1.8.3.1: sulfite oxidase
This is an abbreviated version!
For detailed information about sulfite oxidase, go to the full flat file.
Word Map on EC 1.8.3.1
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1.8.3.1
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molybdenum
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sulfur
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xanthine
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heme
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thiosulfate
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moco
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epr
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seizures
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molybdopterin
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molybdoenzymes
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sulfur-containing
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tungsten
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molybdenum-containing
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pterin
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s-sulfocysteine
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soxs
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sulfurtransferase
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ectopia
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low-ph
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pyranopterins
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lentis
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dithiolene
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amidoxime
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eseem
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hyperfine
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food industry
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agriculture
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high-ph
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analysis
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oxidase-deficient
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medicine
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xanthinuria
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marc
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molecular biology
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encephalomalacia
- 1.8.3.1
- molybdenum
- sulfur
- xanthine
- heme
- thiosulfate
- moco
- epr
- seizures
- molybdopterin
-
molybdoenzymes
-
sulfur-containing
- tungsten
-
molybdenum-containing
- pterin
- s-sulfocysteine
- soxs
- sulfurtransferase
-
ectopia
-
low-ph
-
pyranopterins
- lentis
-
dithiolene
-
amidoxime
-
eseem
-
hyperfine
- food industry
- agriculture
-
high-ph
- analysis
-
oxidase-deficient
- medicine
-
xanthinuria
-
marc
- molecular biology
- encephalomalacia
Reaction
Synonyms
At-SO, AtSOX, CG7280, HSO, NIA, oxidase, sulfite, PSO, Shopper, SO, SorT, SOX, sulfite oxidase, sulfite oxidase homologue, sulfite: acceptor oxidoreductase, sulfite:acceptor oxidoreductase, sulfite:oxygen oxidoreductase, sulphite oxidase cytochrome b9, SUOX, YedY, YedYZ, ZmSO
ECTree
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General Information
General Information on EC 1.8.3.1 - sulfite oxidase
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malfunction
metabolism
physiological function
additional information
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defects in the enzyme cause a severe infant disease leading to early death with no efficient or costeffective therapy in sight
malfunction
in humans, sulfite oxidase deficiency is one of the most accepted causes of sulfite hypersensitivity and toxicity. A congenital deficiency of sulfite oxidase can cause an excessive accumulation of sulfite and lead to early death in infancy (usually between 2 and 6 years of age), or in neonatal cases, neurological abnormalities, mental retardation, intractable seizures, and ocular lens dislocation. Molybdenum cofactor deficiency, which compromises sulfite oxidase activity, results in profound mental retardation, brain damage, microcephaly, and spasticity. It has also been suggested that hypoxic-ischemic encephalopathy is due to molybdenum cofactor deficiency
malfunction
R309H and K322R mutations are responsible for isolated sulfite oxidase deficiency
malfunction
silencing of ZmSO could lead to seed germination delay upon sulfite exposure, but not under normal conditions
malfunction
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the imbalanced sulfite level resulting from sulfite oxidase impairment confers a metabolic shift towards elevated reduced S-compounds, namely sulfide, S-amino acids (S-AA), Co-A and acetyl-CoA, followed by non-S-AA, nitrogen and carbon metabolite enhancement, including polar lipids. Exposing mutant plants to dark-induced carbon starvation result in a higher degradation of S-compounds, total AA, carbohydrates, polar lipids and total RNA in the mutant plants. Significantly, a failure to balance the carbon backbones is evident in the mutants, indicated by an increase in tricarboxylic acid cycle (TCA) cycle intermediates, whereas a decrease is shown in stressed wild-type plants. Sulfite oxidase deficiency is not necessarily lethal, unless other sulfite network enzymes are down-regulated or the capacity of the sulfite network enzymes in sulfite detoxification is exceeded. Sulfite oxidase mutation affects carbon metabolism in normal and dark-stressed plants. Extended dark stress leads to enhanced degradation of organic nitrogen, elevated ammonium and preference for lower C/N ratio metabolites in the sulfite oxidase mutants as compared with the wild-type plants. Phenotype, detailed overview
malfunction
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enzyme absence confers reduced biomass accumulation in Arabidopsis plants exposed to carbon starvation. Enzyme impairment leads to a reduced sulfur reduction pathway under sucrose depletion and reduced biomass accumulation in plants grown on excess carbon supply
malfunction
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enzyme knockdown animals move less resulting from a reduced peristalsis efficacy
malfunction
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impairment in enzyme activity results in enhanced water consumption
malfunction
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impairment in enzyme activity results in enhanced water consumption
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the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
