HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.10.3.11 - ubiquinol oxidase (non-electrogenic)
for references in articles please use BRENDA:EC1.10.3.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.10.3.11 ubiquinol oxidase (non-electrogenic)IUBMB Comments
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.
Specify your search results
Word Map
- 1.10.3.11
-
salicylhydroxamic
- antimycin
- oxidases
- chloroplast
-
sham
- succinate
- ubiquinone
- nicotiana
- brucei
-
trypanosome
- quinols
- tabacum
- kcn
-
thermogenic
-
photosystem
-
rotenone-insensitive
- rotenone
-
energy-dissipating
-
non-phosphorylating
-
thermogenesis
-
protist
- intestinalis
-
diiron
- anserina
-
cyanide-sensitive
-
podospora
- ciona
-
photorespiratory
-
over-reduction
- azoxystrobin
-
photoinhibition
- castellanii
-
acid-sensitive
- maculatum
-
pentatricopeptide
-
photorespiration
-
benzohydroxamic
-
havana
-
sa-induced
-
poise
- anomala
- myxothiazol
-
plant-like
-
high-light
-
strobilurins
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alternative oxidase, alternative oxidase 1a, AOX, AOX1, AOX1a, AOX2b1, AOX3, AppBC, CIO, CioAB, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alternative oxidase
AOX
AOX1a
AppBC
CIO
CioAB
cyanide-insensitive alternative oxidase
cyanide-insensitive oxidase
cyanide-insensitive quinol oxidase
cyanide-insensitive terminal quinol oxidase
cyanide-resistant alternative oxidase
cytochrome bb3 oxidase
-
-
-
-
plant alternative oxidase
-
-
-
-
TAO
cyanide-insensitive oxidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
-
-
-
-
2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
modified ping-pong bi-bi mechanism
-
2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
modified ping-pong bi-bi mechanism
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2 ubiquinol-8 + O2
2 ubiquinone-8 + 2 H2O
-
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
-
-
?
2 ubiquinol + O2
2 ubiquinone + 2 H2O
ubiquinol binding model, overview. During the sequential electron reduction process, following the activation of oxygen, free radicals are generated on a tightly bound ubiquinol and Tyr220
-
-
?
ubiquinol + O2
ubiquinone + H2O
-
a non-proton-pumping ubiquinol oxidase that catalyzes the fourelectron reduction of dioxygen to water
-
-
?
ubiquinol + O2
ubiquinone + H2O
-
a non-proton-pumping ubiquinol oxidase that catalyzes the fourelectron reduction of dioxygen to water
-
-
?
additional information
?
-
-
the enzyme is able to oxidize both reduced cytochrome c and ubiquinol
-
-
-
additional information
?
-
the enzyme is able to oxidize both reduced cytochrome c and ubiquinol
-
-
-
additional information
?
-
-
two assay methods: a coupled assay with rat liver DT-diaphorase and NADH as the reductant, and a direct assay using a oxygen electrode, overview
-
-
-
additional information
?
-
-
the enzyme is unable to use NADH as respiratory substrate
-
-
-
additional information
?
