Information on EC 1.10.3.11 - ubiquinol oxidase (non-electrogenic)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.10.3.11
-
RECOMMENDED NAME
GeneOntology No.
ubiquinol oxidase (non-electrogenic)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aerobic respiration III (alternative oxidase pathway)
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-
SYSTEMATIC NAME
IUBMB Comments
ubiquinol:O2 oxidoreductase (non-electrogenic)
The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit II, Coxb2
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
subunit I, CioA; genes cioA and cioB encoding subunits I and II
UniProt
Manually annotated by BRENDA team
variant Leucorrhiza
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
cultivar Petit Havana SR1
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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transgenic plant cells lacking mitochondrial alternative oxidase have increased susceptibility to mitochondria-dependent and -independent pathways of programmed cell death and show higher sensitivity to treatment with hydrogen peroxide, salicylic acid and cantharidin as compared to the wild type enzyme
metabolism
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the alternative oxidase actively competes with the cytochrome pathway for reducing equivalents and contributes up to 24% to the overall respiratory activity
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ubiquinol + O2
2 ubiquinone + 2 H2O
show the reaction diagram
2 ubiquinol-1 + O2
2 ubiquinone-1 + 2 H2O
show the reaction diagram
2 ubiquinol-10 + O2
2 ubiquinone-10 + 2 H2O
show the reaction diagram
2 ubiquinol-2 + O2
2 ubiquinone-2 + 2 H2O
show the reaction diagram
2 ubiquinol-8 + O2
2 ubiquinone-8 + 2 H2O
show the reaction diagram
-
the quinone bound at the QH site can form a stable semiquinone. The tightly bound ubiquinone-8 at the QH site is not displaced by ubiquinol-1 even during enzyme turnover
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-
?
decylubiquinol + O2
decylubiquinone + H2O
show the reaction diagram
duroquinol + O2
duroquinone + H2O
show the reaction diagram
NADH + O2
?
show the reaction diagram
succinate + O2
?
show the reaction diagram
ubiquinol + O2
ubiquinone + H2O
show the reaction diagram
ubiquinol-1 + O2
ubiquinone-1 + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ubiquinol + O2
2 ubiquinone + 2 H2O
show the reaction diagram
2 ubiquinol-1 + O2
2 ubiquinone-1 + 2 H2O
show the reaction diagram
2 ubiquinol-10 + O2
2 ubiquinone-10 + 2 H2O
show the reaction diagram
2 ubiquinol-2 + O2
2 ubiquinone-2 + 2 H2O
show the reaction diagram
ubiquinol + O2
ubiquinone + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
heme-copper terminal oxidase
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
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i.e. HQNO, binds stoichiometrically to the enzyme and prevents formation of the ubisemiquinone at the QH-site, but does not displace the ubiquinone-8 bound at the QH-site, enzyme binding kineticss, overview
2-Heptyl-4-hydroxyquinoline-N-oxide
;
2-hydroxybenzhydroxamic acid
-
competitive inhibitor towards ubiquinol
5-chloro-3-[(2E)-3,7-dimethylocta-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
an ascofuranone derivative
5-chloro-3-[(2E,6E)-8-hydroxy-3,7-dimethylnona-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
an ascofuranone derivative
antimycin A
56% residual activity at 0.005 mg/ml; 56% residual activity at 0.005 mg/ml
ascofuranone
aurachin C 1-10
15% residual activity at 0.005 mg/ml; 15% residual activity at 0.005 mg/ml
aurachin C1-10
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prevents formation of the ubisemiquinone at the QH-site, but appears to compete for quinol binding at the QL-site, enzyme binding kineticss, overview
aurachin D
16% residual activity at 0.005 mg/ml; 16% residual activity at 0.005 mg/ml
cyanide
Gramicidin S
67% residual activity at 0.005 mg/ml; 67% residual activity at 0.005 mg/ml
LL-Z1272gamma
69% residual activity at 0.005 mg/ml; 69% residual activity at 0.005 mg/ml
n-octyl gallate
n-propyl gallate
octyl gallate
Piericidin A
14% residual activity at 0.005 mg/ml; 14% residual activity at 0.005 mg/ml
propyl gallate
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Salicylhydroxamic acid
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ubiquinol
ubiquinol-1
substrate inhibition
ubiquinol-2
substrate inhibition
ubiquinone-1
product inhibition, an excess amount of ubiquinol-2 is unable to suppress product inhibition with ubiquinone-1 therefore, the inhibition mode may not be competitive
ubiquinone-2
product inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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Carbonyl cyanide m-chlorophenylhydrazone
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dithiothreitol
EDT-20
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glyoxylate
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Hydroxypyruvate
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L-Malate
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in whole mitochondria, L-malate stimulates respiration via alternative oxidase in a pH- (and NAD+)-dependent manner
oxaloacetate
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pyruvate
succinate
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in whole mitochondria, succinate (in the presence of malonate) stimulates respiration via alternative oxidase in a pH- (and NAD+)-dependent manner
