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acetyl-CoA + 2'-N-ethyl netilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
-
-
-
?
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
acetyl-CoA + amikacin
?
-
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
acetyl-CoA + aminoglycoside
CoA + 6'-N-acetylaminoglycoside
-
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
acetyl-CoA + arbekacin
CoA + N6'-acetylarbekacin
acetyl-CoA + butirosin
CoA + N6'-acetylbutirosin
-
-
-
-
?
acetyl-CoA + butirosin A
CoA + 6'-N-acetyl-butirosin A
acetyl-CoA + ciprofloxacin
CoA + N4'-acetylnorfloxacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
acetyl-CoA + fortimicin A
CoA + N6'-acetylfortimicin A
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
acetyl-CoA + gentamicin B
CoA + N6'-acetylgentamicin B
-
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
acetyl-CoA + gentamicin C1
CoA + N6'-acetylgentamicin C1
-
the AAC(6')-Ib protein is unable to efficiently modify gentamicin C1, 1.7% relative activity to sisomicin, however it is capable of modifying amikacin, 65.5% relative activity to sisomycin. The mutant enzyme AAC(6')-Ib L119S shows a 2.8fold increase in acetylation of gentamicin C1, but a 8.7fold reduction in the ability to modify amikacin. The AAC(6')-IIa protein modifies gentamicin C1 at 10.1% relative activity to sisomicin, however it shows low activity towards amikacin, 4.1% activity relative to sisomycin. The mutation AAC(6')-IIa S119L results in a 4.8fold reduction in the acetylation of gentamicin C1, but causes an 2fold increase in the ability to modify amikacin
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
acetyl-CoA + gentamicin C2
CoA + N6'-acetylgentgamicin C2
-
poor substrate, not gentamicin A and C1
-
-
?
acetyl-CoA + gentamycin
CoA + ?
-
-
-
?
acetyl-CoA + histone
CoA + ?
a mixture of calf histones enriched in H3 and H4
-
-
?
acetyl-CoA + human histone H3 peptide containing a C-terminal cysteine residue
CoA + ?
-
-
-
-
?
acetyl-CoA + hybrimycin A1
CoA + N6'-acetylhybrimycin A1
-
-
-
-
?
acetyl-CoA + hybrimycin A2
CoA + N6'-acetylhybrimycin A2
-
-
-
-
?
acetyl-CoA + hybrimycin A3
CoA + N6'-acetylhybrimycin A3
-
-
-
-
?
acetyl-CoA + hybrimycin B1
CoA + N6'-acetylhybrimycin B1
-
-
-
-
?
acetyl-CoA + hybrimycin B2
CoA + N6'-acetylhybrimycin B2
-
-
-
-
?
acetyl-CoA + hybrimycin B3
CoA + N6'-acetylhybrimycin B3
-
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
acetyl-CoA + isepamicin
CoA + N6'-acetylisepamicin
-
-
-
-
?
acetyl-CoA + istamycin-B
CoA + N6'-acetylistamycin-B
-
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
acetyl-CoA + kanamycin C
CoA + N6'-acetylkanamycin C
-
-
-
?
acetyl-CoA + lividomycin A
CoA + O6'-acetyllividomycin A
-
-
-
?
acetyl-CoA + micromomicin
CoA + N6'-acetylmicromomicin
acetyl-CoA + myelin basic protein
CoA + ?
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
acetyl-CoA + neamine
CoA + N6'-acetylneamine
acetyl-CoA + nebramycin factor 4
CoA + N6'-acetylnebramycin factor 4
-
no activity with factor 2
-
-
?
acetyl-CoA + nebramycin factor 6
CoA + N6'-acetylnebramycin factor 6
-
no activity with factor 2
-
-
?
acetyl-CoA + neomycin
CoA + 6'-N-acetylneomycin
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
acetyl-CoA + neomycin A
CoA + N6'-acetylneomycin A
-
-
-
-
?
acetyl-CoA + neomycin B
CoA + ?
-
-
-
?
acetyl-CoA + neomycin B
CoA + N6'-acetylneomycin B
acetyl-CoA + neomycin C
CoA + 6'-N-acetylneomycin C
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
acetyl-CoA + norfloxacin
CoA + N4'-acetylnorfloxacin
-
-
-
-
?
acetyl-CoA + paromomycin
CoA + O6'-acetylparomomycin
-
-
-
-
?
acetyl-CoA + poly-L-Lys
CoA + ?
-
-
-
?
acetyl-CoA + ribostamycin
CoA + 6'-N-acetylribostamycin
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
acetyl-CoA + ribostamycin
CoA + N6'acetylribostamycin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
acetyl-CoA + tobramicin
CoA + 6'-N-acetyltobramicin
acetyl-CoA + tobramicin
CoA + N6'-acetyltobramicin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
butyryl-CoA + tobramycin
CoA + N6'-butyryltobramycin
-
-
-
-
?
malonyl-CoA + sisomycin
CoA + ?
-
-
-
?
malonyl-CoA + tobramycin
CoA + N6'-malonyltobramycin
-
-
-
-
?
n-butyryl-CoA + sisomycin
CoA + ?
-
-
-
?
n-propionyl-CoA + sisomycin
CoA + ?
-
-
-
?
propionyl-CoA + kanamycin A
CoA + N6'-propionylkanamycin A
-
-
-
-
?
propionyl-CoA + tobramycin
CoA + N6'-propionyltobramycin
-
tobramycin exhibits a rapid, tobramycin-independent rate of hydrolysis that is linearly proportional to enzyme
-
-
?
additional information
?
-
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
-
-
-
?
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
-
-
-
-
?
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
aminoglycoside acetyltransferase eis acetylates and inactivates amikacin
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
the enzyme variant of enzyme type Ib has at position 119 a Ser instead of the Leu, conferring resistance to amikacin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
the enzyme variant of enzyme type Ib has at position 119 a Ser instead of the Leu, conferring resistance to amikacin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
the enzyme variant of enzyme type Ib has at position 119 a Ser instead of the Leu, conferring resistance to amikacin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
the enzyme variant of enzyme type Ib has at position 119 a Ser instead of the Leu, conferring resistance to amikacin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
the AAC(6')-Ib protein is unable to efficiently modify gentamicin C1, 1.7% relative activity to sisomicin, however it is capable of modifying amikacin, 65.5% relative activity to sisomycin. The mutant enzyme AAC(6')-Ib L119S shows a 2.8fold increase in acetylation of gentamicin C1, but a 8.7fold reduction in the ability to modify amikacin. The AAC(6')-IIa protein modifies gentamicin C1 at 10.1% relative activity to sisomicin, however it shows low activity towards amikacin, 4.1% activity relative to sisomycin. The mutation AAC(6')-IIa S119L results in a 4.8fold reduction in the acetylation of gentamicin C1, but causes an 2fold increase in the ability to modify amikacin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
gentamicin complex: C1 41%, C1a 26% and C2 33%. The aac(6')-Ib gene from strain BM2687 and the aac(6')-Ib gene from strain BM2656 show total identity with the exception of a C to T transition that results in a Ser to Leu substitution at position 83 of the deduced polypeptide. The enzyme encoded by aac(6')-Ib shows resistance to gentamicin but not to amikacin. The enzyme encoded by aac(6')-Ib shows resistance to amikacin but not to gentamicin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
gentamicin complex: C1 41%, C1a 26% and C2 33%. The aac(6')-Ib gene from strain BM2687 and the aac(6')-Ib gene from strain BM2656 show total identity with the exception of a C to T transition that results in a Ser to Leu substitution at position 83 of the deduced polypeptide. The enzyme encoded by aac(6')-Ib shows resistance to gentamicin but not to amikacin. The enzyme encoded by aac(6')-Ib shows resistance to amikacin but not to gentamicin
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
-
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + 6'-N-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + N6'-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + N6'-acetylarbekacin
-
-
-
?
