EC Number   |
Protein Variants |
Reference |
|---|
   5.6.2.2 | A772P |
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, about 10% activity compared to the recombinant wild-type enzyme in strain JN394t2-4 |
662968 |
| 5.6.2.2 | C170A |
potential site of quinone adduction. Mutant does not show reduced sensitivity to benzoquinone |
678261 |
| 5.6.2.2 | C392A |
potential site of quinone adduction. Mutant shows 50% reduced sensitivity to benzoquinone and displays 2fold faster rates of DNA religation than wild-type. Mutation does not affect the ability of benzoquinone to block the N-terinal gate of the enzyme |
678261 |
| 5.6.2.2 | C405A |
potential site of quinone adduction. Mutant shows 50% reduced sensitivity to benzoquinone and displays 2fold faster rates of DNA religation than wild-type. Mutation does not affect the ability of benzoquinone to block the N-terinal gate of the enzyme |
678261 |
| 5.6.2.2 | C455A |
mutant is 1.5fold more sensitive to 1,4-benzoquinone and 2-(4-chlorophenyl)benzo-1,4-quinone, but shows wild-type sensitivity to traditional topoisomerase II poisons |
679203 |
| 5.6.2.2 | C455A |
potential site of quinone adduction. Mutant does not show reduced sensitivity to benzoquinone |
678261 |
| 5.6.2.2 | D130G |
site-directed mutagenesis, reduced ATPase activity compared to the wild-type |
661004 |
| 5.6.2.2 | D211K/E212K/E213K/E214K |
site-directed mutagenesis, the GyrBAKKKK mutant comprises the charge-reversal mutation of all the acidic residues composing the DEEE loop into basic ones (211DEEE214 into 211KKKK214) |
-, 758494 |
| 5.6.2.2 | D75N |
nucleotide-binding-deficient mutant of subunit GyrB |
751334 |
| 5.6.2.2 | E155F |
site-directed mutagenesis, mutation of ATP binding pocket residue in the N-terminal domain, no reduction of ATPase activity compared to the wild-type, altered etoposide binding compared the wild-type |
661004 |
