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
1.8.3.1
-
RECOMMENDED NAME
GeneOntology No.
sulfite oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
ping-pong mechanism
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
ping-pong mechanism
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
this direct reduction of O2 is prevented completely in presence of cytochrome c
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
x-ray absorption spectroscopy of oxidation states
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
intramolecular electron transfer and effect of solution viscosity
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
kinetics and proposed mechanism
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
mechanism and kinetics of electron transfer
-
sulfite + O2 + H2O = sulfate + H2O2
show the reaction diagram
mechanism and kinetics of electron transfer
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
-
sulfate reduction
-
-
sulfite oxidation IV
-
-
Sulfur metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
sulfite:oxygen oxidoreductase
A molybdohemoprotein.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidase, sulfite
-
-
-
-
sulphite oxidase cytochrome b9
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-38-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acidithiobacillus thiooxidans NB1-3
strain NB1-3
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
strain NRRL B-14911
-
-
Manually annotated by BRENDA team
strain NRRL B-14911
-
-
Manually annotated by BRENDA team
strain HB101
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
three patients with isolated sulfite oxidase deficiency, who manifested intractable seizures and severe hypotonia in the immediate postnatal period with an unknown diagnosis, despite extensive workup
UniProt
Manually annotated by BRENDA team
pacific hake
-
-
Manually annotated by BRENDA team
DSMZ 10014; strain DSMZ 10014
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
strain AT62
-
-
Manually annotated by BRENDA team
Thermus thermophilus AT62
strain AT62
-
-
Manually annotated by BRENDA team
immunochemical comparison
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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
M4MVJ1
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
selenite + ferricyanide + H2O
? + ferrocyanide
show the reaction diagram
-
approximately 5% of the observed sulfite activity
-
-
?
SO32- + H2O + 2 Fe(III)cytochrome c
SO42- + 2 Fe(II)cytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
SO32- + H2O + 2 ferricyanide
SO42- + 2 ferrocyanide + 2 H+
show the reaction diagram
-
-
-
-
?
SO32- + H2O + 2 ferricytochrome c
SO42- + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
SO32- + H2O + O2
SO42- + H2O2
show the reaction diagram
-
-
-
-
?
SO32- + H2O + O2
SO42- + H2O2
show the reaction diagram
-
-
-
-
?
sodium sulfite + H2O + A
NaSO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
genetic deficiency results in neurological abnormities
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
catalytic cycle
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
natural acceptor
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
significantly slower activity than that observed with ferricyanide
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
M4MVJ1
substrates horse heart cytochrome c, and recombinant Starkeya novella cytochrome c are only reduced to about 40% while Sinorhizobium meliloti cytochrome c is almost completely reduced. 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
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
A5H1Q7
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
C5HG86
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
-
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
artificial A: tetramethylphenylenediamine, 2,6-dichloroindophenol, methylene blue
-
-
-
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
H2O2 acceptor only when respiratory chain is inhibited
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
Acidithiobacillus thiooxidans NB1-3
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
show the reaction diagram
Thermus thermophilus AT62
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
synthetic construct
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
-
the active site of the native enzyme can adopt both six-coordinate and five-coordinate geometries, which may be important in the catalytic mechanism, which may involve the binding of anions such as sulfite directly to Mo
-
-
?
sulfite + H2O + A
sulfate + AH2
show the reaction diagram
synthetic construct
-
the initial step in the oxygen-atom transfer reaction with HSO3- takes place by oxoanionic binding of the substrate to the MoVI center with the formation of a stable Michaelis complex
-
-
?
sulfite + H2O + ferricyanide
sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
ir
sulfite + H2O + O2
sulfate + hydrogen peroxide
show the reaction diagram
-
-
-
-
?
sulfite + O2
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2
sulfate + H2O
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
-
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
A5H1Q7
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
lack of active enzyme produces severe neurodegeneration and early death in humans
-
-
?
sulfite + O2 + H2O
sulfate + hydrogen peroxide
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
-
additional information
?
-
-
No activity is found with cytochrome c as electron acceptor, since the heme domain known to mediate electron transfer between the molybdenum cofactor-domain and cytochrome c in rat hepatic SO is missing in the plant enzyme
-
-
-
additional information
?
-
-
the enzyme does not react with cytochrome c
-
-
-
additional information
?
-
-
The optimal substrate or precise physiological role for YedYZ in Escherichia coli and its well-conserved orthologs in other bacteria remains unknown.
-
-
-
additional information
?
