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2.7.1.190: aminoglycoside 2''-phosphotransferase

This is an abbreviated version!
For detailed information about aminoglycoside 2''-phosphotransferase, go to the full flat file.

Word Map on EC 2.7.1.190

Reaction

GTP
+
gentamicin
=
GDP
 +
gentamicin 2''-phosphate

Synonyms

AAC(6')-APH(2''), AAC(6')-Ie/APH(2'')-Ia, aac6-aph2, aacA-aphD, AME, aminoglycoside (2'') kinase, aminoglycoside 2''-phosphotransferase IVa, aminoglycoside 2''-phosphotransferase type IIIa, aminoglycoside kinase, aminoglycoside phosphotransferase, aminoglycoside-2''-phosphotransferase, aminoglycoside-2''-phosphotransferase type IVa, aminoglycoside-modification enzyme, APH, APH(2''), APH(2'')-Ia, APH(2'')-Ia aminoglycoside resistance enzyme, APH(2'')-Id, Aph(2'')-If, APH(2'')-IIIa, APH(2'')-IVa, aphD, AphSR2, bifunctional 6'-aminoglycoside acetyltransferase/2"-aminoglycoside phosphotransferase, bifunctional AAC/APH, bifunctional aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2'')-Ia, bifunctional aminoglycoside acetyltransferase/phosphotransferase, gentamicin kinase, gentamicin phosphotransferase, gentamicin resistance protein

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.190 aminoglycoside 2''-phosphotransferase

Engineering

Engineering on EC 2.7.1.190 - aminoglycoside 2''-phosphotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F95M
no significantly different binding affinities as compared with the wild-type
F95Y
mutation shifts the nucleotide selectivity from a 2.5fold preference for ATP to a 1.5fold preference for GTP
S376N
-
a clinically identified naturally occuring S376N mutation of APH(2'')-Ia elevates resistance to N1-substituted aminoglycosides but eliminates modification of nonsubstituted compounds. Mutation of serine 376 to asparagine does not lead to substantial rearrangements in the aminoglycoside binding site. In fact, the addition of the larger asparagine residue in place of serine 376 creates an obstruction that prevents binding in the neamine binding pocket. As a result, any compounds that bind using the neamine rings are blocked from the antibiotic binding site of APH(2x02)-Ia. But the mutation remains compatible with one of the alternate binding modes of amikacin, which does not use this site to interact with the enzyme
Y92A
residue Y92 blocks access to the ATP-binding template. Mutant shows 8fold decrease in km value for ATP
F108L
-
site-directed mutagenesis, the point mutant and wild-type enzymes have the same structure
S214A
site-directed mutagenesis
Y237F
site-directed mutagenesis, the mutant removes the other hydrogen bond between the phosphate and the protein, and a greatly reduced electron density for the gamma-phosphate is observed
additional information