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046 - 0.0205
O2
0.0403 - 0.331
ubiquinol-1
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000074
2-heptyl-4-hydroxyquinoline N-oxide
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pH 7.0, 37C, wild-type enzyme
0.000015
aurachin C1-10
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pH 7.0, 37C, wild-type enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
2-Heptyl-4-hydroxyquinoline-N-oxide
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.00000048
5-chloro-3-[(2E,6E)-8-hydroxy-3,7-dimethylnona-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
Trypanosoma brucei
Q26710
pH and temperature not specified in the publication
0.017
antimycin A
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.00004
aurachin C 1-10
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.82
azide
Gluconobacter oxydans
Q5FU85
pH 6.5, 25C
0.008 - 13
cyanide
0.04
Gramicidin S
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.013
LL-Z1272gamma
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.00007 - 0.0001
octyl gallate
0.0007
Piericidin A
Gluconobacter oxydans
Q5FU84, Q5FU85
at 25C in 50 mM potassium phosphate (pH 6.5); at 25C in 50 mM potassium phosphate (pH 6.5)
0.00036 - 0.00044
propyl gallate
0.042 - 0.194
Salicylhydroxamic acid
0.012 - 0.02
sialic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
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recombinant enzyme, in the presence of 10 nM ascofuranone, at 25C, in 50 mM Tris-HCl (pH 7.4)
0.2
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recombinant enzyme, in the presence of 10 nM ascofuranone, at 25C, in 50 mM Tris-HCl (pH 7.4)
1.6
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recombinant enzyme, at 25C, in 50 mM Tris-HCl (pH 7.4)
2.2
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recombinant enzyme, at 25C, in 50 mM Tris-HCl (pH 7.4)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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7
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assay at
7 - 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
band 1, isoelectric focusing
7
band 2, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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mature enzyme, SDS-PAGE
42000
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precursor, SDS-PAGE
110000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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the enzyme exists mainly as a non-covalently linked dimer when expressed in Schizosaccharomyces pombe
heterodimer
homodimer
monomer
trimer
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trypanosomal alternative oxidase in the absence and presence of ascofuranone and ascofuranone derivative 5-chloro-3-[(2E,6E)-8-hydroxy-3,7-dimethylnona-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde, the reservoir solution contains using 28-34% w/v PEG 400, 100 mM imidazole buffer (pH 7.4), and 500 mM potassium formate, X-ray diffraction structure determination and analysis, single-wavelength anomalous dispersion method, anomalous scattering effects caused by Fe measured to 3.2 A resolution
hanging drop vapor diffusion method, using 28-34% (w/v) PEG 400, 100 mM imidazole buffer pH 7.4, 500 mM potassium formate and 0.4% (w/v) C8E4l
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Q-Sepharose column chromatography
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native enzyme from membranes by anion exchange chromatography and gel filtration
native enzyme from membranes by detergent solubilization, anion exchange and hydroxyapatite chromatography
ultracentrifugation and Talon Co2+-affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli SASX41B cells
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expressed in Escherichia coli strain C41 membranes and in Saccharomyces cerevisiae
expressed in Escherichia strain SASX41B
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expressed in heme-deficient Escherichia coli BL21(DE3) cells
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expressed in Nicotiana tabacum
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expressed in Schizosaccharomyces pombe and Escherichia coli
expressed in Schizosaccharomyces pombe mitochondria and spheroplasts
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expressed in Schizosaccharomyces pombe strain sp.011
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expression of wild-type and mutant enzymes in Schizosaccharomyces pombe strain Sp.011, subcloning in Escherichia coli strains JM101 and 110
genes cioA and cioB encoding subunits I and II, phylogenetic analysis
mutant enzymes are expressed in heme-deficient Escherichia coli SASX41B cells
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wild type and mutant enzymes are expressed in Schizosaccharomyces pombe strain sp.011
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cytochrome bd-I-deficient Escherichia coli strain cydB has elevated levels of the AppBC cytochrome bd-II terminal oxidase
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C127S
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the substitution prevents oxidative inactivation of alternative oxidase and renders the protein insensitive to pyruvate activation, the mutated protein is instead activated specifically by succinate
C78A
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the mutant shows significant (418%) stimulation by 5 mM succinate and little response to 5 mM pyruvate
