J. Biol. Chem. |
264 |
2615-2624 |
1989 |
Bacillus subtilis BD170 |
2492520 |
2.1.1.184 | 662611 |
Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC' |
J. Mol. Biol. |
332 |
99-109 |
2003 |
Bacillus subtilis |
12946350 |