EC Number   |
Protein Variants |
Reference |
|---|
   2.7.1.190 | F108L |
site-directed mutagenesis, the point mutant and wild-type enzymes have the same structure |
760284 |
| 2.7.1.190 | F95M |
no significantly different binding affinities as compared with the wild-type |
734174 |
| 2.7.1.190 | F95Y |
mutation shifts the nucleotide selectivity from a 2.5fold preference for ATP to a 1.5fold preference for GTP |
734174 |
| 2.7.1.190 | more |
in combination with selection for resistance to the aminoglycoside tobramycin, the aac(6')-Ie/aph(2'')-Ia gene represents an efficient marker for plastid transformation in that it produces similar numbers of transplastomic lines as the spectinomycin resistance gene aadA. No spontaneous antibiotic resistance mutants appear under tobramycin selection |
758025 |
| 2.7.1.190 | more |
The N-terminal region contains a sequence homologous to the chloramphenicol acetyltransferase of Bacillus pumUus, and the C-terminal region contains a sequence homologous to the aminoglycoside phosphotransferase of Streptomyces fradiae. It is possible to obtain gene segments independently specifying the acetyltransferase and phosphotransferase activities |
-, 734051 |
| 2.7.1.190 | S214A |
site-directed mutagenesis |
762483 |
| 2.7.1.190 | S376N |
a clinically identified naturally occuring S376N mutation of APH(2'')-Ia elevates resistance to N1-substituted aminoglycosides but eliminates modification of nonsubstituted compounds. Mutation of serine 376 to asparagine does not lead to substantial rearrangements in the aminoglycoside binding site. In fact, the addition of the larger asparagine residue in place of serine 376 creates an obstruction that prevents binding in the neamine binding pocket. As a result, any compounds that bind using the neamine rings are blocked from the antibiotic binding site of APH(2x02)-Ia. But the mutation remains compatible with one of the alternate binding modes of amikacin, which does not use this site to interact with the enzyme |
760355 |
| 2.7.1.190 | Y237F |
site-directed mutagenesis, the mutant removes the other hydrogen bond between the phosphate and the protein, and a greatly reduced electron density for the gamma-phosphate is observed |
762483 |
| 2.7.1.190 | Y92A |
residue Y92 blocks access to the ATP-binding template. Mutant shows 8fold decrease in km value for ATP |
734173 |
