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1.10.3.11: ubiquinol oxidase (non-electrogenic)

This is an abbreviated version!
For detailed information about ubiquinol oxidase (non-electrogenic), go to the full flat file.

Word Map on EC 1.10.3.11

Reaction

2 ubiquinol +

O2
= 2 ubiquinone + 2 H2O

Synonyms

alternative oxidase, alternative oxidase 1a, alternative oxidase 1b, alternative oxidases, AOX, AOX1, AOX1a, AOX1b, AOX1C, AOX1D, AOX2, AOX2b, AOX2b1, AOX3, AppBC, AtAOX1A, CIO, CioAB, Cox2, CrAOX1, CrAOX2, cyanide-insensitive alternative oxidase, cyanide-insensitive oxidase, cyanide-insensitive quinol oxidase, cyanide-insensitive terminal quinol oxidase, cyanide-resistant alternative oxidase, cyanide-resistant bd-type ubiquinol oxidase, cyanide-resistant oxidase, cyanide-resistant ubiquinol oxidase, CydA, CydB, cytochrome ba3 oxidase, cytochrome bb3 oxidase, cytochrome bd-II, cytochrome bd-type quinol oxidase, cytochrome bo3, cytochrome bo3 ubiquinol oxidase, heme-copper terminal oxidase, mitochondrial alternative oxidase, MpAOX, plant alternative oxidase, TAO, TAOX, trypanosomal alternative oxidase, ubiquinol:oxygen oxidoreductase

ECTree

     1 Oxidoreductases
         1.10 Acting on diphenols and related substances as donors
             1.10.3 With oxygen as acceptor
                1.10.3.11 ubiquinol oxidase (non-electrogenic)

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C127S
-
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
-
the mutant shows significant (418%) stimulation by 5 mM succinate and little response to 5 mM pyruvate
C78D
-
the mutant is significantly stimulated (28%) by 5 mM succinate, pyruvate has no significant effect on the mutant enzyme activity
C78E
-
the mutant is significantly stimulated (37%) by 5 mM succinate
C78K
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78L
-
inactive
C78Q
-
inactive
C78R
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78S
-
the mutant is significantly (489%) stimulated by 5 mM succinate
F215L
-
the mutant exhibits 1.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
G303E
-
the mutant exhibits 4.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219I
-
the mutant exhibits 1.4fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219V
-
the mutant exhibits 1.7fold resistance to salicylhydroxamic acid compared to the wild type enzyme
D188A
-
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
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme
D75E
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows similar activity compared to the wild-type enzyme
D75H
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75R
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98T
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
Q101N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R257Q
-
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
-
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
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71K
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71Q
-
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
Y253F
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
-
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
-
Y253A
-
the mutant shows 28% activity compared to the wild type enzyme
-
Y253F
-
the mutant shows 61% activity compared to the wild type enzyme
-
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
D100A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 8.8fold lower than the kcat/Km-value of wild-type enzyme
D100E
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 5.7fold lower than the kcat/Km-value of wild-type enzyme
E215A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 34fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
E215D
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 528fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
E215N
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 567fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
L122A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 34.3fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
L212A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 31.2fold lower than the kcat/Km-value of wild-type enzyme
R118A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 22.5fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
R118K
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 19.6fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
R96A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 7.9fold lower than the kcat/Km-value of wild-type enzyme
R96K
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 7.8fold lower than the kcat/Km-value of wild-type enzyme
T219A
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 36.4fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid
T219S
kcat/Km-value of the mutant enzyme for ubiquinol-1 is 89.1fold lower than the kcat/Km-value of wild-type enzyme. No inhibition by ascochlorin, ascofuranone, colletochlorin B, colletochlorin D, octyl-gallate and salicylic hydroxamic acid