Information on EC 2.3.1.82 - aminoglycoside 6'-N-acetyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.3.1.82
-
RECOMMENDED NAME
GeneOntology No.
aminoglycoside 6'-N-acetyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + kanamycin-B = CoA + N6'-acetylkanamycin-B
show the reaction diagram
mechanism
-
acetyl-CoA + kanamycin-B = CoA + N6'-acetylkanamycin-B
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:kanamycin-B N6'-acetyltransferase
The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2 and sisomicin are substrates. The antibiotics gentamicin, tobramycin and neomycin, but not paromomycin, can also act as acceptors. The 6-amino group of the purpurosamine ring is acetylated.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AAC(3)-Ib/AAC(6')-Ib'
-
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 (EC 2.3.1.82) exhibits a broad substrate spectrum
AAC(6')
-
-
-
-
AAC(6')-Ib-cr
-
bifunctional variant of AAC(6')-Ib
AAC(6')-Ie
-
aminoglycoside acetyltransferase domain of acetyltransferase-6'-aminoglycoside phosphotransferase-2'
AAC(6')-Ie/APH(2')-Ia
-
-
AAC(6')-Isa
Streptomyces albulus IFO14147
-
-
AAC(6')-Iy
-
-
AAC(6')-Iz acetyltransferase
-
-
acetyltransferase, aminoglycoside 6'-N-
-
-
-
-
acetyltransferase, kanamycin
-
-
-
-
acetyltransferase-6'-aminoglycoside phosphotransferase-2'
-
-
aminoglycoside 6'-N-acetyltransferase
-
-
-
-
aminoglycoside 6'-N-acetyltransferase
-
-
aminoglycoside 6'-N-acetyltransferase
-
-
aminoglycoside 6'-N-acetyltransferase
-
aminoglycoside 6'-N-acetyltransferase
-
aminoglycoside 6'-N-acetyltransferase
Streptomyces albulus IFO14147
-
-
aminoglycoside 6'-N-acetyltransferase Ib
-
-
aminoglycoside 6'-N-acetyltransferase type Ib
-
-
aminoglycoside 6'-N-acetyltransferase type Ii
-
-
aminoglycoside 6-N-acetyltransferase
-
-
aminoglycoside acetyltransferase eis
-
-
aminoglycoside N-6'-acetyltransferase
-
-
aminoglycoside N-6'-acetyltransferase Ii
-
-
aminoglycoside N-acetyltransferase
-
-
aminoglycoside-6'-acetyltransferase
-
-
-
-
aminoglycoside-6'-N-acetyltransferase
-
-
-
-
aminoglycoside-6-N-acetyltransferase
-
-
-
-
ANT(3'')-Ii/AAC(6')-IId
-
bifunctional enzyme catalyzes adenylation and acetylation of aminoglycoside antibiotics
CAS REGISTRY NUMBER
COMMENTARY
56467-65-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 8
-
-
Manually annotated by BRENDA team
Actinomyces sp. 8
strain 8
-
-
Manually annotated by BRENDA team
strain CFr564, enzyme variant with Ser119
-
-
Manually annotated by BRENDA team
Citrobacter freundii CFr564
strain CFr564, enzyme variant with Ser119
-
-
Manually annotated by BRENDA team
strain EC1562 and EC1563, enzyme variant with Ser119
-
-
Manually annotated by BRENDA team
Enterobacter cloacae EC1562
strain EC1562 and EC1563, enzyme variant with Ser119
-
-
Manually annotated by BRENDA team
6'-N-acetyltransferase type li, transformation of Escherichia coli methionine auxotroph B834(DE3)/pLys S with a pPLaac-1 overexpression plasmid containing the aac(6')-li gene
SwissProt
Manually annotated by BRENDA team
chromosomally encoded aminoglycoside 6'-N-acetyltransferase
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
DH5alpha, AAC(6')-Ib protein and AAC(6')-IIa protein
-
-
Manually annotated by BRENDA team
encoded by multiresistance transposon Tn1331
-
-
Manually annotated by BRENDA team
encoded by plasmid pJHCMW1
-
-
Manually annotated by BRENDA team
strains W677 carrying either R factor R-5 or R-79
-
-
Manually annotated by BRENDA team
Escherichia coli CS2R2
CS2R2
-
-
Manually annotated by BRENDA team
Escherichia coli NR79
NR79
-
-
Manually annotated by BRENDA team
plasmid C-MW1 mutant AAC6'-IbL160A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid C-MW1 mutant AAC6'-IbN159A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbC165A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbE167A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbE172A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbF171A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbG170A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbG175A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbI163A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbK168A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbP155A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbP157A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbQ174A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbR161A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbR164A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbR173A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbS156A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbS158A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
plasmid pJHC-MW1 mutant AAC6'-IbY166A 6'-N-acetyltransferase gene
SwissProt
Manually annotated by BRENDA team
strains 2513 and 731
-
-
Manually annotated by BRENDA team
strains GN315 and 141
-
-
Manually annotated by BRENDA team
strain BM2687, enzyme Ib
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens BM2687
strain BM2687, enzyme Ib
-
-
Manually annotated by BRENDA team
chromosomally encoded
-
-
Manually annotated by BRENDA team
serovar typhimurium, bla(PER-1)-carrying plasmid pSTI1
-
-
Manually annotated by BRENDA team
wild-type enzyme and mutant enzymes C109A and C109A/C70A
-
-
Manually annotated by BRENDA team
strain VU12944/77
-
-
Manually annotated by BRENDA team
Serratia marcescens VU12944/77
strain VU12944/77
-
-
Manually annotated by BRENDA team
bifucntional aminoglycoside (6') acetyltransferase-Ie/aminoglycoside (2') phosphotransferase-Ia
-
-
Manually annotated by BRENDA team
harbouring plasmid RPAL
-
-
Manually annotated by BRENDA team
Staphylococcus epidermidis RYC 13036
RYC 13036
-
-
Manually annotated by BRENDA team
IFO14147
SwissProt
Manually annotated by BRENDA team
Streptomyces albulus IFO14147
IFO14147
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + 2'-N-ethylnetilmicin
CoA + N6'-acetyl-2'-N-ethylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Streptomyces albulus IFO14147
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
Staphylococcus epidermidis RYC 13036
-
-
-
?
acetyl-CoA + amikacin
CoA + N6'-acetylamikacin
show the reaction diagram
Citrobacter freundii CFr564, Enterobacter cloacae EC1562
-
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
show the reaction diagram
Pseudomonas fluorescens BM2687
-
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
?
show the reaction diagram
-
-
-
-
?
acetyl-CoA + amikacin
CoA + 6'-N-acetylamikacin
show the reaction diagram
-
aminoglycoside acetyltransferase eis acetylates and inactivates amikacin
-
?