-
-
the enzyme is unable to use NADH as respiratory substrate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
heme b558, heme b595 and heme d; heme b558, heme b595 and heme d
heme
-
the enzyme contains reduced hemes b and of oxygenated and ferric heme d, differing from cytochrome bd. Heme d serves as the ligand-binding site of CIO
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
the enzyme is a diiron carboxylate protein, the nonheme diiron carboxylate active site is buried within a four-helix bundle. The structure of the diiron active site was refined as an oxidized Fe(III)-Fe(III) form with a single hydroxo-bridge
Iron
-
the enzyme possesses a hydroxo-bridged di-iron center in the active site
Iron
-
the enzyme possesses a hydroxo-bridged di-iron center in the active site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
-
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
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
aurachin C 1-10
15% residual activity at 0.005 mg/ml; 15% residual activity at 0.005 mg/ml
aurachin C1-10
-
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
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
Piericidin A
14% residual activity at 0.005 mg/ml; 14% residual activity at 0.005 mg/ml
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
ascofuranone
-
specifically inhibits the quinol oxidase activity of TAO
cyanide
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration; quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration
ubiquinol
-
AOX is inactivated by its product ubiquinol during catalysis, this inhibition is prevented in the presence of pyruvate. The inhibition can be reversed by a reductive process, achieved by high levels of reduction of the ubiquinone-pool or by dithiothreitol
ubiquinol
-
AOX is inactivated by its product ubiquinol during catalysis, this inhibition is prevented in the presence of pyruvate. The inhibition can be reversed by a reductive process, achieved by high levels of reduction of the ubiquinone-pool or by dithiothreitol
additional information
-
the enzyme is cyanide- and antimycin-resistant
-
additional information
-
presence of high affinity inhibitors, 2-heptyl-4-hydroxyquinoline N-oxide and aurachin C1–10, does not displace ubiquinone-8 from the QH site
-
additional information
-
not inhibited by ascofuranone; not inhibited by ascofuranone
-
additional information
not inhibited by ascofuranone; not inhibited by ascofuranone
-
additional information
-
CIO activity is much more resistant to cyanide, compared with Escherichia coli cytochrome bd, but sensitive to azide
-
additional information
-
the respiratory activity exhibited by mitochondria containing the wild type AOX is partially resistant to antimycin A (about 18% of the NADH-dependent rate)
-
additional information
-
the enzyme is cyanide- and antimycin-resistant
-
additional information
inhibitor binding induces the ligation of a histidine residue in the active site, inhibitor binding site and structures, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-malate
-
in whole mitochondria, L-malate stimulates respiration via alternative oxidase in a pH- (and NAD+)-dependent manner
succinate
-
in whole mitochondria, succinate (in the presence of malonate) stimulates respiration via alternative oxidase in a pH- (and NAD+)-dependent manner
EDT-20
-
the addition of 0.025% (v/v) EDT-20 in the assay increases the activity 3-4fold
-
EDT-20
-
the addition of 0.025% (v/v) EDT-20 in the assay increases the activity 3-4fold
-
pyruvate
-
the alternative oxidase is 50% activated at a concentration of 0.1 mM pyruvate
pyruvate
-
the wild type enzyme activity is significantly stimulated (122%) by 5 mM pyruvate
pyruvate
-
AOX is activated when the ubiquinone-pool becomes highly reduced in the presence of pyruvate. The enzyme is not activated when pyruvate is added after a transient high reduction level of the Q-pool, but is when pyruvate is added before the transient reduction. In the presence of pyruvate, NADH and succinate oxidation can stimulate AOX activity by substituting for dithiothreitol
pyruvate
-
potent activator, its presence is essential for maximum activity, pyruvate increases the activity of AOX but does not increase its affinity for its substrate
pyruvate
-
AOX is activated when the ubiquinone-pool becomes highly reduced in the presence of pyruvate. The enzyme is not activated when pyruvate is added after a transient high reduction level of the Q-pool, but is when pyruvate is added before the transient reduction. In the presence of pyruvate, NADH and succinate oxidation can stimulate AOX activity by substituting for dithiothreitol
pyruvate
-
potent activator, its presence is essential for maximum activity, pyruvate increases the activity of AOX but does not increase its affinity for its substrate
pyruvate
-
half-maximal stimulation of alternative oxidase by pyruvate occurs at less than 0.005 mM in submitochondrial particles, one twentieth of that in whole mitochondria
additional information
-
