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Information on EC 2.3.1.81 - aminoglycoside 3-N-acetyltransferase
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EC Tree
2.3.1.81 aminoglycoside 3-N-acetyltransferaseIUBMB Comments
Different from EC 2.3.1.60 gentamicin 3-N-acetyltransferase. A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
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Word Map
- 2.3.1.81
- gentamicin
- amikacin
- tobramycin
- integrons
-
aminoglycoside-modifying
-
gentamicin-resistant
- apramycin
- netilmicin
- sisomicin
-
blatem
-
aac3-ii
-
aac6\'-ib-cr
-
apramycin-resistant
-
aminoglycoside-resistant
-
aac6'-ie
-
aph3\'-iiia
- lividomycin
- ribostamycin
- arbekacin
-
ant6-ia
- isepamicin
-
dfra12
- butirosin
- fortimicin
-
quinolone-resistant
-
2'-n-acetyltransferase
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
3'-aminoglycoside acetyltransferase, 3-N-acetyltransferase, 3-N-aminoglycoside acetyltransferase, AAC, AAC (3)-IIIb, AAC(3), AAC(3)-Id, AAC(3)-Ig acetyltransferase, Aac(3)-IIIb, AAC(3)-IV, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-aminoglycoside acetyltransferase
-
-
-
-
3-N-aminoglycoside acetyltransferase
AAC(3)
AAC(3)-IV
AAC(3)-XI
AAC3-IV aminoglycoside acetyltransferase
aminoglycoside 3-N-acetyltransferase
aminoglycoside 3-N-acetyltransferase type XI
aminoglycoside N3-acetyltransferase
-
-
-
-
3-N-aminoglycoside acetyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:2-deoxystreptamine-antibiotic N3-acetyltransferase
Different from EC 2.3.1.60 gentamicin 3-N-acetyltransferase. A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
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CAS REGISTRY NUMBER
COMMENTARY
60120-42-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
acetyl-CoA + dactimicin
CoA + N4-acetyldactamicin + N4,N6'-diacetyldactimicin
-
the percentage of dactimicin affinity relative to gentamicin C1a is very high (74.6%) only with AAC(3)-I, to the most other enzymes tested, in spite of the bifunctional AAC(6')/APH(2''), dactamicin is stable
-
-
?
acetyl-CoA + fortimicin
CoA + N3-acetylfortimicin
-
-
-
?
acetyl-CoA + gentamicin A
CoA + N3'-acetylgentamicin A
-
acetylation at 6% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C
CoA + N3'-acetylgentamicin C
-
acetylation at 86% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C1A
CoA + N3-acetylgentamicin C1A
-
-
-
?
acetyl-CoA + gentamicin C2
CoA + N3'-acetylgentamicin C2
-
acetylation at 84% the rate of gentamicin C1
-
-
?
acetyl-CoA + isepamycin
CoA + N3'-acetylisepamycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + neomycin
CoA + N2'-acetylneomycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + spectinomycin
CoA + N3'-acetylspectinomycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + streptomycin
CoA + ?
wild-type and recombinant enzyme
-
?
acetyl-CoA + tobramycin
CoA + N3-acetyltobramycin
-
-
-
?
n-propionyl-CoA + kanamycin A
CoA + N3'-n-propionylkanamycin A
-
-
-
-
?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
wild-type and recombinant enzyme
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
Arizona sp.
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
-
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
acetylation at 8% the rate of gentamicin C1
-
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
product identification by high-field NMR
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
product identification by high-field NMR
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
best substrate
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
acetylation at 60% the rate of gentamicin C1
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
wild-type and recombinant enzyme
-
-
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
acetylation at 7% the rate of gentamicin C1
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
-
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
-
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
-
the much higher treshold value for the modification of netilmicin as compared with the one for the modification of sisomicin is due to the 1-N side chain
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
-
the much higher treshold value for the modification of netilmicin as compared with the one for the modification of sisomicin is due to the 1-N side chain
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
acetylation at 51% the rate of gentamicin C1
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
acetylation at 6% the rate of gentamicin C1
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
additional information
?
-
determination of imipenem, meropenem, and gentamicin resistant clinical isolates
-
-
-
additional information
?
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
-
additional information
?
-
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
-
additional information
?
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
-
additional information
?