acetyl-CoA + aminoglycoside
CoA + 6'-N-acetylaminoglycoside
show the reaction diagram
-
-
-
?
acetyl-CoA + butirosin
CoA + N6'-acetylbutirosin
show the reaction diagram
-
-
-
?
acetyl-CoA + ciprofloxacin
CoA + N4'-acetylnorfloxacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
Actinomyces sp. 8
-
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
Streptomyces albulus IFO14147
-
-
?
acetyl-CoA + dibekacin
CoA + N6'-acetyldibekacin
show the reaction diagram
Escherichia coli NR79, Serratia marcescens VU12944/77
-
-
-
?
acetyl-CoA + fortimicin A
CoA + N6'-acetylfortimicin A
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin
CoA + N6'-acetylgentamicin
show the reaction diagram
Staphylococcus epidermidis, Staphylococcus epidermidis RYC 13036
-
-
-
?
acetyl-CoA + gentamicin
CoA + 6'-N-acetylgentamicin
show the reaction diagram
-
-
?
acetyl-CoA + gentamicin B
CoA + N6'-acetylgentamicin B
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C
CoA + N6'-acetylgentamicin C
show the reaction diagram
Staphylococcus epidermidis, Staphylococcus epidermidis RYC 13036
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N6'-acetylgentamicin C1
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
-
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
show the reaction diagram
-
poor substrate, AAC-(6')-II type
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
Escherichia coli NR79, Serratia marcescens VU12944/77
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N6'-acetylgentamicin C1a
show the reaction diagram
Pseudomonas fluorescens BM2687
-
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 C2
CoA + N6'-acetylgentgamicin C2
show the reaction diagram
-
poor substrate, not gentamicin A and C1
-
?
acetyl-CoA + histone
CoA + ?
show the reaction diagram
a mixture of calf histones enriched in H3 and H4
-
?
acetyl-CoA + human histone H3 peptide containing a C-terminal cysteine residue
CoA + ?
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin A1
CoA + N6'-acetylhybrimycin A1
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin A2
CoA + N6'-acetylhybrimycin A2
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin A3
CoA + N6'-acetylhybrimycin A3
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin B1
CoA + N6'-acetylhybrimycin B1
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin B2
CoA + N6'-acetylhybrimycin B2
show the reaction diagram
-
-
-
?
acetyl-CoA + hybrimycin B3
CoA + N6'-acetylhybrimycin B3
show the reaction diagram
-
-
-
?
acetyl-CoA + isepamicin
CoA + N6'-acetylisepamicin
show the reaction diagram
-
-
-
?
acetyl-CoA + istamycin-B
CoA + N6'-acetylistamycin-B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
show the reaction diagram
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
?
acetyl-CoA + kanamycin
CoA + N6'-acetylkanamycin
show the reaction diagram
Actinomyces sp. 8
-
-
-
?
acetyl-CoA + kanamycin
CoA + 6'-N-acetylkanamycin
show the reaction diagram
-
aminoglycoside acetyltransferase eis acetylates and inactivates kanamycin
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
-
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
-
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
show the reaction diagram
Streptomyces albulus IFO14147
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
Escherichia coli CS2R2
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N6'-acetylkanamycin A
show the reaction diagram
Escherichia coli NR79, Serratia marcescens VU12944/77
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N6'-acetylkanamycin B
show the reaction diagram
Escherichia coli CS2R2
-
-
-
?
acetyl-CoA + lividomycin A
CoA + O6'-acetyllividomycin A
show the reaction diagram
-
-
?
acetyl-CoA + micromomicin
CoA + N6'-acetylmicromomicin
show the reaction diagram
Actinomyces sp., Actinomyces sp. 8
-
-
-
?
acetyl-CoA + myelin basic protein
CoA + ?
show the reaction diagram
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + 6'-N-acetylneamine
show the reaction diagram
Moraxella sp., Escherichia coli CS2R2
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + neamine
CoA + N6'-acetylneamine
show the reaction diagram
-
-
-
?
acetyl-CoA + nebramycin factor 4
CoA + N6'-acetylnebramycin factor 4
show the reaction diagram
-
no activity with factor 2
-
?
acetyl-CoA + nebramycin factor 6
CoA + N6'-acetylnebramycin factor 6
show the reaction diagram
-
no activity with factor 2
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin
CoA + N6'-acetylneomycin
show the reaction diagram
-
-
?
acetyl-CoA + neomycin A
CoA + N6'-acetylneomycin A
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin B
CoA + N6'-acetylneomycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin B
CoA + N6'-acetylneomycin B
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin B
CoA + ?
show the reaction diagram
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin C
show the reaction diagram
Escherichia coli CS2R2
-
-
-
?
acetyl-CoA + neomycin C
CoA + N6'-acetylneomycin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
-
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
?
acetyl-CoA + netilmicin
CoA + N6'-acetylnetilmicin
show the reaction diagram
Pseudomonas fluorescens BM2687
-
-
-
?
acetyl-CoA + norfloxacin
CoA + N6'-acetylnorfloxacin
show the reaction diagram
-
-
-
?
acetyl-CoA + paromomycin
CoA + O6'-acetylparomomycin
show the reaction diagram
-
-
-
?
acetyl-CoA + poly-L-Lys
CoA + ?
show the reaction diagram
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'-acetylribostamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + ribostamycin
CoA + N6'acetylribostamycin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
-
-
?
acetyl-CoA + sisomicin
CoA + N6'-acetylsisomicin
show the reaction diagram
Actinomyces sp. 8
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
-
wild-type enzyme shows activity, mutant enzymes show no activity or reduced activity
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
Streptomyces albulus IFO14147
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
Staphylococcus epidermidis RYC 13036
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
Escherichia coli NR79, Serratia marcescens VU12944/77
-
-
-
?
acetyl-CoA + tobramycin
CoA + N6'-acetyltobramycin
show the reaction diagram
Pseudomonas fluorescens BM2687
-
-
-
?
butyryl-CoA + tobramycin
CoA + N6'-butyryltobramycin
show the reaction diagram
-
-
-
?
malonyl-CoA + sisomycin
CoA + ?
show the reaction diagram
-
-
?
n-butyryl-CoA + sisomycin
CoA + ?
show the reaction diagram
-
-
?
n-propionyl-CoA + sisomycin
CoA + ?
show the reaction diagram
-
-
?
propionyl-CoA + tobramycin
CoA + N6'-propionyltobramycin
show the reaction diagram
-
tobramycin exhibits a rapid, tobramycin-independent rate of hydrolysis that is linearly proportional to enzyme
-
?
malonyl-CoA + tobramycin
CoA + N6'-malonyltobramycin
show the reaction diagram
-
-
-
?
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
?
-
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
?
-
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
?
-
-
C70 is directly involved in aminoglycoside binding
-
-
-
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, 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
?
-
-
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
?
-
-
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
?
-
-
confer broad aminoglycoside resistance in strains in which the structural gene is expressed
-
-
-
additional information
?
-
-
the enzyme is an important microbial resistance determinant
-
-
-
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
?
-
-
Asp-88 acts as an active site base in the molecular mechanism of AAC(6')-Ie
-
-
-
additional information
?
-
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
-
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
?
-
-
use of aminoglycoside derivatives to study the mechanism of aminoglycoside 6'-N-acetyltransferase
-
-
-
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
?
-
Actinomyces sp. 8
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Streptomyces albulus IFO14147
the enzyme is susceptoble to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer
-
-
-
additional information
?
-
Staphylococcus epidermidis RYC 13036
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Escherichia coli CS2R2
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Citrobacter freundii CFr564
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Escherichia coli NR79, Serratia marcescens VU12944/77
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Enterobacter cloacae EC1562
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Pseudomonas fluorescens BM2687
-
involved in resistance to antibiotics
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + aminoglycoside
CoA + 6'-N-acetylaminoglycoside
show the reaction diagram
-
-
-
?
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
?
-
-
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
?
-
Q47764
involved in resistance to antibiotics
-
-
-
additional information
?
-
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Q93TA5, Q93TA6, Q93TA7, Q93TA8, Q93TA9, Q93TB0, Q93TB1, Q93TB2, Q93TB3, Q93TB4, Q93TB5, Q93TB6, Q93TB7, Q93TB8, Q93TB9, Q93TC0, Q93TC1, Q93TC2, Q93TC3
involved in resistance to antibiotics
-
-
-
additional information
?
-
P19650
involved in resistance to antibiotics
-
-
-
additional information
?
-
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
P10051
involved in resistance to antibiotics
-
-
-
additional information
?
-
P50858
involved in resistance to antibiotics
-
-
-
additional information
?
-
P20092
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
?
-
-
confer broad aminoglycoside resistance in strains in which the structural gene is expressed
-
-
-
additional information
?
-
-
the enzyme is an important microbial resistance determinant
-
-
-
additional information
?
-
Actinomyces sp. 8
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Staphylococcus epidermidis RYC 13036
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Escherichia coli CS2R2
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Citrobacter freundii CFr564
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Escherichia coli NR79, Serratia marcescens VU12944/77
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Enterobacter cloacae EC1562
-
involved in resistance to antibiotics
-
-
-
additional information
?
-
Pseudomonas fluorescens BM2687
-
involved in resistance to antibiotics
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(3-sulfanylpropanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(4-sulfanylbutanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(5-sulfanylpentanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(sulfanylacetyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(2-sulfanylethyl)sulfonyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(dioxidosulfanyl)acetyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(oxidosulfanyl)acetyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[3-(dioxidosulfanyl)propanoyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[3-(oxidosulfanyl)propanoyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-6-O-[methoxy(2-sulfanylethyl)phosphoryl]-alpha-D-glucopyranoside-S-CoA
-
-
1-(bromomethyl)phenanthrene
-
inactivates through covalent modification of Asp99
6'-N-acetylkanamycin A
-
competitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA
6'-N-acetylneamine
-
product inhibition
amikacin
-
substrate inhibition
Butyryl-CoA
-
-
Butyryl-CoA
-
uncompetitive versus kanamycin A and competitive versus acetyl CoA
Butyryl-CoA
-
-
CoA
-
product inhibition
CoA-aminoglycoside 1
-
-
CoA-aminoglycoside 11a
-
-
CoA-aminoglycoside 11b
-
-
CoA-aminoglycoside 11c
-
-
CoA-aminoglycoside 1a
-
-
CoA-aminoglycoside 1b
-
-
CoA-aminoglycoside 1c
-
-
CoA-aminoglycoside 1d
-
-
CoA-aminoglycoside 2
-
-
CoA-aminoglycoside 3
-
-
CoA-aminoglycoside 4a
-
competitive
CoA-aminoglycoside 4b
-
competitive
CoA-aminoglycoside 4c
-
competitive
CoA-aminoglycoside 4d
-
competitive
CoA-aminoglycoside 4e
-
competitive
CoA-aminoglycoside 4f
-
competitive
CoA-aminoglycoside 5b
-
competitive
CoA-aminoglycoside 5d
-
competitive
CoA-aminoglycoside 5e
-
competitive
CoASH
-
uncompetitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA
dithio-CoA
-
-
gentamicin
-
substrate inhibition
gentamicin A
-
-
gentamicin C1
-
-
gentamicin C1
-
competitive inhibitor of neamine, non-competitive inhibitor of acetyl-CoA
gentamine A
-
-
iodoacetamide
-
inactivation in a biphasic manner, half of the activity is lost rapidly and the other half more slowly, tobramycin but not acetyl-CoA protects
kanamycin A
-
-
kanamycin B
-
-
lividomycin
-
-
N6'-acetyl kanamycin A
-
-
N6'-Acetylgentamicin C1a
-
-
N6'-acetylneomycin B
-
-
netilmicin
-
substrate inhibition
netilmicin
-
-
paromamine
-
-
paromomycin
-
-
paromomycin
-
inhibits reaction with neamine
paromomycin
-
competitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA
paromomycin
-
-
Pefloxacin
-
-
poly-L-Lys
substrate inhibition
tobramycin
-
substrate inhibition
tobramycin
-
-
lividomycin A
-
-
additional information
-
no inhibition by GTP
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
acetyl-CoA
-
pH 6.0, 37C, mutant enzyme L76A
0.0041
acetyl-CoA
-
pH 6.0, 37C, mutant enzyme Y147F
0.0047
acetyl-CoA