acetyl-CoA + arbekacin
CoA + N6'-acetylarbekacin
-
-
-
?
acetyl-CoA + butirosin A
CoA + 6'-N-acetyl-butirosin A
-
-
-
?
acetyl-CoA + butirosin A
CoA + 6'-N-acetyl-butirosin A
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + 6'-N-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
-
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
-
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
-
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
poor substrate, AAC-(6')-II type
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
gentamicin complex: C1 41%, C1a 26% and C2 33%. The aac(6')-Ib gene from strain BM2687 and the aac(6')-Ib gene from strain BM2656 show total identity with the exception of a C to T transition that results in a Ser to Leu substitution at position 83 of the deduced polypeptide. The enzyme encoded by aac(6')-Ib shows resistance to gentamicin but not to amikacin. The enzyme encoded by aac(6')-Ib shows resistance to amikacin but not to gentamicin
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
gentamicin complex: C1 41%, C1a 26% and C2 33%. The aac(6')-Ib gene from strain BM2687 and the aac(6')-Ib gene from strain BM2656 show total identity with the exception of a C to T transition that results in a Ser to Leu substitution at position 83 of the deduced polypeptide. The enzyme encoded by aac(6')-Ib shows resistance to gentamicin but not to amikacin. The enzyme encoded by aac(6')-Ib shows resistance to amikacin but not to gentamicin
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + isepamicin
CoA + 6'-N-acetylisepamicin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
aminoglycoside acetyltransferase eis acetylates and inactivates kanamycin
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
the bifunctional antibiotic resistance enzyme from Serratia marcescens catalyzes adenylation and acetylation of aminoglycoside antibiotics. The structure assignment of the enzymic products indicated that acetylation takes place on the 6'-amine of kanamycin A and the adenylation on 3''- and 9-hydroxyl groups of streptomycin and spectinomycin, respectively. The adenyltransferase domain appears to be highly specific to spectinomycin and streptomycin, while the acetyltransferase domain shows a broad substrate profile. Initial velocity patterns indicate that both domains follow a sequential kinetic mechanism
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + micromomicin
CoA + N6'-acetylmicromomicin
-
-
-
-
?
acetyl-CoA + micromomicin
CoA + N6'-acetylmicromomicin
-
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
-
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
-
-
-
-
?
acetyl-CoA + neomycin
CoA + 6'-N-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + 6'-N-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + 6'-N-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + 6'-N-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin B
CoA + N6'-acetylneomycin B
-
-
-
?
acetyl-CoA + neomycin B
CoA + N6'-acetylneomycin B
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + 6'-N-acetylneomycin C
-
-
-
?
acetyl-CoA + neomycin C
CoA + 6'-N-acetylneomycin C
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
-
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + 6'-N-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
-
-
-
-
?
acetyl-CoA + ribostamycin
CoA + 6'-N-acetylribostamycin
-
-
-
?
acetyl-CoA + ribostamycin
CoA + 6'-N-acetylribostamycin
-
-
-
?
acetyl-CoA + ribostamycin
CoA + 6'-N-acetylribostamycin
-
-
-
?
acetyl-CoA + ribostamycin
CoA + 6'-N-acetylribostamycin
-
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
-
-
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + 6'-N-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
-
-
-
?
acetyl-CoA + tobramicin
CoA + 6'-N-acetyltobramicin
-
-
-
?
acetyl-CoA + tobramicin
CoA + 6'-N-acetyltobramicin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + 6'-N-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
-
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
no activity with aminoglycoside kinase APH(3')-IIIa, yeast homoserine dehydrogenase, spermine and serotonin
-
-
?
additional information
?
-
-
acetyl-CoA and propionyl-CoA are comparable substrates, but butyryl-CoA is not
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
the enzyme is an important microbial resistance determinant
-
-
?
additional information
?
-
-
use of aminoglycoside derivatives to study the mechanism of aminoglycoside 6'-N-acetyltransferase
-
-
?
additional information
?
-
-
Asp-88 acts as an active site base in the molecular mechanism of AAC(6')-Ie
-
-
?
additional information
?
-
-
a single amino acid, Leu119 in AAC(6')-Ib and S119 in AAC(6')-IIa, is largely responsible for determining the specificity of the AAC(6')-Ib and AAC(6')-IIa proteins. Changing this amino acid in either the AAC(6')-Ib or the AAC(6')-IIa protein results in a dramatic change in substrate specificity
-
-
?
additional information
?
-
-
the smallest antibiotic moiety required for recognition as a substrate by the acetylating enzyme is a 6-amino-6-deoxy-hexose glycosidically linked to a streptamine or deoxystreptamine ring
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
strong substrate inhibition with all 4,6-disubstituted aminoglycosides tested at concentrations required to determine kcat and Km values
-
-
-
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
acetylation reaction occurs through a direct mechanism rather than a ping-pong mechanism that includes a transient transfer of the acetyl group to a cysteine residue
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
no activity with fortimicin A. Bifunctional antibiotic-resistance enzyme. Both domains are acetyltransferases. The AAC(3)-Ib domain appears to be highly specific to fortimicin A and gentamicin as substrates, while the AAC(6')-b'?domain exhibits a broad substrate spectrum
-
-
?
additional information
?
-
lividomycin A is also a substrate, although with extremely small activity, thus the enzyme has acetylation activity with alternate amino groups in aminoglycosides
-
-
?
additional information
?
-
-
lividomycin A is also a substrate, although with extremely small activity, thus the enzyme has acetylation activity with alternate amino groups in aminoglycosides
-
-
?
additional information
?
-
no substrate: gentamicin
-
-
?
additional information
?
-
-
no substrate: gentamicin
-
-
?
additional information
?
-
no substrate: gentamicin
-
-
?
additional information
?
-
-
no substrate: gentamicin
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
C70 is directly involved in aminoglycoside binding
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
confer broad aminoglycoside resistance in strains in which the structural gene is expressed
-
-
?
additional information
?
-
-
AAC(6')-Iy catalyzes both acetyl-CoA-dependent self-alpha-N-acetylation and acetylation of eukaryotic histone proteins and the human histone H3 N-terminal peptide
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
isoform AAC(6')-Ian acetylates 4,6- and 4,5-disubstituted 2-deoxystreptamine aminoglycosides
-
-
?
additional information
?
-
-
isoform AAC(6')-Ian acetylates 4,6- and 4,5-disubstituted 2-deoxystreptamine aminoglycosides
-
-
?
additional information
?
-
enzyme acetylates all the aminoglycosides tested, except for apramycin, gentamicin, and lividomycin
-
-
-
additional information
?
-
isoform AAC(6')-Ian acetylates 4,6- and 4,5-disubstituted 2-deoxystreptamine aminoglycosides
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
aac(6')-Iz can restore aminoglycoside resistance to tobramycin, netilimicin and sisomicin (four- to eight-fold increase in the MICs) upon Escherichia coli
-
-
?
additional information
?
-
no substrates: apramycin, gentamicin, or lividomycin
-
-
?
additional information
?
-
no substrates: apramycin, gentamicin, or lividomycin
-
-
?
additional information
?
-
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
?
additional information
?
-
-
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
?
additional information
?
-
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
?
additional information
?
-
-
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
additional information
?
-
-
involved in resistance to antibiotics
-
-
?
