Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Information on EC 2.7.1.190 - 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.
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.

The enzyme appears in viruses and cellular organisms

Synonyms
aph(2'')-id, aminoglycoside kinase, aph(2''), aph(2'')-ia, aph(2'')-iva, aac6-aph2, aph(2'')-iiia, aminoglycoside 2''-phosphotransferase, gentamicin phosphotransferase, aminoglycoside 2''-phosphotransferase iva, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + gentamicin = GDP + gentamicin 2''-phosphate
show the reaction diagram