EC Number |
Protein Variants |
Reference |
---|
2.7.7.47 | D178A |
the mutation destabilizes the enzyme leading to reduced melting temperature (47 C). When titrated with streptomycin, temperature stabilization occurs at higher streptomycin concentration compared with wild type, indicating weaker binding affinity |
761481 |
2.7.7.47 | D182A |
mutation reduces the MIC of streptomycin and spectinomycin |
737356 |
2.7.7.47 | D182N |
mutation reduces the MIC of streptomycin and spectinomycin |
737356 |
2.7.7.47 | E87A |
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain |
737356 |
2.7.7.47 | E87Q |
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain |
737356 |
2.7.7.47 | E87Q |
the nonadenylating mutant can hydrolyze ATP in the presence of streptomycin. The mutant does not convey resistance to streptomycin but still binds ATP and streptomycin, although with 4 and 20fold lower affinity than the wild type enzyme |
761481 |
2.7.7.47 | K205A |
mutation reduces the MIC of streptomycin and spectinomycin |
737356 |
2.7.7.47 | more |
amino acid sequence of str is 80.3% and 13.9% identical to 6'-streptomycin adenylyltransferase (aadE) and 3'-streptomycin adenylyltransferase (aadA), respectively, from Enterococcus |
-, 675323 |
2.7.7.47 | more |
amino acid sequence shows 100% identity to plasmid-mediated streptomycin adenylyltransferase gene from Lactococcus lactis |
-, 675323 |
2.7.7.47 | more |
generation of a carboxy-terminal truncated variant molecule, residues 1-264. The truncated residues have little influence on protein folding, whereas they have a positive effect on the enzymic activity and stabilize dimers at high protein concentrations |
-, 739973 |