-
synthetic construct
-
Oax-Mo-Sthiolate-C dihedral angles near 90 effectively eliminate covalency contributions to the Mo(xy) redox orbital from the thiolate sulfur. The Oax-Mo-Sthiolate-C dihedral angle is shown to have a pronounced effect on the relative intensity ratios of the XAS spin-allowed S(1s)fSv(p) + Mo-(xy) and S(1s)fSv(p) + Mo(xz,yz) transitions
-
-
-
additional information
?
-
P07850
R138, R190, and R450 contribute to a positively charged binding pocket, which stabilizes substrate/product binding
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
genetic deficiency results in neurological abnormities
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
catalytic cycle
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
show the reaction diagram
-
natural acceptor
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
-
lack of active enzyme produces severe neurodegeneration and early death in humans
-
-
?
additional information
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
-
crystal structure of the cytochrome b5 domain
-
heme
-
-
heme
-
-
heme
-
interactions of residue H90 with a heme propionate group destabilize the Fe(III) state of the heme
Molybdenum
-
molybdoenzyme
molybdopterin
-
-
molybdopterin
-
-
molybdopterin
-
-
molybdopterin
-
-
additional information
-
no heme domain
-
additional information
-
the enzyme is lacking the heme domain that is known from vertebrate sulfite oxidase
-
additional information
-
AMP independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
synthetic construct
-
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
K+
-
45-100 mM, 54-88% increase of activity
Mo
-
molybdohemoprotein, structure of molybdopterin
Mo
-
molybdohemoprotein, structure of molybdopterin
Mo
-
x-ray absorption spectroscopy of oxidation states
Mo
-
proposed structure of molybdenum center
Mo
-
molybdopterin
Mo
-
x-ray absorption spectroscopy of oxidation states
Mo
-
modeling of active site, kinetics
Mo
synthetic construct
-
the oxygen-atom transfer reactions involve the formation of the stable intermediate (MoO2HSO3)- through oxoanionic binding of HSO3- at the Mo center
Mo
-
direct coordination of molybdenum by chloride. Increase in Mo-S/Cl ligation with reduced conditions of low-pH Cl- formation, relative to those of high-pH formation
Mo
-
coordination of sulfate to the Mo(V) center in the blocked form of sulfite oxidase
Mo
-
the wild-type enzyme is five-coordinate with approximately square-based pyramidal geometry
Mo
synthetic construct
-
the putative chlorine nucleus is, in all probability, weakly coordinated to the Mo(V) complex of the enzyme
Mo
-
the organism is comprised of only the Mo-PPT binding SUOX fold itself
Molybdenum
-
molybdoenzyme
Molybdenum
-
dimeric enzyme contains only a single molybdenum cofactor domain without an additional redox center
Molybdenum
-
molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin, essential for dimerization of the enzyme
Molybdenum
-
-
Molybdenum
-
consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule
Molybdenum
-
the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
Molybdenum
-
molybdenum enzyme
Molybdenum
-
sulfite oxidation occurs at the dioxomolybdenum center of the enzyme
Molybdenum
-
-
Molybdenum
M4MVJ1
recombinant enzyme contains 0.69 molecules of Mo per protein subunit
NaCl
-
up to a concentration of 100 mM, up to 2fold activation
NH4+
-
30 mM, 74% increase of activity
Sodium arsenate
-
up to a concentration of 5 mM, up to 2fold activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
-
EDC
2,6-dichloroindophenol
-
inhibition of O2 consumption
arsenate
-
100 mM, EPR spectra
arsenite
-
-
arsenite
-
7.4 mM, 50% inhibition
CN-
-
more than 10 mM
CN-
-
profound at low O2 concentration, not at high O2 concentration
CN-
-
mechanism of inactivation
cytochrome c
-
inhibition of O2 consumption
Diethylpyrocarbonate
-
modifies ten His per enzyme molecule
EDTA
-
20 mM, 50% inhibition