during extended dark, sulfite oxidase activity is enhanced in tomato wild-type leaves, while the other sulfite network components are down-regulated. RNA interference treated plants accumulate sulfite, resulting in leaf damage and mortality. Exogenous sulfite application induces up-regulation of the sulfite scavenger activities in dark-stressed or unstressed wild-type plants, while expression of the sulfite producer, adenosine 5'-phosphosulfate reductase, is down-regulated. Unstressed or dark-stressed wild-type plants are resistant to sulfite applications, but enzyme RNA interference plants show sensitivity and overaccumulation of sulfite. Under extended dark stress, SO activity is necessary to cope with rising endogenous sulfite levels. Under nonstressed conditions, the sulfite network can control sulfite levels in the absence of enzyme activity
physiological function
enzyme is able to couple efficiently to a cytochrome c isolated from the same organism despite being unable to efficiently reduce horse heart cytochrome c. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene. The pseudoazurin may act as an intermediate electron shuttle between. The protein system appears to couple directly to the respiratory chain, most likely to a cytochrome oxidase
physiological function
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enzyme-deficient mutants are consistently negatively affected upon SO2 exposure at 600 nl/l for 60 h and show phenotypical symptoms of injury with small necrotic spots on the leaves. The mean g(H2O) is reduced by about 60% over the fumigation period, accompanied by a reduction of net CO2 assimilation and SO2 uptake of about 50 and 35%, respectively. Sulfur metabolism is completely distorted. Whereas sulfate pool is kept constant, thiol-levels strongly increase
physiological function
sulfite is detoxified in the liver and lung to sulfate by sulfite oxidase (SO), a molybdenum dependent mitochondrial enzyme. The enzyme ensures that intracellular levels of the sulfite ion remain at acceptably low levels. Sulfite oxidation is the final step in the metabolism of sulfur derived from sulfur containing amino acids. SO catalyzes the oxidation of endogenous or exogenous sulfite to sulfate, which is excreted in to the urine
physiological function
sulfite oxidase (SO) is an essential molybdoenzyme for humans, catalyzing the final step in the degradation of sulfur-containing amino acids and lipids, which is the oxidation of sulfite to sulfate
physiological function
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sulfite oxidase activity is essential for normal sulfur, nitrogen and carbon metabolism in tomato leaves. The enzyme is a key player in protecting plants against exogenous toxic sulfite. And the enzyme activity is essential to cope with rising dark-induced endogenous sulfite levels in tomato plants. The role of sulfite oxidase is not limited to a rescue reaction under elevated sulfite, but sulfite oxidase is a key player in maintaining optimal carbon, nitrogen and sulfur metabolism in tomato plants
physiological function
sulfite oxidase detoxifies sulfite by oxidizing it to sulfate, which detoxifies sulfite by oxidizing it to sulfate. This reaction is the terminal step in the biological sulfur cycle in many organisms, including humans
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
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sulfite oxidase is a mitochondria-located molybdenum-containing enzyme catalyzing the oxidation of sulfite to sulfate in the amino acid and lipid metabolism. It plays a major role in detoxification processes. It catalyzes the oxidation of sulfite to sulfate using ferricytochrome c as the physiological electron acceptor. This reaction is biologically essential as the final step in the catabolism of sulfur-containing amino acids cysteine and methionine. SuOx functions in detoxifying exogenously supplied sulfite and sulfur dioxide (e.g., pollution, preservatives)
physiological function
sulfite oxidase plays an important role in sulfite metabolism by catalyzing the physiologically vital oxidation of sulfite to sulfate in plants. Sulfite oxidase is essential for timely germination of maize seeds upon sulfite exposure, seed germination is inhibited by sulfite. Embryonic sulfite oxidase might be essential for timely seed germination upon sulfite exposure in maize
physiological function
sulfite oxidase significantly contributes to hypoxic nitrite signaling as demonstrated by activation of the canonical NO-sGCcGMP pathway
physiological function
enzyme overexpression improves drought tolerance in tobacco. Enzyme-overexpressing transgenic plants show higher sulfate and glutathione (GSH) levels but lower hydrogen peroxide and malondialdehyde contents under drought stress, indicating that the enzyme confers drought tolerance by enhancing GSH-dependent antioxidant system that scavenges reactive oxygen species and reduces membrane injury. In addition, the transgenic plants exhibit more increased stomatal response than the wild type to water deficit
physiological function
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the enzyme is specifically required for larval locomotion control in ensheathing glia to regulate head bending and peristalsis
physiological function
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the enzyme plays an important role in sulfite homeostasis and stomatal closure
physiological function
the enzyme serves as an anti-viral factor through sequestering Turnip crinkle virus coat protein for binding with Argonaute 1 and confers virus resistance
physiological function
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the role of the enzyme is not limited to protection against elevated sulfite toxicity but to maintaining optimal carbon and sulfur metabolism in Arabidopsis plants
physiological function
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the enzyme plays an important role in sulfite homeostasis and stomatal closure
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the catalytic site of SO consists of a molybdenum ion bound to the dithiolene sulfurs of one molybdopterin (MPT) molecule, carrying two oxygen ligands, and is further coordinated by the thiol sulfur of a conserved cysteine residue
additional information
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the catalytic site of SO consists of a molybdenum ion bound to the dithiolene sulfurs of one molybdopterin (MPT) molecule, carrying two oxygen ligands, and is further coordinated by the thiol sulfur of a conserved cysteine residue
additional information
three-dimensional modeling and structure-based phylogeny
additional information
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three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny
additional information
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three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny
additional information
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three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview
additional information
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three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview