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drug target
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the development of AOX-targeting antifungal agents against Moniliophthora perniciosa is an important outcome for the chocolate industry
drug target
validated as a drug target against trypanosomes
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
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the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
evolution
the enzyme is found in mitochondria of all higher plants studied to date
evolution
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the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
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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
malfunction
Glycine max antisense lines for AOX2b result in a decrease in photosynthesis rates, altered fertility, and slower vegetative growth
malfunction
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inhibition of enzyme (AOX) activity by salicylhydroxamic acid signficantly alters the capacity of the fungus to grow and sporulate
malfunction
over 7000 genes, encoding proteins involved in antioxidant and other functions, are significantly altered in AOX1a knockout plants
malfunction
overexpression of PpAOX disturbes redox homeostasis in chloroplasts
malfunction
the deletion mutant strain is more sensitive than wild-type cells to high light under mixotrophic and photoautotrophic conditions
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
metabolism
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alternative oxidase is a key enzyme for cyanide-resistant respiration
metabolism
AOX isoforms from Arabidopsis are differentially fine-regulated by tricarboxylic acid cycle metabolites
metabolism
AOX isoforms from Arabidopsis are differentially fine-regulated by tricarboxylic acid cycle metabolites. Expression of isoenzyme AOX1D is increased in aox1a knockout mutants from Arabidopsis (especially after restriction of the cytochrome c pathway) but cannot compensate for the lack of AOX1A, suggesting a difference in the regulation of these isoforms
metabolism
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expression of alternative oxidase (AOX) is able to promote cell migratory behavior in two different models: in Drosophila, AOX expression corrects thoracic closure defects produced by impaired signaling at several steps in the JNK pathway, while AOX-expressing immortalized mouse embryonic fibroblasts but not primary mouse embryonic fibroblasts show enhanced migration, which is abolished by JNK inhibitor V. AOX was unable to correct cell migration defects resulting from downregulation of the main JNK substrate, the c-Jun subunit of AP-1, or by manipulation of other factors, such as the AP-1 downstream target puc or the pnr transcription factor
metabolism
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the AOX pathway could influence chloroplast energy metabolism and is essential for the maintenance of photosynthetic carbon assimilation in pepper leaves under normal conditions. Drought induces upregulation of the AOX pathway, which plays an important role in protection against drought-induced photoinhibition. The AOX pathway could optimize carbon assimilation and PSII function in plants experiencing drought, which could help avoid overreduction of PSII. Inhibition of AOX pathway could be compensated by increasing the thermal energy dissipation and cyclic electron flow around PSI (CEF-PSI) under drought stress, and the compensation of CEF-PSI is especially significant
physiological function
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AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol 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
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cytochrome bo3 oxidase catalyzes the 2-electron oxidation of ubiquinol-8 and the 4-electron reduction of dioxygen to water
physiological function
the alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase
physiological function
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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
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enzyme signaling regulates the greening process
physiological function
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plastid signals enhance plant cold stress tolerance mainly through the induction of the gene AOX1a
physiological function
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the alternative oxidase pathway plays an important role in the sodium nitroprusside-elevated resistance of Medicago to salt stress
physiological function
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the enzyme is central for metabolic heat-production
physiological function
the enzyme is required for the N gene-mediated resistance to Tobacco mosaic virus
physiological function
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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
AOX1a is involved in adaptation to As(V)-induced oxidative stress
physiological function
critical enzyme for the respiration of bloodstream forms of trypanosomes
physiological function
the alternative oxidase (AOX) pathway is the most effective pathway in maintaining cellular redox and energy balance, especially under stress conditions, including light stress
physiological function
the alternative oxidase (AOX) pathway is the most effective pathway in maintaining cellular redox and energy balance, especially under stress conditions, including light stress
physiological function
the alternative oxidase (AOX) pathway is the most effective pathway in maintaining cellular redox and energy balance, especially under stress conditions, including light stress. AOX dissipates excess reductants produced in the chloroplasts, and thereby prevents photooxidation
physiological function
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the alternative oxidase (AOX) pathway is the most effective pathway in maintaining cellular redox and energy balance, especially under stress conditions, including light stress. The alternative oxidase in the regulation of cellular homeostasis during development of photosynthetic function in greening leaves
physiological function
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the AOX pathway plays an important role in photoprotection in Malus hupehensis leaves under drought stress
physiological function
the Chlamydomonas AOX proteins (CrAOX1 and CrAOX2) can participate in acclimation of Chlamydomonas reinhardtii cells to excess absorbed light energy
physiological function
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the enzyme (AOX) is determinant for growth and sporulation. It participates in life cycle control in Blastocladiella emersonii
physiological function
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the enzyme (MpAOX) is crucial for survival the fungal pathogen Moniliophthora perniciosa (causal agent of the witches' broom disease of cocoa)
physiological function
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the enzyme is important for plant growth and performance under a variety of stress or adverse growth conditions
physiological function
the enzyme is important for plant growth and performance under a variety of stress or adverse growth conditions. During severe or prolonged mild drought stress in, the amount of AOX protein is important to maintain photosynthetic performance. Enzyme form AOX1a is under strong transcriptional suppression
physiological function
the enzyme is required for optimal photosynthesis and growth, and gametophyte development
physiological function
the enzyme participates in plant salt tolerance in Physcomitrella patens and there is a functional link between mitochondria and chloroplast under challenge conditions
physiological function
the enzyme plays a central role in metabolism through facilitating the turnover of the TCA cycle whilst reducing ROS production
physiological function
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the enzyme plays an essential role in ethylene-induced drought tolerance and also played important roles in mediating autophagy generation via balancing ROS level
physiological function
the enzyme reduces stress in Aliivibrio fischeri cells exposed to nitric oxide
physiological function
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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
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physiological function
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AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation
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additional information
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analysis of a one-site Q-site model and a two-site Q-site model, overview
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
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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 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
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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
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the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
additional information
AOX1c is not affected by As(V) treatments (0.1, 0.2 or 0.3 mM)
additional information
AOX1c is not affected by As(V) treatments (0.1, 0.2 or 0.3 mM)
additional information
AOX1c is not affected by As(V) treatments (0.1, 0.2 or 0.3 mM)
additional information
AOX1c is not affected by As(V) treatments (0.1, 0.2 or 0.3 mM)
additional information
AOX1c is not affected by As(V) treatments (0.1, 0.2 or 0.3 mM)
additional information
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developmental arrest in Drosophila melanogaster caused by mitochondrial DNA replication defects cannot be rescued by xenotopic expression of the alternative oxidase (AOX) from Ciona intestinalis. AOX does not rescue developmental lethality, nor alter the biochemical and molecular parameters associated with Twinkle and pol gamma mutations or knockdown. This restricts the potential therapeutic use of AOX to specific types of mitochondrial dysfunction
additional information
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the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
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