ferricyanide
-
irreversible inactivation of molybdenum center
ferricyanide
-
inhibition of O2 consumption
Heavy metal ions
-
-
-
imidazole
-
0.1 mM, complete inhibition
K2HPO4
-
at 26 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
K2SO4
-
at 22 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KCl
-
at 95 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KCl
-
30 mM, 50% inhibition
KF
-
at 72 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNCS
-
at 57 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNO3
-
at 78 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNO3
-
3 mM, 50% inhibition
mannitol
-
only with O2 as electron acceptor
N-bromosuccinimide
-
94% inhibition at 0.1 mM
N-cyclohexyl-N'-[2-(N-methylmorpholino)-ethyl]carbodiimide p-toluene sulfonate
-
CMC
N-ethyl-5-phenylisoxazolium-3'-sulfonate
-
Woodward's reagent K
NaCl
-
at 100 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
NaCl
-
50% inhibition at 70 mM, in Tris/HCl 20 mM, pH 8.5
NaCl
-
150 mM, 50% inhibition
Ni2+
-
stronger inhibition at pH 7.0 than at pH 3.0
NiCl2
-
0.1 mM, complete inhibition
phosphate
-
100 mM, EPR spectra
potassium nitrate
-
50% inhibition at 1 mM, in Tris/HCl 20 mM, pH 8.5
potassium phosphate
-
50% inhibition at 30 mM, pH 8.5
potassium phosphate
-
20 mM, pH 8.0, 50% inhibition
RNAi
-
abrogates sulfite oxidase expression, whereby accumulating relatively less sulfate after SO2 application and showing enhanced induction of senescence and wounding associated transcripts, leaf necrosis and chlorophyll bleaching
-
Sodium arsenate
-
7 mM, 50% inhibition
Sodium sulfate
-
20 mM, 50% inhibition
sodium sulfite
-
a high initial concentration of sodium sulfite decreases dramatically the enzyme expression
sodium tungstate
-
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
-
80 mM, pH 8.0, 50% inhibition
Tris-HCl
-
100 mM, pH 8.0, 50% inhibition
Tris/HCl
-
50% inhibition at 90 mM, pH 8.5
methylene blue
-
70% inhibition at 0.4 mM
additional information
-
not inhibitory: NaN3 at 0.5 mM, NaCN at 0.5 mM
-
additional information
-
not inhibitory: CN-
-
additional information
-
not inhibitory: CN-
-
additional information
-
inhibition at 400 mM salt concentrations; no inhibition by periodate or 80 mM sulfate
-
additional information
-
maintaining animals on high tungsten, low molybdenum diet, effectively induces SOX deficiency
-
additional information
-
maintaining the animal on low-molybdenum, high-tungsten diet, leads to an effective production of SOX deficiency
-
additional information
-
administration of high-tungsten/low molybdenum regimen leads to deficiency in SOX
-
additional information
-
is inactivated in the dark via a process in which a Ser residue (Ser543) in the hinge region connecting the Mo-PPT dimerization domain with the heme b5 domain is phosphorylated, followed by binding of the NIA inhibitor protein
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
-
at lower oxygen concentrations
Di-(carboxamidomethyl)molybdopterin
-
-
Di-(carboxamidomethyl)molybdopterin
-
-
Sodium deoxycholate
-
at 0.04%, acceptor: cytochrome c
Tris-acetate
-
up to a concentration of 70 mM, up to 2fold activation
Tris-HCl
-
up to a concentration of 70 mM, up to 2fold activation
Molybdenum
-
the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
additional information
-
molybdenum concentrations higher than 2.07 mM do not show increase of enzyme activity
-
additional information
-
electrocatalytic performance requires a sufficient SOx surface concentration in order to generate a catalytic current, and that the amount of cytochrome c within the assembly is high enough to provide a long-range electron transfer to connect the enzyme to the electrode
-
additional information
-
2fold increase in SO activity in fumigated leaf material as compared to non-fumigated plants
-
additional information
-
no variation in SO activity between fumigated and non-fumigated plants
-
additional information
-
