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2.3.1.82: aminoglycoside 6'-N-acetyltransferase

This is an abbreviated version!
For detailed information about aminoglycoside 6'-N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.82

Reaction

acetyl-CoA
+
kanamycin-B
=
CoA
 +
N6'-acetylkanamycin-B

Synonyms

6'-acetyltransferase-Im, 6'-N-acetyltransferase type Ib, AAC, aac(3)-Ib/aac(6')-Ib, AAC(3)-Ib/AAC(6')-Ib', AAC(6'), AAC(6')-I, AAC(6')-Iaf, AAC(6')-IaI, AAC(6')-Iaj, AAC(6')-Ian, AAC(6')-Ib, AAC(6')-Ib-cr, AAC(6')-Ie, AAC(6')-Ie/APH(2")-Ia, AAC(6')-Ie/APH(2'')-Ia, AAC(6')-Ie/APH(2')-Ia, AAC(6')-Ig, AAC(6')-Ih, AAC(6')-Ii, AAC(6')-Im, AAC(6')-Isa, AAC(6')-Iy, AAC(6')-Iz acetyltransferase, AAC(6)-Iak, aac(6)-Ib, AAC3-I, aacA-aphD, acetyltransferase, aminoglycoside 6'-N-, acetyltransferase, kanamycin, acetyltransferase-6'-aminoglycoside phosphotransferase-2", aminoglycoside (3) acetyltransferase AAC(3)-Ia, aminoglycoside 3-N-acetyltransferase/aminoglycoside 6'-N-acetyltransferase fusion protein, aminoglycoside 6'-acetyltransferase-Ie, aminoglycoside 6'-N-acetyltransferase, aminoglycoside 6'-N-acetyltransferase Ib, aminoglycoside 6'-N-acetyltransferase type Ib, aminoglycoside 6'-N-acetyltransferase type Ii, aminoglycoside 6-N-acetyltransferase, aminoglycoside acetyltransferase, aminoglycoside acetyltransferase eis, aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2')-Ia, aminoglycoside N(6')-acetyltransferase type 1, 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, EC 2.3.1.55, meta-AAC0020

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.82 aminoglycoside 6'-N-acetyltransferase

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
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
Y138A
catalytically inactive
additional information
separation of the 3''-adenylyltransferase-aminoglycoside and 6'-acetyltransferase domains of the bifunctional enzyme, and comparison of their activity to that of the full-length enzyme