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0.049
2'-N-ethyl netilmicin
S 0.5 value, Hill coefficient 1.39, pH 8.0, 37°C
0.0183
2'-N-ethylnetilmicin
S 0.5 value, Hill coefficient 2.28, pH 8.0, 37°C
0.0033 - 0.215
acetyl-CoA
0.014
butirosin
-
pH 6.0, 37°C
0.0173 - 0.0216
butirosin A
9.3
butyryl-CoA
-
reaction with tobramycin, wild-type enzyme
0.07
Ciprofloxacin
-
AAC(6')-Ib-cr variant
0.00038 - 0.582
dibekacin
0.0254 - 0.07
fortimicin A
0.00504 - 0.653
gentamicin
0.0223
gentamicin B
-
pH 6.0, 37°C
0.0082
gentamicin C
-
wild-type enzyme
0.022
gentamycin
K 0.5 value, Hill coefficient 3.14, pH 7.5, 25°C
0.0003 - 0.404
isepamicin
0.00202 - 0.346
kanamycin
0.00027 - 0.9
kanamycin B
0.04188
lividomycin A
pH 8.0, 30°C
0.0686
n-butyryl-CoA
pH 8.0, 30°C, cosubstrate: sisomycin
0.0161
n-propionyl-CoA
pH 8.0, 30°C, cosubstrate: sisomycin
0.00052 - 0.02
neomycin B
0.00531 - 0.25
neomycin C
0.067
Norfloxacin
-
AAC(6')-Ib-cr variant
0.324 - 0.771
paromomycin
0.038
poly-L-Lys
pH 7.5, 37°C
0.0195 - 0.27
propionyl-CoA
0.0062 - 0.306
ribostamycin
0.0029 - 0.216
tobramicin
0.00353 - 1.15
tobramycin
0.0033
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme L76A
0.0041
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme Y147F
0.0047
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme Y147A
0.0053
acetyl-CoA
-
AAC(6')-Ib-cr variant
0.0073
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme H74A
0.009
acetyl-CoA
-
reaction with AAC (6?)-Ib' domain
0.01
acetyl-CoA
-
reaction with tobramycin
0.0158
acetyl-CoA
-
wild-type enzyme
0.017
acetyl-CoA
-
reaction with tobramycin, mutant enzyme C109A
0.017
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.0187
acetyl-CoA
pH 8.0, 30°C, cosubstrate: sisomycin
0.021
acetyl-CoA
K 0.5 value, Hill coefficient 1.77, pH 7.5, 25°C
0.0235
acetyl-CoA
-
pH 6.0, 37°C
0.0235
acetyl-CoA
-
pH 6.0, 37°C, wild-type enzyme
0.035
acetyl-CoA
-
AAC(6')-Ib, wild type
0.038
acetyl-CoA
-
pH 7.5, 37°C,wild-type AAC(6')-Ie
0.0399
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.044
acetyl-CoA
-
pH 7.5
0.0453
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.0489
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme L76P
0.07
acetyl-CoA
-
reaction with tobramycin, mutant enzyme C109A/C70A
0.0736
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.108
acetyl-CoA
-
AAC(6')-Ib-cr variant
0.147
acetyl-CoA
isolated AAC(6') domain, pH 7.5, 25°C
0.154
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme E72A
0.215
acetyl-CoA
full length enzyme, pH 7.5, 25°C
0.00055
amikacin
full length enzyme, pH 7.5, 25°C
0.001
amikacin
-
reaction with AAC (6?)-Ib' domain
0.00434
amikacin
pH 8.0, 30°C
0.0114
amikacin
-
pH 6.0, 37°C, mutant enzyme L76A
0.0131
amikacin
-
pH 6.0, 37°C
0.0131
amikacin
-
pH 6.0, 37°C, wild-type enzyme
0.032
amikacin
pH not specified in the publication, temperature not specified in the publication
0.036
amikacin
-
pH 7.5, 37°C
0.0441
amikacin
S 0.5 value, Hill coefficient 1.55, pH 8.0, 37°C
0.05
amikacin
-
wild-type enzyme
0.0582
amikacin
-
pH 6.0, 37°C, mutant enzyme H74A
0.0693
amikacin
-
wild-type enzyme
0.075
amikacin
-
mutant enzyme C109A
0.086
amikacin
pH not specified in the publication, temperature not specified in the publication
0.0996
amikacin
S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C
0.127
amikacin
isolated AAC(6') domain, pH 7.5, 25°C
0.364
amikacin
-
pH 6.5, 37°C
0.38
amikacin
-
pH 6.0, 37°C, mutant enzyme E72A
0.571
amikacin
-
pH 5.5, 37°C
2.19
amikacin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.0059
arbekacin
S 0.5 value, Hill coefficient 2.5, pH 8.0, 37°C
0.0139
arbekacin
S 0.5 value, Hill coefficient 2.19, pH 8.0, 37°C
0.036
arbekacin
pH not specified in the publication, temperature not specified in the publication
0.399
arbekacin
pH not specified in the publication, temperature not specified in the publication
0.0173
butirosin A
S 0.5 value, Hill coefficient 1.77, pH 8.0, 37°C
0.0216
butirosin A
S 0.5 value, Hill coefficient 2.03, pH 8.0, 37°C
0.00038
dibekacin
pH 8.0, 30°C
0.003
dibekacin
-
reaction with AAC (6?)-Ib' domain
0.0098
dibekacin
S 0.5 value, Hill coefficient 1.42, pH 8.0, 37°C
0.024
dibekacin
pH not specified in the publication, temperature not specified in the publication
0.0259
dibekacin
S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C
0.03
dibekacin
-
wild-type enzyme
0.036
dibekacin
-
pH 6.0, 37°C
0.582
dibekacin
pH not specified in the publication, temperature not specified in the publication
0.0254
fortimicin A
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.0435
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.07
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.00504
gentamicin
full length enzyme, pH 7.5, 25°C
0.0083
gentamicin
-
reaction with AAC (6?)-Ib' domain
0.0087
gentamicin
S 0.5 value, Hill coefficient 1.84, pH 8.0, 37°C
0.0143
gentamicin
isolated AAC(6') domain, pH 7.5, 25°C
0.015
gentamicin
-
pH 7.5
0.0176
gentamicin
S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C
0.077
gentamicin
-
pH 7.5, 37°C
0.297
gentamicin
-
pH 6.5, 37°C
0.653
gentamicin
-
pH 5.5, 37°C
0.0003
isepamicin
-
reaction with AAC (6?)-Ib' domain
0.044
isepamicin
pH not specified in the publication, temperature not specified in the publication
0.104
isepamicin
S 0.5 value, Hill coefficient 1.45, pH 8.0, 37°C
0.111
isepamicin
S 0.5 value, Hill coefficient 1.48, pH 8.0, 37°C
0.404
isepamicin
pH not specified in the publication, temperature not specified in the publication
0.00202
kanamycin
full length enzyme, pH 7.5, 25°C
0.016
kanamycin
isolated AAC(6') domain, pH 7.5, 25°C
0.03
kanamycin
pH not specified in the publication, temperature not specified in the publication
0.322
kanamycin
pH not specified in the publication, temperature not specified in the publication
0.346
kanamycin
K 0.5 value, Hill coefficient 0.62, pH 7.5, 25°C
0.001
kanamycin A
-
pH 7.5
0.001
kanamycin A
-
pH 6.0
0.001
kanamycin A
-
reaction with AAC (6?)-Ib' domain
0.005
kanamycin A
-
pH 6.0
0.006
kanamycin A
-
pH 7.5
0.0074
kanamycin A
pH 8.0, 30°C
0.0114
kanamycin A
-
wild-type enzyme
0.012
kanamycin A
-
pH 7.5
0.0144
kanamycin A
-
pH 6.0, 37°C, mutant enzyme H74A
0.0199
kanamycin A
-
pH 6.0, 37°C
0.0199
kanamycin A
-
pH 6.0, 37°C, wild-type enzyme
0.0257
kanamycin A
-
pH 6.0, 37°C, mutant enzyme L76A
0.031
kanamycin A
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.079
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.0902
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.102
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.105
kanamycin A
-
wild-type enzyme
0.11
kanamycin A
-
pH 6.0, 37°C, mutant enzyme Y147A
0.34
kanamycin A
-
pH 6.0, 37°C, mutant enzyme Y147F
0.771
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