AOX is not stimulated by lactate, phosphoenolpyruvate, propionate, acetate, glycine, L-alanine, crotonate, acrylate, acetoacetate, malonate, fumarate, oxalate, tartrate, D-malate, citrate, and isocitrate; in submitochondrial particle preparations with negligible malic enzyme activity, neither L- nor D-malate stimulate alternative oxidase activity
-
additional information
-
alternative oxidase activity is not stimulated by pyruvate and glyoxylate. Pyruvate does only stimulate activity when succinate is the respiratory substrate but this is not a direct effect on the alternative oxidase
-
additional information
-
alternative oxidase activity is not stimulated by pyruvate and glyoxylate. Pyruvate does only stimulate activity when succinate is the respiratory substrate but this is not a direct effect on the alternative oxidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
0.0046
O2
mutant T179A, pH and temperature not specified in the publication
0.0092
O2
mutant C172A, pH and temperature not specified in the publication
0.017
O2
mutant Y299F, pH and temperature not specified in the publication
0.018
O2
wild-type enzyme, pH and temperature not specified in the publication
0.0205
O2
mutant Y253F, pH and temperature not specified in the publication
0.0403
ubiquinol-1
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.1153
ubiquinol-1
-
in the presence of EDT-20 (0.025%) and pyruvate, 0.3 M succinate, 25 mM TES, 10 mM potassium phosphate, and 2 mM magnesium sulfate, pH 7.0, at 25°C
0.331
ubiquinol-1
-
in the presence of EDT-20 (0.025%) and pyruvate, 0.3 M succinate, 25 mM TES, 10 mM potassium phosphate, and 2 mM magnesium sulfate, pH 7.0, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000074
2-heptyl-4-hydroxyquinoline N-oxide
-
pH 7.0, 37°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
2-Heptyl-4-hydroxyquinoline-N-oxide
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C 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
pH and temperature not specified in the publication
0.017
antimycin A
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00004
aurachin C 1-10
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.04
Gramicidin S
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.013
LL-Z1272gamma
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.0007
Piericidin A
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5); at 25°C in 50 mM potassium phosphate (pH 6.5)
0.008
cyanide
Gluconobacter oxydans
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 0.013 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5); quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 0.013 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5)
13
cyanide
Gluconobacter oxydans
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 13 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5); quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 13 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00007
octyl gallate
Sauromatum venosum
mutant Y299F, pH and temperature not specified in the publication
0.00008
octyl gallate
Sauromatum venosum
mutants C172A and T179A, pH and temperature not specified in the publication
0.00009
octyl gallate
Sauromatum venosum
wild-type enzyme, pH and temperature not specified in the publication
0.0001
octyl gallate
Sauromatum venosum
mutant Y253F, pH and temperature not specified in the publication
0.00036
propyl gallate
Arabidopsis thaliana
-
mutant enzyme F215L, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00039
propyl gallate
Arabidopsis thaliana
-
mutant enzyme M219V, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C; wild type enzyme, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00042
propyl gallate
Arabidopsis thaliana
-
mutant enzyme M219I, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00044
propyl gallate
Arabidopsis thaliana
-
mutant enzyme G303E, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.042
Salicylhydroxamic acid
Arabidopsis thaliana
-
wild type enzyme, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.057
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme M219I, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.069
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme F215L, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.073
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme M219V, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.194
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme G303E, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.012
sialic acid
Sauromatum venosum
mutant T179A, pH and temperature not specified in the publication
0.016
sialic acid
Sauromatum venosum
wild-type enzyme, pH and temperature not specified in the publication
0.018
sialic acid
Sauromatum venosum
mutant Y299F, pH and temperature not specified in the publication
0.019
sialic acid
Sauromatum venosum
mutant C172A, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
-
recombinant enzyme, in the presence of 10 nM ascofuranone, at 25°C, in 50 mM Tris-HCl (pH 7.4)
0.2
-
recombinant enzyme, in the presence of 10 nM ascofuranone, at 25°C, in 50 mM Tris-HCl (pH 7.4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit II; formerly Gluconobacter suboxydans strain IFO12528. The enzyme from strain 621H is expressed in strain NBRC3172
UniProt
brenda
