Information on EC 1.8.3.1 - sulfite oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.8.3.1
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RECOMMENDED NAME
GeneOntology No.
sulfite oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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additional information
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the enzyme also functions as a selenite oxidase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfide oxidation IV (metazoa)
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sulfite oxidation IV
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sulfate reduction
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Sulfur metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
sulfite:oxygen oxidoreductase
A molybdohemoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-38-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
kenaf
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Manually annotated by BRENDA team
pacific hake
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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M4MVJ1
UniProt
Manually annotated by BRENDA team
DSMZ 10014; strain DSMZ 10014
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
selenite + ferricyanide + H2O
? + ferrocyanide
show the reaction diagram
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approximately 5% of the observed sulfite activity
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?
SO32- + H2O + 2 Fe(III)cytochrome c
SO42- + 2 Fe(II)cytochrome c + 2 H+
show the reaction diagram
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?
SO32- + H2O + 2 ferricyanide
SO42- + 2 ferrocyanide + 2 H+
show the reaction diagram
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?
SO32- + H2O + 2 ferricytochrome c
SO42- + 2 ferrocytochrome c + 2 H+
show the reaction diagram
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?
SO32- + H2O + O2
SO42- + H2O2
show the reaction diagram
sodium sulfite + H2O + A
NaSO42- + AH2
show the reaction diagram
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?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
sulfite + ferricyanide + H+
sulfate + reduced ferricyanide
show the reaction diagram
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
sulfite + H2O + ferricyanide
sulfate + ferrocyanide
show the reaction diagram
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ir
sulfite + H2O + O2
sulfate + hydrogen peroxide
show the reaction diagram
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?
sulfite + O2
sulfate + H2O
show the reaction diagram
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?
sulfite + O2
sulfate + H2O2
show the reaction diagram
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?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
sulfite + O2 + H2O
sulfate + hydrogen peroxide
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
additional information
?
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the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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cytochrome c
Molybdenum
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molybdoenzyme
molybdenum cofactor
molybdopterin
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
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equatorial coordination of chloride in the enzyme. Chloride in low pH sulfite oxidase can only be weakly coordinated to the axial position, trans to the oxo ligand
Iron
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K+
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45-100 mM, 54-88% increase of activity
Molybdenum
NaCl
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up to a concentration of 100 mM, up to 2fold activation
NH4+
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30 mM, 74% increase of activity
Sodium arsenate
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up to a concentration of 5 mM, up to 2fold activation
additional information
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the SO Moco binding domain has the ability to oxidize sulfite in the presence of artificial electron acceptors like ferricyanide. The two-electron oxidation of sulfite to sulfate occurs at the molybdenum site, which is reduced from Mo(VI) to Mo(IV), followed by intramolecular electron transfer to the cytb5 site, with cytochrome c serving as the terminal electron acceptor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
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EDC
2,6-dichloroindophenol
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inhibition of O2 consumption
arsenate
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100 mM, EPR spectra
arsenite
cytochrome c
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inhibition of O2 consumption
Diethylpyrocarbonate
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modifies ten His per enzyme molecule
EDTA
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20 mM, 50% inhibition
ferricyanide
Heavy metal ions
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imidazole
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0.1 mM, complete inhibition
K2HPO4
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at 26 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
K2SO4
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at 22 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KF
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at 72 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNCS
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at 57 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
mannitol
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only with O2 as electron acceptor
methylene blue
N-bromosuccinimide
N-cyclohexyl-N'-[2-(N-methylmorpholino)-ethyl]carbodiimide p-toluene sulfonate
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CMC
N-ethyl-5-phenylisoxazolium-3'-sulfonate
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Woodward's reagent K
Ni2+
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stronger inhibition at pH 7.0 than at pH 3.0
NiCl2
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0.1 mM, complete inhibition
p-chloromercuribenzoate
phosphate
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100 mM, EPR spectra
potassium nitrate
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50% inhibition at 1 mM, in Tris/HCl 20 mM, pH 8.5
potassium phosphate
RNAi
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Sodium arsenate
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7 mM, 50% inhibition
Sodium sulfate
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20 mM, 50% inhibition
sodium sulfite
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a high initial concentration of sodium sulfite decreases dramatically the enzyme expression
sodium tungstate
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at pH 7.5 sodium tungstate inhibits enzyme activity as follows: 1 mM 8% inhibition, 3 mM 36% inhibition, 10 mM 49% inhibition, 50 mM complete inhibition, stronger inhibition at pH 7.0 than at pH 3.0
Tris-acetate
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80 mM, pH 8.0, 50% inhibition
Tris-HCl
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100 mM, pH 8.0, 50% inhibition
Tris/HCl
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50% inhibition at 90 mM, pH 8.5
tungstate
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treatment with sodium tungstate, leading to a catalytically inactive analogue by replacing molybdenum with tungsten in molybdenum cofactor because of its higher affinity constant. Determination of tolerance and impact of different concentrations of tungstate on the viability of HepG2 cells using a luciferase-based cytotoxicity assay, sodium tungstate is nontoxic up to 1000 ppm
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
Di-(carboxamidomethyl)molybdopterin
glycine
Molybdenum
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the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
sodium deoxycholate
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at 0.04%, acceptor: cytochrome c
Tris-acetate
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up to a concentration of 70 mM, up to 2fold activation
Tris-HCl
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up to a concentration of 70 mM, up to 2fold activation
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043 - 0.107
cytochrome c
0.698
ferricyanide
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0.015
O2
0.00046 - 418
sulfite
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34 - 85
cytochrome c
0.14 - 4500
sulfite
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00047 - 27000
sulfite
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0162
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crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.0322
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crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.1006
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crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.1457
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crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.191
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crude cell extract
0.2032
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crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.4036
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9.2
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; crude extract
56.67
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after 297fold purification
188
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20fold purified enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
6 - 11
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pH dependence of the maximum catalytic oxidation current at the GC/HSO electrode with 4 mM sulfite and in the presence of 10 mM [Fe(tacn)]23+ in 100 mM mixed buffer solution, overview
7
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below: less than 50% of maximal activity
additional information
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presence of coordinated sulfate in the sulfite reduced low-pH form of the plant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.64
sequence calculation
8.18
sequence calculation
8.43
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sequence calculation
8.8
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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little expression
Manually annotated by BRENDA team
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perpheral blood, little expression
Manually annotated by BRENDA team
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leucocyte, little expression
Manually annotated by BRENDA team
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substantial expression
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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substantial expression
Manually annotated by BRENDA team
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little expression
Manually annotated by BRENDA team
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little expression
Manually annotated by BRENDA team
additional information