3.49
kanamycin A
-
pH 6.0, 37°C, mutant enzyme E72A
0.00027
kanamycin B
-
AAC(6')-Ib, wild type
0.0067
kanamycin B
-
AAC(6')-Ib-cr variant
0.012
kanamycin B
S 0.5 value, Hill coefficient 2.30, pH 8.0, 37°C
0.017
kanamycin B
-
mutant enzyme C109A
0.0189
kanamycin B
-
pH 6.0, 37°C
0.029
kanamycin B
S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C
0.079
kanamycin B
-
wild-type enzyme
0.9
kanamycin B
-
mutant enzyme C109A/C70A
0.58
malonyl-CoA
pH 8.0, 30°C, cosubstrate: sisomycin
0.82
malonyl-CoA
-
reaction with tobramycin, wild-type enzyme
0.0058
neamine
-
pH 6.0, 37°C, wild-type enzyme
0.00582
neamine
-
pH 6.0, 37°C
0.0224
neamine
-
pH 6.0, 37°C, mutant enzyme L76A
0.0432
neamine
-
pH 6.0, 37°C, mutant enzyme H74A
0.0682
neamine
-
pH 6.0, 37°C, mutant enzyme L76P
0.078
neamine
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.15
neamine
-
pH 6.0, 37°C, mutant enzyme Y147F
0.169
neamine
-
pH 6.0, 37°C, mutant enzyme Y147A
0.229
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.326
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.443
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.482
neamine
-
pH 6.0, 37°C, mutant enzyme E72A
0.509
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.0012
neomycin
-
reaction with AAC (6?)-Ib' domain
0.0039
neomycin
-
wild-type enzyme
0.0053
neomycin
-
pH 6.0, 37°C, wild-type enzyme
0.01
neomycin
pH not specified in the publication, temperature not specified in the publication
0.0182
neomycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.019
neomycin
-
pH 6.0, 37°C, mutant enzyme L76A
0.023
neomycin
full length enzyme, pH 7.5, 25°C
0.029
neomycin
-
pH 6.0, 37°C, mutant enzyme E72A
0.0321
neomycin
isolated AAC(6') domain, pH 7.5, 25°C
0.0386
neomycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.0553
neomycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.0573
neomycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.47
neomycin
pH not specified in the publication, temperature not specified in the publication
0.00052
neomycin B
pH 8.0, 30°C
0.02
neomycin B
-
AAC(6')-Ib, wild type
0.00531
neomycin C
-
pH 6.0, 37°C
0.0074
neomycin C
S 0.5 value, Hill coefficient 1.43, pH 8.0, 37°C
0.0079
neomycin C
S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C
0.014
neomycin C
-
wild-type enzyme
0.25
neomycin C
-
mutant enzyme C109A/C70A
0.001
netilmicin
-
reaction with AAC (6?)-Ib' domain
0.00177
netilmicin
full length enzyme, pH 7.5, 25°C
0.00387
netilmicin
isolated AAC(6') domain, pH 7.5, 25°C
0.006
netilmicin
-
mutant enzyme C109A
0.00638
netilmicin
-
pH 6.0, 37°C
0.008
netilmicin
-
wild-type enzyme
0.023
netilmicin
pH not specified in the publication, temperature not specified in the publication
0.036
netilmicin
-
pH 7.5
0.07
netilmicin
pH not specified in the publication, temperature not specified in the publication
0.259
netilmicin
-
pH 7.5, 37°C
0.46
netilmicin
-
mutant enzyme C109A/C70A
2.44
netilmicin
-
pH 6.5, 37°C
0.324
paromomycin
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.771
paromomycin
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.0195
propionyl-CoA
-
pH 6.0, 37°C
0.27
propionyl-CoA
-
reaction with tobramycin, wild-type enzyme
0.0062
ribostamycin
S 0.5 value, Hill coefficient 1.92, pH 8.0, 37°C
0.00908
ribostamycin
-
pH 6.0, 37°C
0.0091
ribostamycin
-
pH 6.0, 37°C, wild-type enzyme
0.0118
ribostamycin
S 0.5 value, Hill coefficient 1.96, pH 8.0, 37°C
0.016
ribostamycin
full length enzyme, pH 7.5, 25°C
0.0214
ribostamycin
-
pH 6.0, 37°C, mutant enzyme L76A
0.0381
ribostamycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.05
ribostamycin
-
wild-type enzyme
0.0693
ribostamycin
isolated AAC(6') domain, pH 7.5, 25°C
0.107
ribostamycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.109
ribostamycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.301
ribostamycin
-
pH 6.0, 37°C, mutant enzyme E72A
0.306
ribostamycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.0022
sisomicin
full length enzyme, pH 7.5, 25°C
0.00324
sisomicin
pH 8.0, 30°C
0.004
sisomicin
pH not specified in the publication, temperature not specified in the publication
0.0049
sisomicin
isolated AAC(6') domain, pH 7.5, 25°C
0.0105
sisomicin
S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C
0.0117
sisomicin
-
pH 6.0, 37°C
0.012
sisomicin
-
wild-type enzyme
0.012
sisomicin
pH not specified in the publication, temperature not specified in the publication
0.0168
sisomicin
S 0.5 value, Hill coefficient 2.04, pH 8.0, 37°C
0.038
sisomicin
K 0.5 value, Hill coefficient 4.39, pH 7.5, 25°C
0.0029
tobramicin
S 0.5 value, Hill coefficient 2.12, pH 8.0, 37°C
0.022
tobramicin
S 0.5 value, Hill coefficient 1.21, pH 8.0, 37°C
0.216
tobramicin
-
pH 5.5, 37°C
0.00353
tobramycin
pH 8.0, 30°C
0.0037
tobramycin
-
wild-type enzyme
0.0079
tobramycin
full length enzyme, pH 7.5, 25°C
0.0148
tobramycin
isolated AAC(6') domain, pH 7.5, 25°C
0.016
tobramycin
pH not specified in the publication, temperature not specified in the publication
0.022
tobramycin
-
pH 6.0, 37°C
0.022
tobramycin
-
pH 6.0, 37°C, wild-type enzyme
0.026
tobramycin
-
pH 7.5, 37°C
0.026
tobramycin
-
mutant enzyme C109A
0.028
tobramycin
pH not specified in the publication, temperature not specified in the publication
0.028
tobramycin
K 0.5 value, Hill coefficient 2.3, pH 7.5, 25°C
0.0369
tobramycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.066
tobramycin
-
wild-type enzyme
0.077
tobramycin
-
pH 6.5, 37°C
0.136
tobramycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.146
tobramycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.147
tobramycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.54
tobramycin
-
mutant enzyme C109A/C70A
0.62
tobramycin
-
pH 6.0, 37°C, mutant enzyme L76A
1.15
tobramycin
-
pH 6.0, 37°C, mutant enzyme E72A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.098
2'-N-ethyl netilmicin
pH 8.0, 37°C
0.097
2'-N-ethylnetilmicin
pH 8.0, 37°C
0.466
butirosin
-
pH 6.0, 37°C
0.107 - 0.113
butirosin A
1.03
Ciprofloxacin
-
AAC(6')-Ib-cr variant
0.0002 - 0.45
fortimicin A
0.388
gentamicin B
-
pH 6.0, 37°C
1.01
gentamicin C
-
wild-type enzyme
1.17
gentamycin
pH 7.5, 25°C
3.08
neomycin B
-
AAC(6')-Ib, wild type
1.08
Norfloxacin
-
AAC(6')-Ib-cr variant
0.0004 - 0.059
paromomycin
0.0019
poly-L-Lys
pH 7.5, 37°C
0.317
propionyl-CoA
-
pH 6.0, 37°C
0.01
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme Y147A
0.035
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.06
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme L76P
0.07
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme Y147F
0.11
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.17
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.173