-
pH 6.0, 37C, mutant enzyme Y147A
0.0053
acetyl-CoA
-
AAC(6')-Ib-cr variant
0.0073
acetyl-CoA
-
pH 6.0, 37C, 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, 37C, mutant AAC(6')-Ie D99E
0.0187
acetyl-CoA
pH 8.0, 30C, cosubstrate: sisomycin
0.0235
acetyl-CoA
-
pH 6.0, 37C
0.0235
acetyl-CoA
-
pH 6.0, 37C, wild-type enzyme
0.035
acetyl-CoA
-
AAC(6')-Ib, wild type
0.038
acetyl-CoA
-
pH 7.5, 37C,wild-type AAC(6')-Ie
0.0399
acetyl-CoA
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.044
acetyl-CoA
-
pH 7.5
0.0453
acetyl-CoA
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.0489
acetyl-CoA
-
pH 6.0, 37C, mutant enzyme L76P
0.07
acetyl-CoA
-
reaction with tobramycin, mutant enzyme C109A/C70A
0.0736
acetyl-CoA
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.108
acetyl-CoA
-
AAC(6')-Ib-cr variant
0.154
acetyl-CoA
-
pH 6.0, 37C, mutant enzyme E72A
0.001
amikacin
-
reaction with AAC (6?)-Ib' domain
0.00434
amikacin
pH 8.0, 30C
0.0114
amikacin
-
pH 6.0, 37C, mutant enzyme L76A
0.0131
amikacin
-
pH 6.0, 37C
0.0131
amikacin
-
pH 6.0, 37C, wild-type enzyme
0.036
amikacin
-
pH 7.5, 37C
0.05
amikacin
-
wild-type enzyme
0.057
amikacin
-
-
0.0582
amikacin
-
pH 6.0, 37C, mutant enzyme H74A
0.0693
amikacin
-
wild-type enzyme
0.075
amikacin
-
mutant enzyme C109A
0.112
amikacin
-
-
0.313
amikacin
-
pH 7.5
0.364
amikacin
-
pH 6.5, 37C
0.38
amikacin
-
pH 6.0, 37C, mutant enzyme E72A
0.571
amikacin
-
pH 5.5, 37C
2.19
amikacin
-
pH 6.0, 37C, mutant enzyme Y147F
0.014
butirosin
-
pH 6.0, 37C
9.3
Butyryl-CoA
-
reaction with tobramycin, wild-type enzyme
0.07
Ciprofloxacin
-
AAC(6')-Ib-cr variant
0.00038
dibekacin
pH 8.0, 30C
0.003
dibekacin
-
reaction with AAC (6?)-Ib' domain
0.03
dibekacin
-
wild-type enzyme
0.036
dibekacin
-
pH 6.0, 37C
0.0254
fortimicin A
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.0435
fortimicin A
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.07
fortimicin A
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.0083
gentamicin
-
reaction with AAC (6?)-Ib' domain
0.015
gentamicin
-
pH 7.5
0.077
gentamicin
-
pH 7.5, 37C
0.297
gentamicin
-
pH 6.5, 37C
0.653
gentamicin
-
pH 5.5, 37C
0.0223
gentamicin B
-
pH 6.0, 37C
0.0082
gentamicin C
-
wild-type enzyme
0.0003
isepamicin
-
reaction with AAC (6?)-Ib' domain
0.008
kanamycin
-
-
0.154
kanamycin
-
-
0.001
kanamycin A
-
pH 6.0
0.001
kanamycin A
-
pH 7.5
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, 30C
0.0114
kanamycin A
-
wild-type enzyme
0.012
kanamycin A
-
pH 7.5
0.0144
kanamycin A
-
pH 6.0, 37C, mutant enzyme H74A
0.0199
kanamycin A
-
pH 6.0, 37C
0.0199
kanamycin A
-
pH 6.0, 37C, wild-type enzyme
0.0257
kanamycin A
-
pH 6.0, 37C, mutant enzyme L76A
0.031
kanamycin A
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.079
kanamycin A
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.0902
kanamycin A
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.102
kanamycin A
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.105
kanamycin A
-
wild-type enzyme
0.11
kanamycin A
-
pH 6.0, 37C, mutant enzyme Y147A
0.34
kanamycin A
-
pH 6.0, 37C, mutant enzyme Y147F
0.771
kanamycin A
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
3.49
kanamycin A
-
pH 6.0, 37C, mutant enzyme E72A
0.00027
kanamycin B
-
AAC(6')-Ib, wild type
0.0067
kanamycin B
-
AAC(6')-Ib-cr variant
0.017
kanamycin B
-
mutant enzyme C109A
0.0189
kanamycin B
-
pH 6.0, 37C
0.079
kanamycin B
-
wild-type enzyme
0.9
kanamycin B
-
mutant enzyme C109A/C70A
0.04188
lividomycin A
pH 8.0, 30C
0.58
malonyl-CoA
pH 8.0, 30C, cosubstrate: sisomycin
0.82
malonyl-CoA
-
reaction with tobramycin, wild-type enzyme
0.0686
n-Butyryl-CoA
pH 8.0, 30C, cosubstrate: sisomycin
0.0161
n-propionyl-CoA
pH 8.0, 30C, cosubstrate: sisomycin
0.0058
neamine
-
pH 6.0, 37C, wild-type enzyme
0.00582
neamine
-
pH 6.0, 37C
0.0224
neamine
-
pH 6.0, 37C, mutant enzyme L76A
0.0432
neamine
-
pH 6.0, 37C, mutant enzyme H74A
0.0682
neamine
-
pH 6.0, 37C, mutant enzyme L76P
0.078
neamine
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.15
neamine
-
pH 6.0, 37C, mutant enzyme Y147F
0.169
neamine
-
pH 6.0, 37C, mutant enzyme Y147A
0.229
neamine
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.326
neamine
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.443
neamine
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.482
neamine
-
pH 6.0, 37C, mutant enzyme E72A
0.509
neamine
-
pH 7.5, 37C, 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, 37C, wild-type enzyme
0.0182
neomycin
-
pH 6.0, 37C, mutant enzyme H74A
0.019
neomycin
-
pH 6.0, 37C, mutant enzyme L76A
0.029
neomycin
-
pH 6.0, 37C, mutant enzyme E72A
0.0386
neomycin
-
pH 6.0, 37C, mutant enzyme Y147A
0.0553
neomycin
-
pH 6.0, 37C, mutant enzyme Y147F
0.0573
neomycin
-
pH 6.0, 37C, mutant enzyme L76P
0.53
neomycin A
-
-
0.00052
neomycin B
pH 8.0, 30C
0.02
neomycin B
-
AAC(6')-Ib, wild type
0.00531
neomycin C
-
pH 6.0, 37C
0.014
neomycin C
-
wild-type enzyme
0.25
neomycin C
-
mutant enzyme C109A/C70A
0.001
netilmicin
-
reaction with AAC (6?)-Ib' domain
0.006
netilmicin
-
mutant enzyme C109A
0.00638
netilmicin
-
pH 6.0, 37C
0.008
netilmicin
-
wild-type enzyme
0.036
netilmicin
-
pH 7.5
0.259
netilmicin
-
pH 7.5, 37C
0.46
netilmicin
-
mutant enzyme C109A/C70A
2.44
netilmicin
-
pH 6.5, 37C
0.067
Norfloxacin
-
AAC(6')-Ib-cr variant
0.324
paromomycin
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.771
paromomycin
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.038
poly-L-Lys
pH 7.5, 37C
0.0195
propionyl-CoA
-
pH 6.0, 37C
0.27
propionyl-CoA
-
reaction with tobramycin, wild-type enzyme
0.00908
ribostamycin
-
pH 6.0, 37C
0.0091
ribostamycin
-
pH 6.0, 37C, wild-type enzyme
0.0214
ribostamycin
-
pH 6.0, 37C, mutant enzyme L76A
0.0381
ribostamycin
-
pH 6.0, 37C, mutant enzyme H74A
0.05
ribostamycin
-
wild-type enzyme
0.107
ribostamycin
-
pH 6.0, 37C, mutant enzyme L76P
0.109
ribostamycin
-
pH 6.0, 37C, mutant enzyme Y147A
0.301
ribostamycin
-
pH 6.0, 37C, mutant enzyme E72A
0.306
ribostamycin
-
pH 6.0, 37C, mutant enzyme Y147F
0.00324
sisomicin
pH 8.0, 30C
0.0117
sisomicin
-
pH 6.0, 37C
0.012
sisomicin
-
wild-type enzyme
0.216
tobramicin
-
pH 5.5, 37C
0.00353
tobramycin
pH 8.0, 30C
0.0037
tobramycin
-
wild-type enzyme
0.004
tobramycin
-
-
0.022
tobramycin
-
-
0.022
tobramycin
-
pH 6.0, 37C
0.022
tobramycin
-
pH 6.0, 37C, wild-type enzyme
0.026
tobramycin
-
pH 7.5, 37C
0.026
tobramycin
-
mutant enzyme C109A
0.0369
tobramycin
-
pH 6.0, 37C, mutant enzyme H74A