subunit I, CioA; genes cioA and cioB encoding subunits I and II
-
-
brenda
subunit I; formerly Gluconobacter suboxydans strain IFO12528
-
-
brenda
subunit II; formerly Gluconobacter suboxydans strain IFO12528. The enzyme from strain 621H is expressed in strain NBRC3172
UniProt
brenda
subunit I, CioA; genes cioA and cioB encoding subunits I and II
-
-
brenda
subunit I; formerly Gluconobacter suboxydans strain IFO12528
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highest enzyme expression is in filamentous thalli and is about 10times the expression in the foliose thallus
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytochrome bo3 is the major respiratory oxidase located in the cytoplasmic membrane of Escherichia coli when grown under high oxygen tension
brenda
-
; outer surface of the cytoplasmic membrane
-
brenda
-
the alternative oxidase protein is expressed in the inner mitochondrial membrane in its reduced (active) form
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
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
physiological function
additional information
evolution
the enzyme is found in mitochondria of all higher plants studied to date
evolution
-
the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
evolution
the cytochrome ba3 oxidase belongs to the family B of the heme-copper containing terminal oxidases, heme-copper oxidases use either c-type cytochromes or quinols as electron donors
evolution
-
the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
-
metabolism
-
the alternative oxidase actively competes with the cytochrome pathway for reducing equivalents and contributes up to 24% to the overall respiratory activity
metabolism
-
alternative oxidase is a key enzyme for cyanide-resistant respiration
physiological function
-
cytochrome bo3 oxidase catalyzes the 2-electron oxidation of ubiquinol-8 and the 4-electron reduction of dioxygen to water
physiological function
-
AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation
physiological function
the alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase
physiological function
-
ubiquinol-10 molecules are reoxidized by cytochrome bo3 and CIO, terminal oxidases of the respiratory chain. In the Gluconobacter oxydans respiratory chain, CIO may have a physiological role in compensation for lower activity of cytochrome bo3 under low growth pH to maintain rapid substrate oxidation
physiological function
AOX is a diiron carboxylate protein that catalyzes the four-electron reduction of dioxygen to water by ubiquinol. AOX plays a critical role in the survival of the parasite in its bloodstream form
physiological function
-
the expression of AOX1a in Saccharomyces cerevisiae enhances its respiratory tolerance which, in turn, maintains cellular redox homeostasis and protects from oxidative damage
physiological function
-
the alternative oxidase pathway plays an important role in the sodium nitroprusside-elevated resistance of Medicago to salt stress
physiological function
-
enzyme signaling regulates the greening process
physiological function
-
plastid signals enhance plant cold stress tolerance mainly through the induction of the gene AOX1a
physiological function
the enzyme is required for the N gene-mediated resistance to Tobacco mosaic virus
physiological function
-
the enzyme is central for metabolic heat-production
physiological function
-
AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation
-
physiological function
-
ubiquinol-10 molecules are reoxidized by cytochrome bo3 and CIO, terminal oxidases of the respiratory chain. In the Gluconobacter oxydans respiratory chain, CIO may have a physiological role in compensation for lower activity of cytochrome bo3 under low growth pH to maintain rapid substrate oxidation
-
additional information
-
analysis of a one-site Q-site model and a two-site Q-site model, overview
additional information
-
the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
additional information
-
the enzyme can be reduced by ubiquinol, but it alone can also be reduced by decylubiquinol and N,N,N',N'-tetramethyl-4-phenylenediamine/ascorbate in the presence of cyanide
additional information
the enzyme can be reduced by ubiquinol, but it alone can also be reduced by decylubiquinol and N,N,N',N'-tetramethyl-4-phenylenediamine/ascorbate in the presence of cyanide
additional information
putative ubiquinol binding cavities, overview. The nonheme diiron carboxylate active site is buried within a four-helix bundle. The active site is ligated solely by four glutamate residues in its oxidized inhibitor-free state. Highly conserved Tyr220 iswithin 4 A of the active site and is critical for catalytic activity. The enzyme is a homodimer with two hydrophobic cavities per monomer. Both cavities bind ubiquinol and along with Tyr220 are required for the catalytic cycle for O2 reduction, but also inhibitors bind to one cavity and Tyr220, respectively. A second cavity interacts with the inhibitor-binding cavity at the diiron center. The active site, which is located in a hydrophobic environment deep inside the enzyme molecule, is composed of the diiron center and four glutamate (E123, E162, E213, and E266) and two histidine residues (H165 and H269), all of which are completely conserved