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme W164A
0.18
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme H74A
0.23
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme L76A
0.4
acetyl-CoA
-
pH 6.0, 37°C, wild-type enzyme
0.403
acetyl-CoA
-
pH 6.0, 37°C
0.403
acetyl-CoA
-
pH 6.0, 37°C, wild-type enzyme
0.99
acetyl-CoA
-
pH 6.0, 37°C, mutant enzyme E72A
1
acetyl-CoA
-
reaction with AAC (6')-Ib' domain
1.03
acetyl-CoA
-
AAC(6')-Ib-cr variant
1.2
acetyl-CoA
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
1.3
acetyl-CoA
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
1.51
acetyl-CoA
pH 7.5, 25°C
1.61
acetyl-CoA
-
wild-type enzyme
1.62
acetyl-CoA
full length enzyme, pH 7.5, 25°C
2.32
acetyl-CoA
-
AAC(6')-Ib, wild type
5.23
acetyl-CoA
-
AAC(6')-Ib-cr variant
12.1
acetyl-CoA
isolated AAC(6') domain, pH 7.5, 25°C
0.003
amikacin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.03
amikacin
-
pH 6.0, 37°C, mutant enzyme L76A
0.04
amikacin
-
pH 6.0, 37°C, mutant enzyme H74A
0.05
amikacin
-
pH 6.0, 37°C, mutant enzyme E72A
0.106
amikacin
-
pH 6.0, 37°C
0.11
amikacin
-
pH 6.0, 37°C, wild-type enzyme
0.11
amikacin
pH not specified in the publication, temperature not specified in the publication
0.2
amikacin
pH not specified in the publication, temperature not specified in the publication
0.29
amikacin
-
wild-type enzyme
0.328
amikacin
pH 8.0, 37°C
0.496
amikacin
pH 8.0, 37°C
2.92
amikacin
full length enzyme, pH 7.5, 25°C
3.5
amikacin
-
reaction with AAC (6')-Ib' domain
7.09
amikacin
isolated AAC(6') domain, pH 7.5, 25°C
0.021
arbekacin
pH 8.0, 37°C
0.077
arbekacin
pH 8.0, 37°C
0.57
arbekacin
pH not specified in the publication, temperature not specified in the publication
17
arbekacin
pH not specified in the publication, temperature not specified in the publication
0.107
butirosin A
pH 8.0, 37°C
0.113
butirosin A
pH 8.0, 37°C
0.04
dibekacin
pH 8.0, 37°C
0.127
dibekacin
pH 8.0, 37°C
0.25
dibekacin
pH not specified in the publication, temperature not specified in the publication
0.632
dibekacin
-
pH 6.0, 37°C
1.3
dibekacin
-
reaction with AAC (6')-Ib' domain
85
dibekacin
pH not specified in the publication, temperature not specified in the publication
0.0002
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.0008
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.006
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.28
fortimicin A
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.45
fortimicin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.016
gentamicin
pH 8.0, 37°C
0.055
gentamicin
pH 8.0, 37°C
1.11
gentamicin
full length enzyme, pH 7.5, 25°C
2
gentamicin
-
reaction with AAC (6')-Ib' domain
3.33
gentamicin
isolated AAC(6') domain, pH 7.5, 25°C
0.05
isepamicin
pH not specified in the publication, temperature not specified in the publication
0.62
isepamicin
pH 8.0, 37°C
0.779
isepamicin
pH 8.0, 37°C
2.4
isepamicin
-
reaction with AAC (6')-Ib' domain
25
isepamicin
pH not specified in the publication, temperature not specified in the publication
0.04
kanamycin
pH not specified in the publication, temperature not specified in the publication
0.207
kanamycin
pH 7.5, 25°C
2.13
kanamycin
isolated AAC(6') domain, pH 7.5, 25°C
3.81
kanamycin
full length enzyme, pH 7.5, 25°C
10
kanamycin
pH not specified in the publication, temperature not specified in the publication
0.01
kanamycin A
-
pH 6.0, 37°C, mutant enzyme Y147A
0.03
kanamycin A
-
pH 6.0, 37°C, mutant enzyme Y147F
0.033
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.038
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.05
kanamycin A
-
pH 6.0, 37°C, mutant enzyme H74A
0.08
kanamycin A
-
pH 6.0, 37°C, mutant enzyme W164A
0.19
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.27
kanamycin A
-
pH 6.0, 37°C, mutant enzyme L76A
0.55
kanamycin A
-
pH 6.0, 37°C, mutant enzyme E72A
0.816
kanamycin A
-
pH 6.0, 37°C
0.816
kanamycin A
-
pH 6.0, 37°C, wild-type enzyme
0.82
kanamycin A
-
pH 6.0, 37°C, wild-type enzyme
1.1
kanamycin A
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
1.68
kanamycin A
-
wild-type enzyme
1.7
kanamycin A
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
2.4
kanamycin A
-
reaction with AAC (6')-Ib' domain
0.06
kanamycin B
pH 8.0, 37°C
0.181
kanamycin B
pH 8.0, 37°C
1.08
kanamycin B
-
pH 6.0, 37°C
2.27
kanamycin B
-
AAC(6')-Ib, wild type
5.25
kanamycin B
-
AAC(6')-Ib-cr variant
0.002
neamine
-
pH 6.0, 37°C, mutant enzyme L76P
0.004
neamine
-
pH 6.0, 37°C, mutant enzyme Y147A
0.028
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99N
0.029
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99A
0.048
neamine
-
pH 6.0, 37°C, mutant enzyme W164A
0.05
neamine
-
pH 6.0, 37°C, mutant enzyme Y147F
0.066
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.15
neamine
-
pH 6.0, 37°C, mutant enzyme H74A
0.38
neamine
-
pH 6.0, 37°C, mutant enzyme L76A
0.419
neamine
-
pH 6.0, 37°C
0.419
neamine
-
pH 6.0, 37°C, wild-type enzyme
0.42
neamine
-
pH 6.0, 37°C, wild-type enzyme
0.43
neamine
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.44
neamine
-
pH 6.0, 37°C, mutant enzyme E72A
1.3
neamine
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.001
neomycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.04
neomycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.07
neomycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.16
neomycin
-
pH 6.0, 37°C, mutant enzyme L76A
0.19
neomycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.2
neomycin
-
pH 6.0, 37°C, wild-type enzyme
0.3
neomycin
-
wild-type enzyme
0.32
neomycin
pH not specified in the publication, temperature not specified in the publication
1.1
neomycin
-
pH 6.0, 37°C, mutant enzyme E72A
6
neomycin
-
reaction with AAC (6')-Ib' domain
7.8
neomycin
pH not specified in the publication, temperature not specified in the publication
9.06
neomycin
full length enzyme, pH 7.5, 25°C
11.1
neomycin
isolated AAC(6') domain, pH 7.5, 25°C
0.057
neomycin C
pH 8.0, 37°C
0.06
neomycin C
pH 8.0, 37°C
0.135
neomycin C
-
pH 6.0, 37°C, mutant enzyme W164A
0.205
neomycin C
-
pH 6.0, 37°C
0.205
neomycin C
-
pH 6.0, 37°C, wild-type enzyme
0.2
netilmicin
-
pH 7.5
0.3
netilmicin
pH not specified in the publication, temperature not specified in the publication
0.512
netilmicin
-
pH 6.0, 37°C
0.73
netilmicin
pH not specified in the publication, temperature not specified in the publication
1.3
netilmicin
-
reaction with AAC (6')-Ib' domain
1.91
netilmicin
full length enzyme, pH 7.5, 25°C
3.21
netilmicin
isolated AAC(6') domain, pH 7.5, 25°C
0.0004
paromomycin
-
pH 7.5, 37°C, mutant AAC(6')-Ie D99E
0.026
paromomycin
-
pH 7.5, 37°C, mutant AAC(6')-Ie Y96F
0.059
paromomycin
-
pH 7.5, 37°C, wild-type AAC(6')-Ie
0.01
ribostamycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.02
ribostamycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.04
ribostamycin
pH 8.0, 37°C
0.046
ribostamycin
-
pH 6.0, 37°C, mutant enzyme W164A
0.072
ribostamycin
pH 8.0, 37°C
0.12
ribostamycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.15
ribostamycin
-
pH 6.0, 37°C, mutant enzyme L76A
0.23
ribostamycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.338
ribostamycin
-
pH 6.0, 37°C
0.338
ribostamycin
-
pH 6.0, 37°C, wild-type enzyme
0.34
ribostamycin
-
pH 6.0, 37°C, wild-type enzyme
0.35
ribostamycin
-
pH 6.0, 37°C, mutant enzyme E72A
3.88
ribostamycin
full length enzyme, pH 7.5, 25°C
5.7
ribostamycin
isolated AAC(6') domain, pH 7.5, 25°C
0.051
sisomicin
pH 8.0, 37°C
0.13
sisomicin
pH 8.0, 37°C
0.16
sisomicin
pH not specified in the publication, temperature not specified in the publication
0.37
sisomicin
-
pH 6.0, 37°C
0.49
sisomicin
pH not specified in the publication, temperature not specified in the publication
2.42
sisomicin
pH 7.5, 25°C
2.93
sisomicin
full length enzyme, pH 7.5, 25°C
5.35
sisomicin
isolated AAC(6') domain, pH 7.5, 25°C
0.022
tobramicin
pH 8.0, 37°C
0.085
tobramicin
pH 8.0, 37°C
0.004
tobramycin
-
pH 6.0, 37°C, mutant enzyme Y147A
0.01
tobramycin
-
pH 6.0, 37°C, mutant enzyme L76P
0.08
tobramycin
pH not specified in the publication, temperature not specified in the publication
0.1
tobramycin
-
pH 6.0, 37°C, mutant enzyme Y147F
0.3
tobramycin
-
pH 6.0, 37°C, mutant enzyme H74A
0.67
tobramycin
pH not specified in the publication, temperature not specified in the publication
0.8
tobramycin
-
wild-type enzyme
0.89
tobramycin
-
pH 6.0, 37°C, mutant enzyme L76A
1.1
tobramycin
-
pH 6.0, 37°C, wild-type enzyme
1.1
tobramycin
-
pH 6.0, 37°C, mutant enzyme E72A
1.11
tobramycin
-
pH 6.0, 37°C
1.2
tobramycin
pH 7.5, 25°C
3.73
tobramycin
isolated AAC(6') domain, pH 7.5, 25°C
3.84
tobramycin
full length enzyme, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2
2'-N-ethyl netilmicin
kcat/S 0.5 value, Hill coefficient 1.39, pH 8.0, 37°C
5.3
2'-N-ethylnetilmicin
kcat/S 0.5 valuevalue, Hill coefficient 2.28, pH 8.0, 37°C
52
gentamycin
K 0.5 value, Hill coefficient 3.14, pH 7.5, 25°C
8.4
acetyl-CoA
full length enzyme, pH 7.5, 25°C
69
acetyl-CoA
K 0.5 value, Hill coefficient 1.77, pH 7.5, 25°C
82
acetyl-CoA
isolated AAC(6') domain, pH 7.5, 25°C
2
amikacin
pH not specified in the publication, temperature not specified in the publication
4
amikacin
pH not specified in the publication, temperature not specified in the publication
4.98
amikacin
kcat/S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C
7.44
amikacin
kcat/S 0.5 value, Hill coefficient 1.55, pH 8.0, 37°C
62.4
amikacin
isolated AAC(6') domain, pH 7.5, 25°C
5250
amikacin
full length enzyme, pH 7.5, 25°C
3.56
arbekacin
kcat/S 0.5 value, Hill coefficient 2.5, pH 8.0, 37°C
5.54
arbekacin
kcat/S 0.5 valuevalue, Hill coefficient 2.19, pH 8.0, 37°C
16
arbekacin
pH not specified in the publication, temperature not specified in the publication
48
arbekacin
pH not specified in the publication, temperature not specified in the publication
5.23
butirosin A
kcat/S 0.5 value, Hill coefficient 2.03, pH 8.0, 37°C
6.18
butirosin A
kcat/S 0.5 valuevalue, Hill coefficient 1.77, pH 8.0, 37°C
4.08
dibekacin
kcat/S 0.5 value, Hill coefficient 1.42, pH 8.0, 37°C
4.9
dibekacin
kcat/S 0.5 valuevalue, Hill coefficient 1.26, pH 8.0, 37°C
10
dibekacin
pH not specified in the publication, temperature not specified in the publication
150
dibekacin
pH not specified in the publication, temperature not specified in the publication
1.84
gentamicin
kcat/S 0.5 value, Hill coefficient 1.84, pH 8.0, 37°C
3.13
gentamicin
kcat/S 0.5 valuevalue, Hill coefficient 2.05, pH 8.0, 37°C
220
gentamicin
full length enzyme, pH 7.5, 25°C
234
gentamicin
isolated AAC(6') domain, pH 7.5, 25°C
1
isepamicin
pH not specified in the publication, temperature not specified in the publication
5.59
isepamicin
kcat/S 0.5 value, Hill coefficient 1.48, pH 8.0, 37°C
7.49
isepamicin
kcat/S 0.5 valuevalue, Hill coefficient 1.45, pH 8.0, 37°C
61
isepamicin
pH not specified in the publication, temperature not specified in the publication
0.6
kanamycin
K 0.5 value, Hill coefficient 0.62, pH 7.5, 25°C
1
kanamycin
pH not specified in the publication, temperature not specified in the publication
32
kanamycin
pH not specified in the publication, temperature not specified in the publication
133
kanamycin
isolated AAC(6') domain, pH 7.5, 25°C
189
kanamycin
full length enzyme, pH 7.5, 25°C
5
kanamycin B
kcat/S 0.5 value, Hill coefficient 2.30, pH 8.0, 37°C
6.24
kanamycin B
kcat/S 0.5 valuevalue, Hill coefficient 1.93, pH 8.0, 37°C
25
neomycin
pH not specified in the publication, temperature not specified in the publication
34
neomycin
pH not specified in the publication, temperature not specified in the publication
346
neomycin
isolated AAC(6') domain, pH 7.5, 25°C
394
neomycin
full length enzyme, pH 7.5, 25°C
7.59
neomycin C
kcat/S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C
7.7
neomycin C
kcat/S 0.5 value, Hill coefficient 1.43, pH 8.0, 37°C
4
netilmicin
pH not specified in the publication, temperature not specified in the publication
32
netilmicin
pH not specified in the publication, temperature not specified in the publication
829
netilmicin
isolated AAC(6') domain, pH 7.5, 25°C
1080
netilmicin
full length enzyme, pH 7.5, 25°C
6.1
ribostamycin
kcat/S 0.5 value, Hill coefficient 1.96, pH 8.0, 37°C
7.1
ribostamycin
kcat/S 0.5 value, Hill coefficient 1.92, pH 8.0, 37°C
82.2
ribostamycin
isolated AAC(6') domain, pH 7.5, 25°C
243
ribostamycin
full length enzyme, pH 7.5, 25°C
4.86
sisomicin
kcat/S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C
7.74
sisomicin
kcat/S 0.5 valuevalue, Hill coefficient 2.04, pH 8.0, 37°C
38
sisomicin
pH not specified in the publication, temperature not specified in the publication
41
sisomicin
pH not specified in the publication, temperature not specified in the publication
64
sisomicin
K 0.5 value, Hill coefficient 4.39, pH 7.5, 25°C
1090
sisomicin
isolated AAC(6') domain, pH 7.5, 25°C
1330
sisomicin
full length enzyme, pH 7.5, 25°C
3.86
tobramicin
kcat/S 0.5 valuevalue, Hill coefficient 1.21, pH 8.0, 37°C
7.59
tobramicin
kcat/S 0.5 value, Hill coefficient 2.12, pH 8.0, 37°C
6
tobramycin
pH not specified in the publication, temperature not specified in the publication
24
tobramycin
pH not specified in the publication, temperature not specified in the publication
43
tobramycin
K 0.5 value, Hill coefficient 2.3, pH 7.5, 25°C
252
tobramycin
isolated AAC(6') domain, pH 7.5, 25°C
485
tobramycin
full length enzyme, pH 7.5, 25°C
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Benveniste, R.; Davies, J.
Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria
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2276-2280
1973
Streptomyces kanamyceticus
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brenda
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24
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170
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New mobile gene cassettes containing an aminoglycoside resistance gene, aacA7, and a chloramphenicol resistance gene, catB3, in an integron in pBWH301
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brenda
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47
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Escherichia coli
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Salmonella enterica serovar typhimurium bla(PER-1)-carrying plasmid pSTI1 encodes an extended-spectrum aminoglycoside 6'-N-acetyltransferase of type Ib
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47
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49
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Kinetic mechanism of the GCN5-related chromosomal aminoglycoside acetyltransferase AAC(6')-Ii from Enterococcus faecium: evidence of dimer subunit cooperativity
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42
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43
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2004
Streptomyces albulus (Q764C8), Streptomyces albulus, Streptomyces albulus IFO14147 (Q764C8), Streptomyces albulus IFO14147
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Boehr, D.D.; Jenkins, S.I.; Wright, G.D.
The molecular basis of the expansive substrate specificity of the antibiotic resistance enzyme aminoglycoside acetyltransferase-6'-aminoglycoside phosphotransferase-2". The role of Asp-99 as an active site base important for acetyl transfer
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Enterococcus sp.
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Burk, D.L.; Xiong, B.; Breitbach, C.; Berghuis, A.M.
Structures of aminoglycoside acetyltransferase AAC(6)-Ii in a novel crystal form: structural and normal-mode analyses
Acta Crystallogr. Sect. D
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1273-1279
2005
Enterococcus faecium
brenda
Gao, F.; Yan, X.; Baettig, O.M.; Berghuis, A.M.; Auclair, K.
Regio- and chemoselective 6-N-derivatization of amino-glycosides: bi-substrate inhibitors as probes to study amino-glycoside 6-N-acetyltransferase
Angew. Chem. Int. Ed. Engl.
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2005
Enterococcus faecium
brenda
Kim, C.; Hesek, D.; Zajicek, J.; Vakulenko, S.B.; Mobashery, S.
Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3)-Ii/AAC(6)-IId from Serratia marcescens
Biochemistry
45
8368-8377
2006
Serratia marcescens
brenda
Kim, C.; Villegas-Estrada, A.; Hesek, D.; Mobashery, S.
Mechanistic characterization of the bifunctional aminoglycoside-modifying enzyme AAC(3)-Ib/AAC(6)-Ib from Pseudomonas aeruginosa
Biochemistry
46
5270-5282
2007
Pseudomonas aeruginosa
brenda
Yan, X.; Gao, F.; Yotphan, S.; Bakirtzian, P.; Auclair, K.
The use of aminoglycoside derivatives to study the mechanism of aminoglycoside 6-N-acetyltransferase and the role of 6-NH2 in antibacterial activity
Bioorg. Med. Chem.
15
2944-2951
2007
Enterococcus faecium
brenda
Filipova, M.; Bujdakova, H.; Drahovska, H.; Liskova, A.; Hanzen, J.
Occurrence of aminoglycoside-modifying-enzyme genes aac(6)-aph(2"), aph(3), ant(4) and ant(6) in clinical isolates of Enterococcus faecalis resistant to high-level of gentamicin and amikacin
Folia Microbiol. (Praha)
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57-61
2006
Enterococcus faecalis
brenda
Gao, F.; Yan, X.; Shakya, T.; Baettig, O.M.; Ait-Mohand-Brunet, S.; Berghuis, A.M.; Wright, G.D.; Auclair, K.
Synthesis and structure-activity relationships of truncated bisubstrate inhibitors of aminoglycoside 6-N-acetyltransferases
J. Med. Chem.
49
5273-5281
2006
Enterococcus faecium
brenda
Chu, X.; Wu, L.; Liu, X.; Li, N.; Li, D.
Detection of broad-spectrum aminoglycoside antibiotics through fluorescence-labeling aminoglycoside acetyltransferase(6)-Ii
Anal. Biochem.
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2008
Enterococcus faecium
brenda
Magalhaes, M.L.; Vetting, M.W.; Gao, F.; Freiburger, L.; Auclair, K.; Blanchard, J.S.
Kinetic and structural analysis of bisubstrate inhibition of the Salmonella enterica aminoglycoside 6-N-acetyltransferase
Biochemistry
47
579-584
2008
Salmonella enterica
brenda
Kitao, T.; Miyoshi-Akiyama, T.; Kirikae, T.
AAC(6)-Iaf, a novel aminoglycoside 6-N-acetyltransferase from multidrug-resistant Pseudomonas aeruginosa clinical isolates
Antimicrob. Agents Chemother.
53
2327-2334
2009
Pseudomonas aeruginosa (C4TGI5), Pseudomonas aeruginosa
brenda
Vetting, M.W.; Park, C.H.; Hegde, S.S.; Jacoby, G.A.; Hooper, D.C.; Blanchard, J.S.
Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6)-Ib and its bifunctional, fluoroquinolone-active AAC(6)-Ib-cr variant
Biochemistry
47
9825-9835
2008
Escherichia coli
brenda
Gao, F.; Yan, X.; Zahr, O.; Larsen, A.; Vong, K.; Auclair, K.
Synthesis and use of sulfonamide-, sulfoxide-, or sulfone-containing aminoglycoside-CoA bisubstrates as mechanistic probes for aminoglycoside N-6-acetyltransferase
Bioorg. Med. Chem. Lett.
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5518-5522
2008
Enterococcus faecium
brenda
Gao, F.; Yan, X.; Auclair, K.
Synthesis of a phosphonate-linked aminoglycoside-coenzyme a bisubstrate and use in mechanistic studies of an enzyme involved in aminoglycoside resistance
Chemistry
15
2064-2070
2009
Enterococcus faecium
brenda
Zaunbrecher, M.A.; Sikes, R.D.; Metchock, B.; Shinnick, T.M.; Posey, J.E.
Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis
Proc. Natl. Acad. Sci. USA
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20004-20009
2009
Mycobacterium tuberculosis
brenda
Caldwell, S.J.; Berghuis, A.M.
Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside (6) acetyltransferase-ie/aminoglycoside (2) phosphotransferase-ia reveals a rigid solution structure
Antimicrob. Agents Chemother.
56
1899-1906
2012
Staphylococcus aureus
brenda
Kim, Y.T.; Jang, J.H.; Kim, H.C.; Kim, H.; Lee, K.R.; Park, K.S.; Lee, H.J.; Kim, Y.J.
Identification of strain harboring both aac(6)-Ib and aac(6)-Ib-cr variant simultaneously in Escherichia coli and Klebsiella pneumoniae
BMB Rep.
