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Literature summary for 2.7.1.190 extracted from

  • Shi, K.; Houston, D.R.; Berghuis, A.M.
    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.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Enterococcus casseliflavus O68183 isoform aminoglycoside-2''-phosphotransferase type IVa
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Synonyms

Synonyms Comment Organism
aminoglycoside-2''-phosphotransferase type IVa
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Enterococcus casseliflavus
APH(2'')-IVa
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Enterococcus casseliflavus