additional information
-
the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
-
Show AA Sequence and Transmembrane Helices (1378 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16800
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry
32000
35000
36000
37813
1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 53583 + 1 * 37813, calculated from amino acid sequence
44000
1 * 54000 + 1 * 44000, SDS-PAGE; 1 * 54000 + 1 * 44000, SDS-PAGE
5200
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry
53583
1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 53583 + 1 * 37813, calculated from amino acid sequence
54000
1 * 54000 + 1 * 44000, SDS-PAGE; 1 * 54000 + 1 * 44000, SDS-PAGE
63900
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
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
heterodimer
1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 54000 + 1 * 44000, SDS-PAGE; 1 * 54000 + 1 * 44000, SDS-PAGE
heterodimer
-
1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 54000 + 1 * 44000, SDS-PAGE
-
heterodimer
-
1 * 53583 + 1 * 37813, calculated from amino acid sequence; 1 * 54000 + 1 * 44000, SDS-PAGE
-
homodimer
with two hydrophobic cavities per monomer. Both cavities bind ubiquinol and along with Tyr220 are required for the catalytic cycle for O2 reduction, but also inhibitors bind to one cavity and Tyr220, respectively. A second cavity interacts with the inhibitor-bindingcavity at the diiron center
additional information
-
subunit composition and structures, overview. No cytochrome bc1 complex subunit
additional information
subunit composition and structures, overview. No cytochrome bc1 complex subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
C78K
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78R
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
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
H98S
-
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
-
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
T179A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
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
Y253F
-
the mutant exhibits a mitochondrial antimycin-resistant respiratory activity that is comparable with that of the wild type
Y253F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells and Saccharomyces cerevisiae strain INVSc1
-
expressed in Escherichia coli strain C41 membranes and in Saccharomyces cerevisiae
expressed in Schizosaccharomyces pombe and Escherichia coli
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
-
wild type and mutant enzymes are expressed in Schizosaccharomyces pombe strain sp.011
-
expressed in Escherichia coli strain C41 membranes and in Saccharomyces cerevisiae
-
expressed in Escherichia coli strain C41 membranes and in Saccharomyces cerevisiae
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cytochrome bd-I-deficient Escherichia coli strain cydB has elevated levels of the AppBC cytochrome bd-II terminal oxidase
the expression of alternative oxidase genes is significantly induced by salt stress (200-400 mM NaCl)
-
the inoculation of Tobacco mosaic virus significantly increases the enzyme transcript and protein levels
cytochrome bd-I-deficient Escherichia coli strain cydB has elevated levels of the AppBC cytochrome bd-II terminal oxidase
-
cytochrome bd-I-deficient Escherichia coli strain cydB has elevated levels of the AppBC cytochrome bd-II terminal oxidase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kido, Y.; Shiba, T.; Inaoka, D.K.; Sakamoto, K.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Moore, A.; Harada, S.; Kita, K.
Crystallization and preliminary crystallographic analysis of cyanide-insensitive alternative oxidase from Trypanosoma brucei brucei
Acta Crystallogr. Sect. F
66
275-278
2010
Trypanosoma brucei brucei, Trypanosoma brucei brucei FN102
brenda
Hoefnagel, M.H.; Wiskich, J.T.
Activation of the plant alternative oxidase by high reduction levels of the Q-pool and pyruvate
Arch. Biochem. Biophys.
355
262-270
1998
Arum italicum, Glycine max
brenda
Umbach, A.L.; Siedow, J.N.
The cyanide-resistant alternative oxidases from the fungi Pichia stipitis and Neurospora crassa are monomeric and lack regulatory features of the plant enzyme
Arch. Biochem. Biophys.
378
234-245
2000
Neurospora crassa, Scheffersomyces stipitis
brenda
Berthold, D.A.
Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid
Biochim. Biophys. Acta
1364
73-83
1998
Arabidopsis thaliana
brenda
Siedow, J.N.; Umbach, A.L.
The mitochondrial cyanide-resistant oxidase: structural conservation amid regulatory diversity
Biochim. Biophys. Acta
1459
432-439
2000
Arabidopsis thaliana
brenda
Umbach, A.L.; Gonzalez-Meler, M.A.; Sweet, C.R.; Siedow, J.N.
Activation of the plant mitochondrial alternative oxidase: insights from site-directed mutagenesis
Biochim. Biophys. Acta
1554
118-128
2002
Arabidopsis thaliana
brenda
Yap, L.L.; Lin, M.T.; Ouyang, H.; Samoilova, R.I.; Dikanov, S.A.; Gennis, R.B.
The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli
Biochim. Biophys. Acta
1797
1924-1932
2010
Escherichia coli
brenda
Albury, M.S.; Elliott, C.; Moore, A.L.