-
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
-
additional information
?
-
-
no activity with benzoyl-CoA, acetoacetyl-CoA, crotonyl-CoA, isovaleryl-CoA, palmitoyl-CoA, and DL-3-hydroxy-butyryl-CoA by AAC(6')-APH(2'')
-
-
-
additional information
?
-
-
CoASH associates with a high-affinity, catalytic site and with a secondary, low-affinity site that overlaps with the antibiotic binding pocket. The binding of CoASH to the high-affinity site occurs with a small, unfavorable enthalpy and a favorable entropy. Binding to the second site is highly exothermic and is accompanied by an unfavorable entropic contribution. The presence of an aminoglycoside alters the binding of CoASH to the enzyme dramatically such that the binding occurs with a favorable enthalpy and an unfavorable entropy. This is irrespective of which aminoglycoside is the cosubstrate and occurs without a significant change in the affinity of CoASH for the enzyme. The presence of antibiotics eliminates binding of CoASH to the second site
-
-
-
additional information
?
-
-
enzyme displays molecular size-dependent stoichiometry where binding stoichiometries are 1.5-2.0 for small antibiotics and 1.0 for larger. Antibiotic-enzyme interaction occurs with a favorable enthalpy and a compensating unfavorable entropy. The presence of coenzyme A significantly increases the affinity of the antibioticthe enthalpy of binding becomes more favored by 1.7-10.0fold in the presence of the cosubstrate CoASH, while the entropy becomes 2.0-22.5fold less favored. The overall free energy change is still only 1.0-1.9 kcal/mol from binary to ternary for all antibiotics tested, similar to those for other aminoglycoside-modifying enzymes
-
-
-
additional information
?
-
isoform AAC-IIIb demonstrates fast antibiotic turnover rates, high antibiotic affinity. Aminoglycoside binding becomes more enthalpically favored and entropically disfavored when CoASH is complexed to AAC-IIIb. The enzyme catalytically and enthalpically favor those aminoglycosides with amine groups at the 2' carbon and show an increase in affinity of all aminoglycosides when CoASH is present
-
-
-
additional information
?
-
-
no substrates are amikacin
-
-
-
additional information
?
-
-
AAC(3)-Id is responsible for the gain of resistance to diverse agents, i.e. gentamicin C1a, gentamicin C1, sisomicin, neomycin, dibekacin, kanamycin, tobramycin, amikacin, netilmicin, apramycin, dactimicin, spectinomycin, streptomycin, lividomycin, and butirosin, in Salmonella enterica serovar Haifa, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
additional information
?
-
determination of imipenem, meropenem, and gentamicin resistant clinical isolates
-
-
-
additional information
?
-
-
AAC(3)-Id is responsible for the gain of resistance to diverse agents, i.e. gentamicin C1a, gentamicin C1, sisomicin, neomycin, dibekacin, kanamycin, tobramycin, amikacin, netilmicin, apramycin, dactimicin, spectinomycin, streptomycin, lividomycin, and butirosin, in Salmonella enterica serovar Haifa, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-cyclohexyl-3-(3-dimethylamino-propylamino)-propionamide
-
0.5 mM, 77% inhibition
N-[2-(3,4-dimethoxyphenyl)-ethyl]-3-(3-dimethylamino-propylamino)-propionamide
-
0.5 mM, 63% inhibition
additional information
determination of imipenem, meropenem, and gentamicin resistant clinical isolates
-
additional information
strain BM4687 is resistant to gentamicin and tobramycin but susceptible to kanamycin A and amikacin
-
additional information
-
strain BM4687 is resistant to gentamicin and tobramycin but susceptible to kanamycin A and amikacin
-
additional information
-
no inhibition by NH4+, K+, Na+, DTT, N-methylmaleimide
-
additional information
-
only small aminoglycosides without intraring constraints show substrate inhibition
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Endocarditis
Activity of isepamicin and selection of permeability mutants to beta-lactams during aminoglycoside therapy of experimental endocarditis due to Klebsiella pneumoniae CF104 producing an aminoglycoside acetyltransferase 6' modifying enzyme and a TEM-3 beta-lactamase.
Tuberculosis
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.
Tuberculosis
Glycine-rich loop encompassing active site at interface of hexameric M. tuberculosis Eis protein contributes to its structural stability and activity.
