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Literature summary extracted from
- Crystal structures of antibiotic-bound complexes of aminoglycoside 2-phosphotransferase IVa highlight the diversity in substrate binding modes among aminoglycoside kinases (2011), Biochemistry, 50, 6237-6244.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 2.7.1.190 | apo form and in complex with a bound antibiotic, tobramycin and kanamycin A, to 2.05 A, 1.8 A and 2.15 A resolution, respectively. Substrate binding induces conformational changes, involving rotational shifts of two distinct segments of the enzyme. The helical subdomain is important in substrate specificity | Enterococcus casseliflavus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.7.1.190 | Enterococcus casseliflavus | O68183 | isoform aminoglycoside-2''-phosphotransferase type IVa | - |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.7.1.190 | aminoglycoside-2''-phosphotransferase type IVa | - |
Enterococcus casseliflavus |
| 2.7.1.190 | APH(2'')-IVa | - |
Enterococcus casseliflavus |
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Release 2023.1 (January 2023)
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