44
262-266
2011
Escherichia coli, Klebsiella pneumoniae
brenda
Chowdhury, G.; Pazhani, G.P.; Nair, G.B.; Ghosh, A.; Ramamurthy, T.
Transferable plasmid-mediated quinolone resistance in association with extended-spectrum beta-lactamases and fluoroquinolone-acetylating aminoglycoside-6-N-acetyltransferase in clinical isolates of Vibrio fluvialis
Int. J. Antimicrob. Agents
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169-173
2011
Vibrio fluvialis
brenda
Smith, C.; Toth, M.; Bhattacharya, M.; Frase, H.; Vakulenko, S.
Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6)-Ie-APH(2")-Ia
Acta Crystallogr. Sect. D
70
1561-1571
2014
Staphylococcus warneri (Q7ATH7)
brenda
Tada, T.; Miyoshi-Akiyama, T.; Shimada, K.; Shimojima, M.; Kirikae, T.
Novel 6'-N-aminoglycoside acetyltransferase AAC(6')-Iaj from a clinical isolate of Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
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96-100
2013
Pseudomonas aeruginosa (K0IV17), Pseudomonas aeruginosa, Pseudomonas aeruginosa NCGM1588 (K0IV17), Pseudomonas aeruginosa NCGM1588
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Lin, D.L.; Tran, T.; Alam, J.Y.; Herron, S.R.; Ramirez, M.S.; Tolmasky, M.E.
Inhibition of aminoglycoside 6-N-acetyltransferase type Ib by zinc: reversal of amikacin resistance in Acinetobacter baumannii and Escherichia coli by a zinc ionophore
Antimicrob. Agents Chemother.
58
4238-4241
2014
Acinetobacter baumannii, Acinetobacter baumannii 155
brenda
Tada, T.; Miyoshi-Akiyama, T.; Dahal, R.K.; Mishra, S.K.; Shimada, K.; Ohara, H.; Kirikae, T.; Pokhrel, B.M.
Identification of a novel 6-N-aminoglycoside acetyltransferase, AAC(6)-Iak, from a multidrug-resistant clinical isolate of Stenotrophomonas maltophilia
Antimicrob. Agents Chemother.
58
6324-6327
2014
Stenotrophomonas maltophilia (V5XKM9), Stenotrophomonas maltophilia IOMTU250 (V5XKM9)
brenda
Li, Y.; Green, K.D.; Johnson, B.R.; Garneau-Tsodikova, S.
Inhibition of aminoglycoside acetyltransferase resistance enzymes by metal salts
Antimicrob. Agents Chemother.
59
4148-4156
2015
Pseudomonas aeruginosa (Q8RPU6), Staphylococcus aureus
brenda
Chiem, K.; Fuentes, B.A.; Lin, D.L.; Tran, T.; Jackson, A.; Ramirez, M.S.; Tolmasky, M.E.
Inhibition of aminoglycoside 6-N-acetyltransferase type Ib-mediated amikacin resistance in Klebsiella pneumoniae by zinc and copper pyrithione
Antimicrob. Agents Chemother.
59
5851-5853
2015
Klebsiella pneumoniae (Q7B8A1), Klebsiella pneumoniae
brenda
Green, K.; Garneau-Tsodikova, S.
Domain dissection and characterization of the aminoglycoside resistance enzyme ANT(3'')-Ii/AAC(6')-IId from Serratia marcescens
Biochimie
95
1319-1325
2013
Serratia marcescens (Q8VQN7)
brenda
Lin, D.L.; Tran, T.; Adams, C.; Alam, J.Y.; Herron, S.R.; Tolmasky, M.E.
Inhibitors of the aminoglycoside 6-N-acetyltransferase type Ib [AAC(6)-Ib] identified by in silico molecular docking
Bioorg. Med. Chem. Lett.
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5694-5698
2013
Escherichia coli (Q6SJ71)
brenda
Jin, W.; Wachino, J.; Kimura, K.; Yamada, K.; Arakawa, Y.
New plasmid-mediated aminoglycoside 6-N-acetyltransferase, AAC(6')-Ian, and ESBL, TLA-3, from a Serratia marcescens clinical isolate
J. Antimicrob. Chemother.
70
1331-1337
2015
Serratia marcescens (A0A0B6VRK1), Serratia marcescens, Serratia marcescens NUBL-11663 (A0A0B6VRK1)
brenda
Stogios, P.; Kuhn, M.; Evdokimova, E.; Law, M.; Courvalin, P.; Savchenko, A.
Structural and biochemical characterization of Acinetobacter spp. aminoglycoside acetyltransferases highlights functional and evolutionary variation among antibiotic resistance enzymes
ACS Infect. Dis.
3
132-143
2017
Acinetobacter baumannii (Q43899), Acinetobacter haemolyticus (Q44057)
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Xu, Z.; Stogios, P.J.; Quaile, A.T.; Forsberg, K.J.; Patel, S.; Skarina, T.; Houliston, S.; Arrowsmith, C.; Dantas, G.; Savchenko, A.
Structural and functional survey of environmental aminoglycoside acetyltransferases reveals functionality of resistance enzymes
ACS Infect. Dis.
3
653-665
2017
uncultured bacterium (A0A059WZ16)
brenda
Kim, D.; Thawng, C.; Lee, K.; Cha, C.
Revisiting polymorphic diversity of aminoglycoside N-acetyltransferase AAC(6)-Ib based on bacterial genomes of human, animal, and environmental origins
Front. Microbiol.
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1831
2018
bacterium
brenda
Chiem, K.; Hue, F.; Magallon, J.; Tolmasky, M.
Inhibition of aminoglycoside 6'-N-acetyltransferase type Ib-mediated amikacin resistance by zinc complexed with clioquinol, an ionophore active against tumors and neurodegenerative diseases
Int. J. Antimicrob. Agents
51
271-273
2018
Acinetobacter baumannii, Acinetobacter baumannii A155
brenda
Tran, T.; Chiem, K.; Jani, S.; Arivett, B.; Lin, D.; Lad, R.; Jimenez, V.; Farone, M.; Debevec, G.; Santos, R.; Giulianotti, M.; Pinilla, C.; Tolmasky, M.
Identification of a small molecule inhibitor of the aminoglycoside 6-N-acetyltransferase type Ib [AAC(6)-Ib] using mixture-based combinatorial libraries
Int. J. Antimicrob. Agents
51
752-761
2018
Acinetobacter baumannii, Klebsiella pneumoniae, Klebsiella pneumoniae JHCK1, Acinetobacter baumannii A155
brenda
Chiem, K.; Jani, S.; Fuentes, B.; Lin, D.; Rasche, M.; Tolmasky, M.
Identification of an inhibitor of the aminoglycoside 6'-N-acetyltransferase type Ib [AAC(6')-Ib] by glide molecular docking
MedChemComm
7
184-189
2016
Escherichia coli (Q6SJ71)
brenda
Smith, C.; Bhattacharya, M.; Toth, M.; Stewart, N.; Vakulenko, S.
Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im
Microb. Cell
4
402-410
2017
Escherichia coli (Q93ET8)
brenda
Tada, T.; Miyoshi-Akiyama, T.; Shimada, K.; Dahal, R.; Mishra, S.; Ohara, H.; Kirikae, T.; Pokhrel, B.
A novel 6'-N-aminoglycoside acetyltransferase, AAC(6)-Ial, from a clinical isolate of Serratia marcescens
Microb. Drug Resist.
22
103-108
2016
Serratia marcescens (V5YUM6)
brenda
Tabatabaei, I.; Ruf, S.; Bock, R.
A bifunctional aminoglycoside acetyltransferase/phosphotransferase conferring tobramycin resistance provides an efficient selectable marker for plastid transformation
Plant Mol. Biol.
93
269-281
2017
Enterococcus faecalis (P0A0C2), Enterococcus faecalis ATCC 700802 (P0A0C2)
brenda