Ubiquinol-binding site in the alternative oxidase: mutagenesis reveals features important for substrate binding and inhibition
Biochim. Biophys. Acta
1797
1933-1939
2010
Schizosaccharomyces pombe, Schizosaccharomyces pombe Sp.011
brenda
Siedow, J.N.; Umbach, A.L.; Moore. A.L.
The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center
FEBS Lett.
362
10-14
1995
Sauromatum venosum
brenda
Djajanegara, I.; Holtzapffel, R.; Finnegan, P.M.; Hoefnagel, M.H.; Berthold, D.A.; Wiskich, J.T.; Day, D.A.
A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation
FEBS Lett.
454
220-224
1999
Arabidopsis thaliana, Glycine max
brenda
Mogi, T.; Ano, Y.; Nakatsuka, T.; Toyama, H.; Muroi, A.; Miyoshi, H.; Migita, C.T.; Ui, H.; Shiomi, K.; Omura, S.; Kita, K.; Matsushita, K.
Biochemical and spectroscopic properties of cyanide-insensitive quinol oxidase from Gluconobacter oxydans
J. Biochem.
146
263-271
2009
Gluconobacter oxydans, Gluconobacter oxydans (Q5FU84), Gluconobacter oxydans 621H (Q5FU84), Gluconobacter oxydans NBRC 3172
brenda
Moore, A.L.; Umbach, A.L.; Siedow, J.N.
Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site
J. Bioenerg. Biomembr.
27
367-377
1995
Arum maculatum, Sauromatum venosum
brenda
Albury, M.S.; Dudley, P.; Watts, F.Z.; Moore, A.L.
Targeting the plant alternative oxidase protein to Schizosaccharomyces pombe mitochondria confers cyanide-insensitive respiration
J. Biol. Chem.
271
17062-17066
1996
Sauromatum venosum
brenda
Affourtit, C.; Albury, M.S.; Krab, K.; Moore, A.L.
Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe
J. Biol. Chem.
274
6212-6218
1999
Sauromatum venosum
brenda
Albury, M.S.; Affourtit, C.; Crichton, P.G.; Moore, A.L.
Structure of the plant alternative oxidase. Site-directed mutagenesis provides new information on the active site and membrane topology
J. Biol. Chem.
277
1190-1194
2002
Sauromatum venosum
brenda
Shepherd, M.; Sanguinetti, G.; Cook, G.M.; Poole, R.K.
Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism
J. Biol. Chem.
285
18464-18472
2010
Escherichia coli, Escherichia coli BW25113
brenda
Sootsuwan, K.; Lertwattanasakul, N.; Thanonkeo, P.; Matsushita, K.; Yamada, M.
Analysis of the respiratory chain in ethanologenic Zymomonas mobilis with a cyanide-resistant bd-type ubiquinol oxidase as the only terminal oxidase and its possible physiological roles
J. Mol. Microbiol. Biotechnol.
14
163-175
2008
Zymomonas mobilis (Q5NM65), Zymomonas mobilis (Q9RH19), Zymomonas mobilis
brenda
Millar, A.H.; Hoefnagel, M.; Day, D.A.; Wiskich, J.T.
Specificity of the organic acid activation of alternative oxidase in plant mitochondria
Plant Physiol.
111
613-618
1996
Ipomoea batatas
brenda
Hoefnagel, M.; Rich, P.R.; Zhang, Q.; Wiskich, J.T.
Substrate kinetics of the plant mitochondrial alternative oxidase and the effects of pyruvate
Plant Physiol.
115
1145-1153
1997
Arum italicum, Glycine max
brenda
Robson, C.A.; Vanlerberghe, G.C.
Transgenic plant cells lacking mitochondrial alternative oxidase have increased susceptibility to mitochondria-dependent and -independent pathways of programmed cell death
Plant Physiol.
129
1908-1920
2002
Nicotiana tabacum
brenda
Williams, B.A.; Elliot, C.; Burri, L.; Kido, Y.; Kita, K.; Moore, A.L.; Keeling, P.J.
A broad distribution of the alternative oxidase in microsporidian parasites
PLoS Pathog.