C78D
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the mutant is significantly stimulated (28%) by 5 mM succinate, pyruvate has no significant effect on the mutant enzyme activity
C78E
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the mutant is significantly stimulated (37%) by 5 mM succinate
C78K
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the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78L
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inactive
C78Q
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inactive
C78R
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the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78S
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the mutant is significantly (489%) stimulated by 5 mM succinate
F215L
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the mutant exhibits 1.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
G303E
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the mutant exhibits 4.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219I
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the mutant exhibits 1.4fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219V
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the mutant exhibits 1.7fold resistance to salicylhydroxamic acid compared to the wild type enzyme
D188A
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site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme, The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase
D188N
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site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme
D75E
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows similar activity compared to the wild-type enzyme
D75H
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75N
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75R
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98N
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98S
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-100 compared to the wild-type enzyme
H98T
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
Q101N
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R257Q
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site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme. The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase
R71D
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71D/D75R
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71K
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71Q
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site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
WI36A
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme
C99S
-
the substitution prevents oxidative inactivation of alternative oxidase and renders the protein insensitive to pyruvate activation, the mutated protein is instead activated specifically by succinate
C172A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
E217A
-
the mutation results in the loss of AOX activity
E270N
-
the mutation results in the loss of AOX activity
T179A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
W206F
site-directed mutagenesis, inactive mutant
W206Y
site-directed mutagenesis, inactive mutant
Y275F
-
the mutant exhibits barely detectable mitochondrial antimycin-resistant respiratory activity
Y299F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H261A
-
the mutant shows 5% activity compared to the wild type enzyme
N247Q
-
the mutant shows 96% activity compared to the wild type enzyme
Q242N
-
the mutant shows 6% activity compared to the wild type enzyme
R262K
-
the mutant shows 6% activity compared to the wild type enzyme
S256T
-
the mutant shows 7% activity compared to the wild type enzyme
Y253A
-
the mutant shows 28% activity compared to the wild type enzyme
Y253F
-
the mutant shows 61% activity compared to the wild type enzyme
H261A
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the mutant shows 5% activity compared to the wild type enzyme
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N247Q
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the mutant shows 96% activity compared to the wild type enzyme
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Q242N
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the mutant shows 6% activity compared to the wild type enzyme
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Y253A
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the mutant shows 28% activity compared to the wild type enzyme
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Y253F
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the mutant shows 61% activity compared to the wild type enzyme
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A216L
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
A216N
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
E213A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
E215A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
L122A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
L122N
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
R118A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
R118Q
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
T219V
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
Y220F
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
Y246A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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