Tuberculosis
Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other Roles.
Tuberculosis
Studying aminoglycoside modification by the acetyltransferase class of resistance-causing enzymes via microarray.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00067
apramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.237
butirosin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
1.16
butyryl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0092
dibekacin
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
0.00097
gentamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00036
neomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.042
netilmicin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.499
propionyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0027
acetyl-CoA
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
0.086
acetyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00096
amikacin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0021
amikacin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0716
amikacin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
11.07
amikacin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0029
gentamicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0046
gentamicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0189
gentamicin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.002
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a
0.0033
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.0048
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a
0.0055
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0091
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.0099
kanamycin A
-
pH 6.6, with acetyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.0111
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0135
kanamycin A
-
pH 6.6, with n-propionyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.238
kanamycin A
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0138
kanamycin B
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
0.477
malonyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0031
neomycin B
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0148
neomycin B
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.00015
paromomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0031
ribostamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00057
sisomicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0015
sisomicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.00033
sisomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00142
tobramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0027
tobramycin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0054
tobramycin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
61
apramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
3.5
butirosin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.3
butyryl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.17
dibekacin
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
40
gentamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
32
netilmicin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
33
propionyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.24
acetyl-CoA
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
39
acetyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.124
amikacin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.126
amikacin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.146
amikacin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.5
amikacin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.041
gentamicin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.123
gentamicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.182
gentamicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.012
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a
0.017
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a
0.044
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.134
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.144
kanamycin A
-
pH 6.6, with n-propionyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.163
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.3
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.559
kanamycin A
-
pH 6.6, with acetyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
80
kanamycin A
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.23
kanamycin B
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
9
malonyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
60
neomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.076
neomycin B
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.188
neomycin B
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
15
paromomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
146
ribostamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.121
sisomicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.173
sisomicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
51
sisomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.089
tobramycin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.179
tobramycin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
162
tobramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
dibekacin
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
89
acetyl-CoA
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
17
kanamycin B
pH 6.0, 37°C; recombinant His-tagged enzyme, pH 6.0, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
corresponds to the plateau region of the pH profile, where the velocity is maximal and the variations in velocity due to changes in pH are smallest
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene aacC2; diverse clinical isolates, gene aacC2
UniProt
brenda
strain isolated from the heel biopsy specimen of an 80-year-old diabetic woman
-
-
brenda
strain isolated from the heel biopsy specimen of an 80-year-old diabetic woman
-
-
brenda
plasmid pPK237 transferred to and expressed in Escherichia coli K12