6
e1000761
2010
Antonospora locustae, Trachipleistophora hominis
brenda
Crichton, P.; Albury, M.; Affourtit, C.; Moore, A.
Mutagenesis of the Sauromatum guttatum alternative oxidase reveals features important for oxygen binding and catalysis
Biochim. Biophys. Acta
1797
732-737
2010
Sauromatum venosum (P22185), Sauromatum venosum
brenda
Miura, H.; Mogi, T.; Ano, Y.; Migita, C.T.; Matsutani, M.; Yakushi, T.; Kita, K.; Matsushita, K.
Cyanide-insensitive quinol oxidase (CIO) from Gluconobacter oxydans is a unique terminal oxidase subfamily of cytochrome bd
J. Biochem.
153
535-545
2013
Gluconobacter oxydans, Gluconobacter oxydans NBRC 3172
brenda
Gao, Y.; Meyer, B.; Sokolova, L.; Zwicker, K.; Karas, M.; Brutschy, B.; Peng, G.; Michel, H.
Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors
Proc. Natl. Acad. Sci. USA
109
3275-3280
2012
Aquifex aeolicus, Aquifex aeolicus (G5DGC8)
brenda
Shiba, T.; Kido, Y.; Sakamoto, K.; Inaoka, D.K.; Tsuge, C.; Tatsumi, R.; Takahashi, G.; Balogun, E.O.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Saimoto, H.; Moore, A.L.; Harada, S.; Kita, K.
Structure of the trypanosome cyanide-insensitive alternative oxidase
Proc. Natl. Acad. Sci. USA
110
4580-4585
2013
Trypanosoma brucei (Q26710), Trypanosoma brucei
brenda
Vishwakarma, A.; Dalal, A.; Tetali, S.D.; Kirti, P.B.; Padmasree, K.
Genetic engineering of AtAOX1a in Saccharomyces cerevisiae prevents oxidative damage and maintains redox homeostasis
FEBS Open Bio
6
135-146
2016
Arabidopsis thaliana
brenda
Zhang, B.; Zhu, D.; Wang, G.; Peng, G.
Characterization of the AOX gene and cyanide-resistant respiration in Pyropia haitanensis (Rhodophyta)
J. Appl. Phycol.
26
2425-2433
2014
Pyropia haitanensis
-
brenda
Jian, W.; Zhang, D.W.; Zhu, F.; Wang, S.X.; Pu, X.J.; Deng, X.G.; Luo, S.S.; Lin, H.H.
Alternative oxidase pathway is involved in the exogenous SNP-elevated tolerance of Medicago truncatula to salt stress
J. Plant Physiol.
193
79-87
2016
Medicago truncatula
brenda
Zhang, D.W.; Yuan, S.; Xu, F.; Zhu, F.; Yuan, M.; Ye, H.X.; Guo, H.Q.; Lv, X.; Yin, Y.; Lin, H.H.
Light intensity affects chlorophyll synthesis during greening process by metabolite signal from mitochondrial alternative oxidase in Arabidopsis
Plant Cell Environ.
39
12-25
2016
Arabidopsis thaliana
brenda
Tang, H.; Zhang, D.; Yuan, S.; Zhu, F.; Xu, F.; Fu, F.; Wang, S.; Lin, H.
Plastid signals induce alternative oxidase expression to enhance the cold stress tolerance in Arabidopsis thaliana
Plant Growth Regul.
74
275-283
2014
Arabidopsis thaliana
brenda
Zhu, F.; Deng, X.G.; Xu, F.; Jian, W.; Peng, X.J.; Zhu, T.; Xi, D.H.; Lin, H.H.
Mitochondrial alternative oxidase is involved in both compatible and incompatible host-virus combinations in Nicotiana benthamiana
Plant Sci.
239
26-35
2015
Nicotiana benthamiana, Nicotiana benthamiana (U5XGW7)
brenda
Sayed, M.A.; Umekawa, Y.; Ito, K.
Metabolic interplay between cytosolic phosphoenolpyruvate carboxylase and mitochondrial alternative oxidase in thermogenic skunk cabbage, Symplocarpus renifolius
Plant Signal. Behav.
11
e1247138
2016
Symplocarpus renifolius
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.10.3.11)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