0.066
tobramycin
-
wild-type enzyme
0.077
tobramycin
-
pH 6.5, 37C
0.136
tobramycin
-
pH 6.0, 37C, mutant enzyme Y147F
0.146
tobramycin
-
pH 6.0, 37C, mutant enzyme L76P
0.147
tobramycin
-
pH 6.0, 37C, mutant enzyme Y147A
0.54
tobramycin
-
mutant enzyme C109A/C70A
0.62
tobramycin
-
pH 6.0, 37C, mutant enzyme L76A
1.15
tobramycin
-
pH 6.0, 37C, mutant enzyme E72A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.035
acetyl-CoA
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.06
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76P
0.07
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.11
acetyl-CoA
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.17
acetyl-CoA
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.173
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme W164A
0.18
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.23
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.4
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.403
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C
0.403
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.8
acetyl-CoA
Serratia marcescens
-
pH 7.5
0.99
acetyl-CoA
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
1
acetyl-CoA
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
1.03
acetyl-CoA
Escherichia coli
-
AAC(6')-Ib-cr variant
1.2
acetyl-CoA
Enterococcus sp.
-
pH 7.5, 37C, wild-type AAC(6')-Ie
1.3
acetyl-CoA
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
1.61
acetyl-CoA
Enterococcus faecium
-
wild-type enzyme
2.32
acetyl-CoA
Escherichia coli
-
AAC(6')-Ib, wild type
5.23
acetyl-CoA
Escherichia coli
-
AAC(6')-Ib-cr variant
0.003
amikacin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.03
amikacin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.04
amikacin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.05
amikacin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
0.05
amikacin
Serratia marcescens
-
pH 7.5
0.106
amikacin
Enterococcus faecium
-
pH 6.0, 37C
0.11
amikacin
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.29
amikacin
Enterococcus faecium
-
wild-type enzyme
3.5
amikacin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
0.466
butirosin
Enterococcus faecium
-
pH 6.0, 37C
1.03
Ciprofloxacin
Escherichia coli
-
AAC(6')-Ib-cr variant
0.632
dibekacin
Enterococcus faecium
-
pH 6.0, 37C
1.3
dibekacin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
0.0002
fortimicin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.0008
fortimicin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.006
fortimicin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.28
fortimicin A
Enterococcus sp.
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.45
fortimicin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.5
gentamicin
Serratia marcescens
-
pH 7.5
2
gentamicin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
0.388
gentamicin B
Enterococcus faecium
-
pH 6.0, 37C
1.01
gentamicin C
Enterococcus faecium
-
wild-type enzyme
2.4
isepamicin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
0.01
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.03
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.033
kanamycin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.038
kanamycin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.05
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.08
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme W164A
0.19
kanamycin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.27
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.55
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
0.8
kanamycin A
Serratia marcescens
-
pH 7.5
0.816
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C
0.816
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.82
kanamycin A
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
1.1
kanamycin A
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
1.68
kanamycin A
Enterococcus faecium
-
wild-type enzyme
1.7
kanamycin A
Enterococcus sp.
-
pH 7.5, 37C, wild-type AAC(6')-Ie
2.4
kanamycin A
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
1.08
kanamycin B
Enterococcus faecium
-
pH 6.0, 37C
2.27
kanamycin B
Escherichia coli
-
AAC(6')-Ib, wild type
5.25
kanamycin B
Escherichia coli
-
AAC(6')-Ib-cr variant
0.002
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76P
0.004
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.028
neamine
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99N
0.029
neamine
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99A
0.048
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme W164A
0.05
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.066
neamine
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.15
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.38
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.419
neamine
Enterococcus faecium
-
pH 6.0, 37C
0.419
neamine
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.42
neamine
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.43
neamine
Enterococcus sp.
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.44
neamine
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
1.3
neamine
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.001
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.04
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76P
0.07
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.16
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.19
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.2
neomycin
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.3
neomycin
Enterococcus faecium
-
wild-type enzyme
1.1
neomycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
6
neomycin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
3.08
neomycin B
Escherichia coli
-
AAC(6')-Ib, wild type
0.135
neomycin C
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme W164A
0.205
neomycin C
Enterococcus faecium
-
pH 6.0, 37C
0.205
neomycin C
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.2
netilmicin
Serratia marcescens
-
pH 7.5
0.512
netilmicin
Enterococcus faecium
-
pH 6.0, 37C
1.3
netilmicin
Pseudomonas aeruginosa
-
reaction with AAC (6')-Ib' domain
1.08
Norfloxacin
Escherichia coli
-
AAC(6')-Ib-cr variant
0.0004
paromomycin
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie D99E
0.026
paromomycin
Enterococcus sp.
-
pH 7.5, 37C, mutant AAC(6')-Ie Y96F
0.059
paromomycin
Enterococcus sp.
