Information on EC - aminoglycoside 2''-phosphotransferase

for references in articles please use BRENDA:EC2.7.1.190
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
Specify your search results
Select one or more organisms in this record: ?
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
aph(2'')-id, aph(2''), aminoglycoside kinase, aph(2'')-ia, aph(2'')-iva, aac6-aph2, aph(2'')-iiia, aminoglycoside 2''-phosphotransferase, aminoglycoside 2''-phosphotransferase type iiia, aph(2'')-if, more
GTP + gentamicin = GDP + gentamicin 2''-phosphate
show the reaction diagram
Select items on the left to see more content.