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Information on EC 2.3.1.81 - aminoglycoside 3-N-acetyltransferase
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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
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aminoglycoside-modifying
- apramycin
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gentamicin-resistant
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aac6\'-ib-cr
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blatem
- netilmicin
- sisomicin
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aac3-ii
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aac6'-ie
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dfra12
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aminoglycoside-resistant
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apramycin-resistant
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ant6-ia
- butirosin
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quinolone-resistant
- arbekacin
- ribostamycin
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blashv
- lividomycin
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oqxab
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aph3\'-iiia
- isepamicin
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2'-n-acetyltransferase
- fortimicin
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amikacin-resistant
- synthesis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
aminoglycoside acetyltransferase, aac(3)-iv, aac(3), aac(6')-aph(2''), aminoglycoside 3-n-acetyltransferase, aac(3)-id, 3-n-acetyltransferase, 3-n-aminoglycoside acetyltransferase, aminoglycoside 3-acetyltransferase, aac-iiib, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-aminoglycoside acetyltransferase
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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
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Eis
Eis2
Enhanced in Intracellular Survival
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
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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
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?
acetyl-CoA + fortimicin
CoA + N3-acetylfortimicin
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?
acetyl-CoA + gentamicin A
CoA + N3'-acetylgentamicin A
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acetylation at 6% the rate of gentamicin C1
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?
acetyl-CoA + gentamicin C
CoA + N3'-acetylgentamicin C
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acetylation at 86% the rate of gentamicin C1
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?
acetyl-CoA + gentamicin C1A
CoA + N3-acetylgentamicin C1A
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?
acetyl-CoA + isepamycin
CoA + N3'-acetylisepamycin
wild-type and recombinant enzyme
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?
acetyl-CoA + neomycin
CoA + N2'-acetylneomycin
wild-type and recombinant enzyme
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?
acetyl-CoA + spectinomycin
CoA + N3'-acetylspectinomycin
wild-type and recombinant enzyme
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?
acetyl-CoA + streptomycin
CoA + ?
wild-type and recombinant enzyme
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?
acetyl-CoA + tobramycin
CoA + N3-acetyltobramycin
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?
n-propionyl-CoA + kanamycin A
CoA + N3'-n-propionylkanamycin A
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?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
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?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
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?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
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?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
wild-type and recombinant enzyme
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?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
Arizona sp.
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a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
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?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
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a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
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?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
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?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
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a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
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?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
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?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
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?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
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acetylation at 8% the rate of gentamicin C1
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?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
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product identification by high-field NMR
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?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
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?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
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product identification by high-field NMR
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?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
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?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
wild-type and recombinant enzyme
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?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
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?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
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best substrate
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?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
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?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
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?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
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acetylation at 60% the rate of gentamicin C1
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?
acetyl-CoA + gentamicin C2
CoA + N3'-acetylgentamicin C2
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acetylation at 84% the rate of gentamicin C1
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?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
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?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
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?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
wild-type and recombinant enzyme
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?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
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?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
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acetylation at 7% the rate of gentamicin C1
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?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
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?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
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?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
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?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
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?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
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?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
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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
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?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
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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
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?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
wild-type and recombinant enzyme
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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best substrate
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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best substrate
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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best substrate
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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best substrate
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
wild-type and recombinant enzyme
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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acetylation at 51% the rate of gentamicin C1
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?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
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best substrate
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?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
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?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
wild-type and recombinant enzyme
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?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
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acetylation at 6% the rate of gentamicin C1
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?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
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?
additional information
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determination of imipenem, meropenem, and gentamicin resistant clinical isolates
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?
additional information
?
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the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
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?
additional information
?
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the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
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?
additional information
?
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the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
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?
additional information
?
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the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
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?
additional information
?
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binding of aminoglycosides to AAC-VIa is enthalpically favored and entropically disfavored with a net result of favorable Gibbs energy. A net deprotonation of the enzyme, ligand, or both accompanies the formation of binary and ternary complexes. Poor substrates: kanamycn A, ribostamycin, neomycin B
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additional information
?
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no activity with benzoyl-CoA, acetoacetyl-CoA, crotonyl-CoA, isovaleryl-CoA, palmitoyl-CoA, and DL-3-hydroxy-butyryl-CoA by AAC(6')-APH(2'')
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?
additional information
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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
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additional information
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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
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additional information
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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
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?
additional information
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no substrates are amikacin
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?
additional information
?
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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
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?