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
analysis of enzyme expression in several clinical isolates, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
presence of genes encoding the following aminoglycoside-modifying enzymes: aph (3')-V1, aph (3')-Ia, aac (3)-Ia, aac (3) IIa, aac (6')-Ih, aac (6')-Ib and ant (2')-Ia responsible for resistance in 4 different groups of clinical isolates, overview
evolution
aminoglycoside 3-N-acetyltransferases [AAC(3)] are widely distributed in Gram-negative bacteria and are categorized in five types (I, II, III, IV, and VI). To date, only four are identified in the Gram-positive aminoglycoside producers, overview
evolution
-
aminoglycoside 3-N-acetyltransferases [AAC(3)] are widely distributed in Gram-negative bacteria and are categorized in five types (I, II, III, IV, and VI). To date, only four are identified in the Gram-positive aminoglycoside producers, overview
-
physiological function
expression in Escherichia coli confers resistance to gentamicin, tobramycin, sisomicin, dibekacin, and fortimicin, the MICs of kanamycin A, netilmicin, amikacin, apramycin, and neomycin B remaining unchanged
physiological function
-
expression in Escherichia coli confers resistance to gentamicin, tobramycin, sisomicin, dibekacin, and fortimicin, the MICs of kanamycin A, netilmicin, amikacin, apramycin, and neomycin B remaining unchanged
-
Show AA Sequence and Transmembrane Helices (5069 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18630
-
18649 Da predicted from nucleotide sequence, 18630 Da found by mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
cleavage of the hexahistidine tag by tobacco etch virus protease
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray structure of a recombinant enzyme, expressed in its selenomethionine substituted form, cocrystallization with 5 mM CoA at 4°C and pH: 7.8, crystal cryoprotection achieved with 17% glycerol and 8% 2R,3R-butanediol, active center found by X-ray analysis and model building
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against EDTA with subsequent Mg2+-addition to dialyzed enzyme has no effect on activity
-
enzyme activity is significantly stabilized when preparations contain substrate
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Fast Flow Q-Sepharose anion exchange column chromatography and Phenyl Sepharose column chromatography
plasmid pPK237 transferred to and expressed in E. coli K12, affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 Star(DE3) by nickel affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli K802N by mating
expression of C- or N-terminally His-tagged enzyme from vectors pET22b, and pET28a or Int-pET19b-pps, respectively
-
gne aac(3)-XI, DNA and amino acid sequence determination and analysis, genomic organization, the aac(3)-XI gene is located downstream from a gene for a transposase (TnpCx) and upstream from that for a two-component system sensor kinase, the sequence upstream from aac(3)-XI does not reveal any putative promoter, recombinant expression of His-tagged enzyme in Escherichia coli strains TOP10 and BL21 Star(DE3)
Pseudomonas aeruginosa plasmid pPK237 transferred to and expressed in Escherichia coli K12
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
-
development of a methodology that utilizes aminoglycoside acetyltransferase and unnatural acyl-CoA analogues for the chemoenzymatic generation of regioselectively N-acylatedaminoglycoside analogues. Aminoglycosides are broad-spectrum antibiotics commonly used for the treatment of serious bacterial infections
medicine
-
mutation in the gene promoter affects the transcription level and enhances resistance to antibiotics
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davies, J.; O'Connor, S.
Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin
Antimicrob. Agents Chemother.
14
69-72
1978
Arizona sp., Escherichia coli, Klebsiella pneumoniae
brenda
Wolf, E.; Vassilev, A.; Makino, Y.; Sali, A.; Nakatani, Y.; Burley, S.K.
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
Cell
94
439-449
1998
Serratia marcescens
brenda
Ishikawa, J.; Sunada, A.; Oyama, R.; Hotta, K.
Identification and characterization of the point mutation which affects the transcription level of the chromosomal 3-N-acetyltransferase gene of Streptomyces griseus SS-1198
Antimicrob. Agents Chemother.
44
437-440
2000
Streptomyces griseus
brenda
Tsuchizaki, N.; Hamadal, M.; Hotta, K.
Rapid characterization by colony direct PCR of distribution specificity in Streptomyces of kan gene encoding a specific aminoglycoside-3-N-acetyltransferase
Actinomycetologica
15
23-29
2001
Streptomyces griseus (Q54216)
-
brenda
Riccio, M.L.; Docquier, J.D.; Dell'Amico, E.; Luzzaro, F.; Amicosante, G.; Rossolini, G.M.
Novel 3-N-aminoglycoside acetyltransferase gene, aac(3)-Ic, from a Pseudomonas aeruginosa integron
Antimicrob. Agents Chemother.
47
1746-1748
2003
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q83V16)
brenda
Biddlecome, S.; Haas, M.; Davies, J.; Rane, D.F.; Daniels, P.J.L.
Enzymatic modification of aminoglycoside antibiotics: a new 3-N-acetylating enzyme from a Pseudomonas aeruginosa isolate
Antimicrob. Agents Chemother.
9
951-955
1976
Escherichia coli, Escherichia coli R135/C600, Pseudomonas aeruginosa, Pseudomonas aeruginosa Travers PST
brenda
Angelatou, F.; Litsas, S.B.; Kontomichalou, P.
Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa
J. Antibiot.
35
235-244
1982
Pseudomonas aeruginosa
brenda
Williams, J.W.; Northrop, D.B.
Kinetic mechanisms of gentamicin acetyltransferase I. Antibiotic-dependent shift from rapid to nonrapid equilibrium random mechanisms
J. Biol. Chem.
253
5902-5907
1978
Escherichia coli, Escherichia coli C600
brenda
Bongaerts, Ger P.A.; Vliegenthart, John S.
Effect of aminoglycoside concentration on reaction rates of aminoglycoside-modifying enzymes
Antimicrob. Agents Chemother.
32
740-746
1988
Escherichia coli, Escherichia coli JR88
brenda
Gomez-Lus, R.; Gomez-Lus, S.; Goni, M.P.; Rivera, M.J.; Martin, C.; Rubio-Calvo, M.C.
