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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Cofactor
Cofactor on EC 1.8.3.1 - sulfite oxidase
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cytochrome c
ferric cytochrome c, Fe3+ cyt c, cytochrome c is known to participate in mitochondrial respiration and has antioxidant and peroxidase activities. Fe3+ cyt c might have a role in the deleterious effects of sulfite in biological systems due to increased production of sulfite radical. Mammalian cytochrome c (cyt c) is a small, globular protein that exists in high concentrations in the inner membrane of mitochondria
heme
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interactions of residue H90 with a heme propionate group destabilize the Fe(III) state of the heme
heme
the heme accepts electrons from the Mo ion following sulfite oxidation, a flexible connects the Mo and heme domains
molybdenum cofactor
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Moco, a molybdopterin, in vitro synthesis and activation of sulfite oxidase molybdenum domain, using recombinant MPTsynthase subunit MoaE and Gephyrin C4 splice variant, overview. The molybdenum cofactor is active site bound, structure analysis. During catalysis, molybdenum enzymes pass through the paramagnetic Mo(V) state, metal-dithiolene interactionsare highly covalent
molybdenum cofactor
the heme accepts electrons from the Mo ion following sulfite oxidation, a flexible connects the Mo and heme domains
molybdenum cofactor
the molybdenum cofactor (Moco) is bound in the active site of sulfite oxidase
molybdenum cofactor
three conserved residues (H304, R309, K322) are hydrogen bonded to the phosphate group of the molybdenum cofactor
molybdenum cofactor
the enzyme contains one molybdenum active site per subunit
molybdopterin
SOX enzyme is characterized with both oxidoreductase molybdopterin binding and Moco oxidoreductase dimerization domains
additional information
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the enzyme is lacking the heme domain that is known from vertebrate sulfite oxidase
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additional information
during the sulfite-sulfite oxidase-cytochrome c catalytic cycle, movement between the molybdenum and heme domain is required to enable efficient single-electron transfer from molybdenum via the heme b5 cofactor to cytochrome c. Using phenosafranine or sulfite as reducing substrate, the Mo-domain shows much faster nitrite reduction to NO than holo-sulfite oxidase
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additional information
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during the sulfite-sulfite oxidase-cytochrome c catalytic cycle, movement between the molybdenum and heme domain is required to enable efficient single-electron transfer from molybdenum via the heme b5 cofactor to cytochrome c. Using phenosafranine or sulfite as reducing substrate, the Mo-domain shows much faster nitrite reduction to NO than holo-sulfite oxidase
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additional information
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molybdenum-containing enzymes contain either one or two pyranopterin dithiolate (molybdopterin, MPT) cofactors that coordinate to the metal through the two sulfur atoms of the ene-dithiolate (dithiolene)1 functionality, structure-activity analysis, detailed overview
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additional information
vertebrate sulfite oxidases can use either cytochrome c or dioxygen as an electron acceptor
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