-
pH 7.5, 37C, wild-type AAC(6')-Ie
0.0019
poly-L-Lys
Enterococcus faecium
Q47764
pH 7.5, 37C
0.317
propionyl-CoA
Enterococcus faecium
-
pH 6.0, 37C
0.01
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76P
0.02
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.046
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme W164A
0.12
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.15
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
0.23
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.338
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C
0.338
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.34
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, wild-type enzyme
0.35
ribostamycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A
0.37
sisomicin
Enterococcus faecium
-
pH 6.0, 37C
0.004
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147A
0.01
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76P
0.1
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme Y147F
0.3
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme H74A
0.8
tobramycin
Enterococcus faecium
-
wild-type enzyme
0.89
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme L76A
1.1
tobramycin
Enterococcus faecium
-
pH 6.0, 37C, mutant enzyme E72A; pH 6.0, 37C, wild-type enzyme
1.11
tobramycin
Enterococcus faecium
-
pH 6.0, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(3-sulfanylpropanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
0.00016
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(4-sulfanylbutanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
0.008
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(5-sulfanylpentanoyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
0.00008
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[(sulfanylacetyl)amino]-alpha-D-glucopyranoside-S-CoA
-
-
0.0016
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(2-sulfanylethyl)sulfonyl]amino]-alpha-D-glucopyranoside-S-CoA
-
competitive inhibition
0.0016
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(2-sulfanylethyl)sulfonyl]amino]-alpha-D-glucopyranoside-S-CoA
-
-
0.00027
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(dioxidosulfanyl)acetyl]amino]-alpha-D-glucopyranoside-S-CoA
-
competitive inhibition
0.00006
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[(oxidosulfanyl)acetyl]amino]-alpha-D-glucopyranoside-S-CoA
-
competitive inhibition
0.00009
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[3-(dioxidosulfanyl)propanoyl]amino]-alpha-D-glucopyranoside-S-CoA
-
competitive inhibition
0.002
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2,6-dideoxy-6-[[3-(oxidosulfanyl)propanoyl]amino]-alpha-D-glucopyranoside-S-CoA
-
competitive inhibition
0.002
(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-6-O-[methoxy(2-sulfanylethyl)phosphoryl]-alpha-D-glucopyranoside-S-CoA
-
-
0.04
6'-N-acetylated kanamycin A
-
versus acetyl-CoA. K(is)
0.05
6'-N-acetylated kanamycin A
-
versus kanamycin A. K(is)
0.38
6'-N-acetylated kanamycin A
-
versus acetyl-CoA. K(ii)
0.55
6'-N-acetylated kanamycin A
-
versus kanamycin A. K(ii)
0.04
6'-N-acetylkanamycin A
-
versus kanamycin A, K(is)
0.15
6'-N-acetylkanamycin A
-
versus acetyl-CoA, K(is)
0.385
6'-N-acetylkanamycin A
-
versus acetyl-CoA, K(ii)
0.00499
amikacin
-
pH 7.5, 37C, substrate inhibition
0.0087
amikacin
-
pH 6.5, 37C, substrate inhibition
0.02206
amikacin
-
pH 5.5, 37C, substrate inhibition
6
AMP
-
pH 6.9, 37C, inhibition of the reaction with neamine
0.025
Butyryl-CoA
-
versus acetyl-CoA, K(is)
0.11
Butyryl-CoA
-
versus acetyl-CoA, K(is)
0.15
Butyryl-CoA
-
versus kanamycin A, K(is)
0.188
Butyryl-CoA
-
versus kanamycin A, K(ii)
0.57
Butyryl-CoA
-
versus kanamycin A, K(ii)
0.0036
CoA
-
pH 6.9, 37C
0.000076
CoA-aminoglycoside 1
-
-
0.000043
CoA-aminoglycoside 11a
-
-
0.000161
CoA-aminoglycoside 11b
-
-
0.00799
CoA-aminoglycoside 11c
-
-
0.000076
CoA-aminoglycoside 1a
-
-
0.000043
CoA-aminoglycoside 1b
-
-
0.000161
CoA-aminoglycoside 1c
-
-
0.008
CoA-aminoglycoside 1d
-
-
0.00011
CoA-aminoglycoside 2
-
-
0.000111
CoA-aminoglycoside 2
-
-
0.000119
CoA-aminoglycoside 3
-
-
0.0034
CoA-aminoglycoside 4a
-
-
0.13
CoA-aminoglycoside 4b
-
-
0.0012
CoA-aminoglycoside 4c
-
-
0.0034
CoA-aminoglycoside 4d
-
-
0.0036
CoA-aminoglycoside 4e
-
-
0.0074
CoA-aminoglycoside 4f
-
-
0.012
CoA-aminoglycoside 5b
-
-
0.0022
CoA-aminoglycoside 5d
-
-
0.011
CoA-aminoglycoside 5e
-
-
0.02
CoASH
-
versus kanamycin A. K(is)
0.03
CoASH
-
versus acetyl-CoA, K(is)
0.042
CoASH
-
versus acetyl-CoA, K(is)
0.043
CoASH
-
versus acetyl-CoA, K(ii)
0.069
CoASH
-
versus kanamycin A, K(ii)
0.2
CoASH
-
versus kanamycin A. K(ii)
0.072
dibekacin
-
pH 6.0, 37C
0.02256
gentamicin
-
pH 5.5, 37C, substrate inhibition
0.0482
gentamicin
-
pH 6.5, 37C, substrate inhibition
0.079
gentamicin
-
pH 7.5, 37C, substrate inhibition
4
gentamicin C1
-
pH 6.9, 37C, inhibition of the reaction with neamine
0.196
kanamycin A
-
pH 6.0, 37C
0.117
kanamycin B
-
pH 6.0, 37C
0.06446
netilmicin
-
pH 5.5, 37C, substrate inhibition
0.075
netilmicin
-
pH 6.5, 37C, substrate inhibition
0.142
netilmicin
-
pH 6.0, 37C
0.168
netilmicin
-
pH 7.5, 37C, substrate inhibition
0.0012
paromomycin
-
versus kanamycin A, K(is)
0.04
paromomycin
-
versus acetyl-CoA, K(ii)
0.06
paromomycin
-
versus kanamycin A, K(is)
0.117
paromomycin
-
versus acetyl-CoA, K(is)
0.145
paromomycin
-
versus acetyl-CoA, K(ii)
7.7
paromomycin
-
pH 6.9, 37C, inhibition of the reaction with neamine
1.78
poly-L-Lys
pH 7.5, 37C
0.063
sisomicin
-
pH 6.0, 37C
0.00059
tobramycin
-
pH 7.5, 37C, substrate inhibition
0.0023
tobramycin
-
pH 6.5, 37C, substrate inhibition
0.00647
tobramycin
-
pH 5.5, 37C, substrate inhibition
0.059
tobramycin
-
pH 6.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
equilibrium binding and the directly determined thermodynamic parameters for different aminoglycosides and acyl-CoA derivatives to the wild-type enzyme and two mutant enzymes c109A and C109A/C70A using fluorescence spectroscopy and isothermal titration calorimetry
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
-
reaction with tobramycin, gentamicin C1a or neomycin
5.6
-
AAC(6')-Ib
5.8
-
reaction with kanamycin, neomycin, hybrimycin, nebramycin factor 4 and 6
6.5
-
reaction with kanamycin, sisomicin, neamine, amikacin
6.5
-
reaction with tobramycin, amikacin or gentamicin
7.5
-
activity with netilmicin
7.5
-
wild-type AAC(6')-Ie with acetyl-CoA or neamine as variable substrate
8
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3 - 7.6
-
pH 5.3: about 50% of maximal activity, pH 7.6: about 20% of maximal activity, kanamycin A
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
activity assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Actinomyces sp. 8
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
evenly distributed
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
determined by SDS-PAGE and Western Blot analysis
701732
35000
-
gel filtration
636913
55000
-
sucrose density gradient centrifugation
636902
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 59000, strain 141, SDS-PAGE
?
-
x * 55000, strain GN315, SDS-PAGE; x * 57000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
Serratia marcescens VU12944/77
-
x * 55000, strain GN315, SDS-PAGE; x * 57000, SDS-PAGE
-
dimer
-
2 * 17000, SDS-PAGE; 2 * 17173, calculation from nucleotide sequence; 2 * 17184, electrospray ionization mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme catalyzes its own alpha-N-acetylation after posttranslational enzymaric deformylation and removal of the initiator Met
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized with its cofactor coenzyme A in space group C222(1), with unit cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit
-
hanging drop vapor diffusion technique, crystal structure of the 6'-N-acetyltransferase type li in complex with acetyl-CoA determined at 2.7 A resolution
the structure of AAC(6')-Ib is determined in various complexes with donor and acceptor ligands to resolutions greater than 2.2 A
-
recombinant enzyme, vapor diffusion under oil, CoA-ribostamycin ternary complex
-
vapor diffusion under oil, crystal structure of the AAC(6')-Iy-CoA-S-monomethyl-N-6'-acetylneamine complex
-
small-angle X-ray scattering analysis shows that the enzyme adopts a rigid conformation in solution, where the N-terminal acetyltransferase domain is fixed to the C-terminal phosphotransferase domain and not loosely tethered. The addition of acetyl-coenzyme A, coenzyme A, GDP, guanosine 5'-[beta,gamma-imido]triphosphate, and combinations thereof to the protein result in only modest changes to the radius of gyration of the enzyme, which are not consistent with any large changes in enzyme structure upon binding. These results imply some selective advantage to the bifunctional enzyme beyond coexpression as a single polypeptide, likely linked to an improvement in enzymatic properties. The rigid structure may contribute to improved electrostatic steering of aminoglycoside substrates toward the two active sites, which may provide such an advantage
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
pH 7.4, 10 mM MgCl2, 0.6 mM 2-mercaptoethanol, about 35% loss of activity after 10 min, acetyl-CoA prevents, kanamycin protects slightly
636898
42
-
pH 7.4, 10 mM MgCl2, 0.6 mM 2-mercaptoethanol, about 70% loss of activity after 10 min, acetyl-CoA prevents, kanamycin protects slightly
636898
additional information
-
GTP, CoA, gentamicin C, neamine protect against thermal inactivation
636902
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis in the absence of Mg2+ causes irreversible loss of activity
-
Mg2+ stabilizes
-
GTP, CoA, gentamicin C, neamine protect against thermal inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, several months
-
-30C, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
on a Ni-NTA and a Superdex S-75 column, the His6 tag is cleaved using thrombin
-
on a His-Bind NiNTA column
-
both acetyltransferase domains of the bifunctional enzyme AAC(3)-Ib/AAC(6')-Ib' are cloned and purified
-
recombinant AAC(6')-Iaf is purified using Ni-nitrilotriacetic acid agarose, native AAC(6')-Iaf from Pseudomonas aeruginosa on an anti-AAC(6')-Iaf-IgG coupled and NHS-activated Sepharose column
unseparable from 2-O-aminoglycoside phosphotransferase by affinity chromatography or sucrose density gradient ultracentrifugation
-
His-tagged AAC(6')-Isa
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans TK21/pANT-S2
-
expression in Escherichia coli
-
into the vector pET-28a+ for expression in Escherichia coli BL21DE3 cells
-
isogenic plasmids pSCH4663 containing aac(6')-Ib gene and pSCHB4105 containing aac(6')-IIa gene, transferred to Escherichia coli DH5alpha
-
Pseudomonas aeruginosa 141, gene transfer via plasmid pBP30 to Escherichia coli Hb101
-
expression of mutant enzymes F171L and Y80C
-
into the vector pET19b
-
both acetyltransferase domains of the bifunctional enzyme AAC(3)-Ib/AAC(6')-Ib' are cloned
-
cloned into the pET23a(+) vector and overexpression in Escherichia coli conferrs high-level resistance to the usual substrates of aminoglycoside N-acetyltransferase except netilmicin
-
into the vectors pSTV28 and pQE2, pQE2 is used for expression of the protein in Escherichia coli BL21DE3 pLysS cells
Pseudomonas aeruginosa 141, gene transfer via plasmid pBP30 to Escherichia coli Hb101
-
aac(6')-Ib gene
-
expression in Escherichia coli
-
aac(6')-Iz can restore aminoglycoside resistance to tobramycin, netilimicin and sisomicin (four- to eight-fold increase in the MICs) upon Escherichia coli
-
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
C-14T mutation in eis increases expression of aminoglycoside acetyltransferase eis
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E72A
-
mutation causes a notable reduction in affinity for both the 4,5- and 4,5-disubstituted classes of aminoglycosides, with the largest changes being an 83fold decrease in the affinity for the minimal substrate neamine and a 175fold reduction in Km-value for kanamycin
H74A
-
kinetic parameters reveal only a small effect of the mutation on enzyme activity, Km-values for acetyl-CoA and the 4,5- and 4,6-disubstituted aminoglycosides only differs by a range of 2-7.5fold compared to that of the wild-type enzyme, indicating no significant change in apparent affinity
L76A
-
mutant enzyme shows virtually wild-type activity, with the biggest changes being a 3.6fold reduction in the apparent affinity for neomycin and a 3.7fold decrease in turnover number for amikacin
L76P
-
mutant enzyme is impaired in both aminoglycoside recognition and catalysis, 2300fold decrease in the ratio of turnover number to Kb-value for neamine, 1300fold reduction in the ratio of turnover number to Kb-value for tobramycin, no detectable activity towardskanamycin A and amikacin
Y147A
-
no detectable activity towardsamikacin
Y147F
-
decrease in aminoglycoside affinity ranges from a 6fold decrease for tobramycin to a large 170fold change in KM-value for amikacin
D99A
-
39fold decrease in the ratio of turnover number to Km-value for acetyl-CoA, 215fold decrease in the ratio of turnover number to Km-value for kanamycin A, 86fold decrease in the ratio of turnover number to Km-value for neamine
D99E
-
4.7fold decrease in the ratio of turnover number to Km-value for acetyl-CoA, 31fold decrease in the ratio of turnover number to Km-value for kanamycin A, 19.3fold decrease in the ratio of turnover number to Km-value for neamine, 134fold decrease in the ratio of turnover number to Km-value for fortimicin A
D99N
-
7fold decrease in the ratio of turnover number to Km-value for acetyl-CoA, 130fold decrease in the ratio of turnover number to Km-value for kanamycin A, 102fold decrease in the ratio of turnover number to Km-value for neamine
Y96F
-
minor effects on the steady state kinetic parameters, largest effects for paromomycin, 5.5fold decrease in the ratio kcat /Km compared with wild-type
D117A
-
complete loss of the resistance phenotype against kanamycin and amikacin
D120A
-
complete loss of the resistance phenotype against kanamycin and amikacin
L119S
-
AAC(6')-Ib L119S. The AAC(6')-Ib protein is unable to efficiently modify gentamicin C1, 1.7% relative to sisomicin, however it is capable of modifying amikacin, 65.5% relative to sisomycin. The mutation results in a 2.8fold increase in acetylation of gentamicin C1, but causes an 8.7fold reduction in the ability to modify amikacin
S119L
-
AAC(6')-IIa S119L. The AAC(6')-IIa protein modifies gentamicin C1 at 10.1% relative to sisomicin, however it shows low activity towards amikacin, 4.1% relative to sisomycin. The mutation results in a 4.8fold reduction in the acetylation of gentamicin C1, but causes an 2fold increase in the ability to modify amikacin
C165A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
E167A
highly reduced ability to confer resistance to kanamycin and amikacin
E172A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
F171G
-
the mutant enzyme is unable to confer resistance against amikacin, kanamycin, netilmicin and tobramicin
F171I
-
the mutant enzyme shows reduced resistance against amikacin, kanamycin, netilmicin and tobramicin
F171K
-
the mutant enzyme is unable to confer resistance against amikacin, kanamycin, netilmicin and tobramicin
F171L
-
the mutant enzyme shows reduced resistance against amikacin, kanamycin, netilmicin and tobramicin
F171L
-
the mutant enzyme of enzyme variant Ib shows lower specific activity than the wild-type enzyme when either kanamycin or its semisynthetic derivative amikacin is used as substrate. Alteration of substrate specificity at 42C. The acetylating activity for kanamycin is higher at 42C than at 30C, the ability to use amikacin as substrate is reduced at 42C. Escherichia coli cells expressing the mutant enzyme are resistant the amikacin at 37C but susceptible at 42C
F171M
-
the mutant enzyme is able to confer detectable resistance against amikacin, kanamycin, netilmicin and tobramicin, although the levels are considerably lower than those conferred by the wild-type enzyme
F171N
-
the mutant enzyme is unable to confer resistance against amikacin, kanamycin, netilmicin and tobramicin
F171S
-
the mutant enzyme is unable to confer resistance against amikacin, kanamycin, netilmicin and tobramicin
F171W
-
the mutant enzyme is able to confer detectable resistance against amikacin, kanamycin, netilmicin and tobramicin, although the levels are considerably lower than those conferred by the wild-type enzyme
G170A
mutant enzyme confers high-level resistance to kanamycin but loses the ability to confer resistance to amikacin
G175A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
I163A
the percentage of loss of resistance to one of the two antibiotics, kanamycin and amikacin, is no more than twice the percentage of loss of resistance to the other antibiotic
K168A
the percentage of loss of resistance to one of the two antibiotics, kanamycin and amikacin, is no more than twice the percentage of loss of resistance to the other antibiotic
L160A
the percentage of loss of resistance to one of the two antibiotics, kanamycin and amikacin, is no more than twice the percentage of loss of resistance to the other antibiotic
N159A
mutant enzyme confers high-level resistance to kanamycin but loses the ability to confer resistance to amikacin
P155A
the percentage of loss of resistance to one of the two antibiotics, kanamycin and amikacin, is no more than twice the percentage of loss of resistance to the other antibiotic
P157A
the percentage of loss of resistance to one of the two antibiotics, kanamycin and amikacin, is no more than twice the percentage of loss of resistance to the other antibiotic
Q174A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
R161A
-
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
R164A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
R173A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
S156A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type
S158A
mutant enzyme shows levels of resistance to both antibiotics no more than threefold lower than that for the wild type; the MICs of amikacin and kanamycin are higher than those for the wild-type enzyme
Y166A
mutant enzyme confers high-level resistance to kanamycin but loses the ability to confer resistance to amikacin
Y80C
-
the mutant enzyme shows only marginal levels of activity when either amikacin, kanamycin, tobramycin or netilmicin is used as substrate
S83L
-
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
S83L
Pseudomonas fluorescens BM2687
-
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
-
C109A
-
mutation neither abolishes activity nor alters the biphasic inactivation by iodoacetamide
C109A/C70A
-
mutant enzyme is not inactivated by iodoacetamide. Double mutant exhibits large increases in Km-values for both acetyl-CoA and aminoglycoside substrates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
aminoglycoside N-6'-acetyltransferases are important determinants of antibiotic resistance
medicine
-
isolation of 85 clinical strains of Klebsiella pneumoniae and Escherichia coli that are believed to be aac(6')-Ib positive. Among them, 38 strains are wild-type, the remaining 47 strains harbour the aac(6')-Ib-cr variant that confers resistance against aminoglycoside and fluoroquinolone simultaneously. Of these 47 strains, 19 simultaneously harbor the aac(6')-Ib and aac(6')-Ib-cr gene
medicine
-
a C-14T mutation in eis confers kanamycin resistance in Mycobacterium tuberculosis
medicine
-
aac(6')-Iz is an important contributor to aminoglycoside resistance in clinical strains of Stenotrophomonas maltophilia
medicine
-
two isolates resistant to fluoroquinolones and beta-lactam antimicrobials show mutations in the quinolone resistance-determining regions of gene GyrA and of ParC as well as carrying a 150 kb plasmid harbouring the quinolone resistance gene qnrA1, the ciprofloxacin-modifying enzyme-encoding gene aac(6')-Ib-cr and genes encoding for extended-spectrum beta-lactamases such as blaSHV and blaCTX-M-3. When this large plasmid is transferred to Escherichia coli by conjugation, the transconjugants show a 10-75fold increase in the minimum inhibitory concentrations of ciprofloxacin and norfloxacin