Stability of dactimicin to aminoglycoside-modifying enzymes produced by 341 bacterial clinical isolates
Drugs Exp. Clin. Res.
15
129-132
1989
Escherichia coli
brenda
Levings, R.S.; Partridge, S.R.; Lightfoot, D.; Hall, R.M.; Djordjevic, S.P.
New integron-associated gene cassette encoding a 3-N-aminoglycoside acetyltransferase
Antimicrob. Agents Chemother.
49
1238-1241
2005
Salmonella enterica subsp. enterica serovar Kentucky (Q6S741)
brenda
Coombe, R.G.; George, A.M.
Purification and properties of an aminoglycoside acetyltransferase from Pseudomonas aeruginosa
Biochemistry
21
871-875
1982
Pseudomonas aeruginosa
brenda
Elbourne, L.D.; Hall, R.M.
Gene cassette encoding a 3-N-aminoglycoside acetyltransferase in a chromosomal integron. Comments
Antimicrob. Agents Chemother.
50
2270-2271
2006
Saccharophagus degradans
brenda
Magalhaes, M.L.; Blanchard, J.S.
The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli
Biochemistry
44
16275-16283
2005
Escherichia coli, Escherichia coli (Q306W4), Escherichia coli BL21(DE3) pLysS (Q306W4)
brenda
Welch, K.T.; Virga, K.G.; Whittemore, N.A.; Oezen, C.; Wright, E.; Brown, C.L.; Lee, R.E.; Serpersu, E.H.
Discovery of non-carbohydrate inhibitors of aminoglycoside-modifying enzymes
Bioorg. Med. Chem.
13
6252-6263
2005
Homo sapiens
brenda
Subba, B.; Kharel, M.K.; Lee, H.C.; Liou, K.; Kim, B.G.; Sohng, J.K.
The ribostamycin biosynthetic gene cluster in Streptomyces ribosidificus: comparison with butirosin biosynthesis
Mol. Cell
20
90-96
2005
Streptomyces ribosidificus (Q4R0X5)
brenda
Green, K.D.; Chen, W.; Houghton, J.L.; Fridman, M.; Garneau-Tsodikova, S.
Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides
ChemBioChem
11
119-126
2010
Escherichia coli
brenda
Cabrera, R.; Ruiz, J.; Sanchez-Cespedes, J.; Goni, P.; Gomez-Lus, R.; Jimenez de Anta, M.T.; Gascon, J.; Vila, J.
Characterization of the enzyme aac(3)-Id in a clinical isolate of Salmonella enterica serovar Haifa causing travelers diarrhea
Enferm. Infecc. Microbiol. Clin.
27
453-456
2009
Salmonella enterica
brenda
Norris, A.L.; Ozen, C.; Serpersu, E.H.
Thermodynamics and kinetics of association of antibiotics with the aminoglycoside acetyltransferase (3)-IIIb, a resistance-causing enzyme
Biochemistry
49
4027-4035
2010
Pseudomonas aeruginosa
brenda
Norris, A.L.; Serpersu, E.H.
Interactions of coenzyme A with the aminoglycoside acetyltransferase (3)-IIIb and thermodynamics of a ternary system
Biochemistry
49
4036-4042
2010
Pseudomonas aeruginosa
brenda
Galimand, M.; Fishovitz, J.; Lambert, T.; Barbe, V.; Zajicek, J.; Mobashery, S.; Courvalin, P.
AAC(3)-XI, a new aminoglycoside 3-N-acetyltransferase from Corynebacterium striatum
Antimicrob. Agents Chemother.
59
5647-5653
2015
Corynebacterium striatum (A0A0K2X0F2), Corynebacterium striatum, Corynebacterium striatum BM4687 (A0A0K2X0F2), Corynebacterium striatum BM4687
brenda
Norris, A.L.; Nickels, J.; Sokolov, A.P.; Serpersu, E.H.
Protein dynamics are influenced by the order of ligand binding to an antibiotic resistance enzyme
Biochemistry
53
30-38
2014
Pseudomonas aeruginosa (Q51405)
brenda
Atasoy, A.R.; Ciftci, I.H.; Petek, M.
Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates
Int. J. Clin. Exp. Med.
8
2874-2880
2015
Acinetobacter baumannii (P29807)
brenda
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