4fold increase in sulfite oxidase activity in fumigated leaf material as compared to non-fumigated plants
-
additional information
-
SO is constitutively expressed and is not significantly induced by SO2, whereas the SiR transcript involved in sulfur assimilation is highly induced by SO2 in an SO-dependent manner
-
additional information
-
during extended dark, sulfite oxidase activity is enhanced in tomato wild-type leaves, while the other sulfite network components are down-regulated. 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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00043
cytochrome c
-
mutant enzyme G473A, pH 8.5
0.00082
cytochrome c
-
mutant enzyme G473A, pH 7.0
0.00092
cytochrome c
-
-
0.00123
cytochrome c
-
mutant enzyme G473A, pH 6.0
0.00141
cytochrome c
-
wild type enzyme, pH 7.0
0.00173
cytochrome c
-
wild type enzyme, pH 6.0
0.002
cytochrome c
-
-
0.002
cytochrome c
-
-
0.00371
cytochrome c
-
mutant enzyme G473D, pH 8.6
0.0044
cytochrome c
-
wild type enzyme, pH 8.5
0.00474
cytochrome c
-
mutant enzyme G473D, pH 8.0
0.00536
cytochrome c
-
mutant enzyme G473W, pH 8.5
0.006
cytochrome c
-
-
0.014
cytochrome c
-
mutant enzyme G473D, pH 7.5
0.0357
cytochrome c
-
mutant enzyme G473W, pH 7.0
0.0362
cytochrome c
-
mutant enzyme G473D, pH 7.0
0.0635
cytochrome c
-
mutant enzyme G473D, pH 6.5
0.0905
cytochrome c
-
mutant enzyme G473W, pH 6.0
0.107
cytochrome c
-
mutant enzyme G473D, pH 6.0
0.00046
sulfite
-
mutant V474M, 25C, pH 6.0
0.001
sulfite
-
-
0.00129
sulfite
-
25C, pH 6.0, 20 mM buffer, wild-type enzyme
0.00129
sulfite
-
wild type enzyme in 20 mM Tris at pH 6.0
0.00129
sulfite
-
wild type enzyme, pH 6.0
0.0013
sulfite
-
wild-type, 25C, pH 6.0
0.00133
sulfite
-
wild-type, 25C, pH 7.0
0.00134
sulfite
-
mutant V474M, 25C, pH 7.0
0.00162
sulfite
-
25C, pH 6.5, 20 mM buffer, wild-type enzyme
0.00162
sulfite
-
wild type enzyme, pH 6.5
0.0017
sulfite
-
mutant Y83A, pH 8.0, 25C
0.0019
sulfite
-
mutant R472M, 25C, pH 6.0
0.0023
sulfite
-
mutant R472Q, 25C, pH 6.0
0.0025
sulfite
-
mutant R472M, 25C, pH 7.0
0.0027
sulfite
-
wild-type, 25C, pH 7.0
0.00272
sulfite
-
25C, pH 7.0, 20 mM buffer, wild-type enzyme
0.00272
sulfite
-
wild type enzyme, pH 7.0
0.0028
sulfite
-
mutant H90F, pH 8.0, 25C
0.00311
sulfite
-
25C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
0.0032
sulfite
-
mutant V474M, 25C, pH 8.0
0.0032
sulfite
-
mutant R472K, pH 7.6, 25C
0.00339
sulfite
-
25C, pH 7.5, 20 mM buffer, wild-type enzyme
0.00339
sulfite
-
wild type enzyme, pH 7.5
0.0035
sulfite
-
mutant R472Q, 25C, pH 7.0
0.00352
sulfite
-
25C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
0.00362
sulfite
-
25C, pH 7.0, 100 mM buffer, wild-type enzyme
0.00367
sulfite
-
25C, pH 7.5, 100 mM buffer, wild-type enzyme
0.0038
sulfite
-
mutant F79A, pH 8.0, 25C
0.0039
sulfite
-
mutant H90Y, pH 8.0, 25C
0.00414
sulfite
-
25C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
0.00423
sulfite
-
25C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
0.0043
sulfite
-
wild-type, 25C, pH 8.0
0.00435
sulfite
-
25C, pH 8.0, 20 mM buffer, wild-type enzyme
0.00435
sulfite
-
wild type enzyme, pH 8.0
0.00453
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
0.00453
sulfite
-
mutant enzyme G473A, pH 6.0
0.00459
sulfite
-
25C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
0.0047
sulfite
-
mutant R472M, 25C, pH 8.0
0.00503
sulfite
-
25C, pH 8.25, 20 mM buffer, wild-type enzyme
0.00536
sulfite
-
mutant enzyme G473A, pH 7.0
0.00612
sulfite
-
25C, pH 8.0, 100 mM buffer, wild-type enzyme
0.00635
sulfite
-
25C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
0.00728
sulfite
-
25C, pH 8.25, 100 mM buffer, wild-type enzyme
0.008
sulfite
-
wild-type, 25C, pH 8.5
0.008
sulfite
-
mutant F57Y, pH 8.0, 25C
0.00825
sulfite
-
25C, pH 8.5, 20 mM buffer, wild-type enzyme
0.00825
sulfite
-
wild type enzyme in 20 mM Tris at pH 8.5
0.00825
sulfite
-
wild type enzyme, pH 8.5
0.0083
sulfite
-
wild-type, 25C, pH 8.5
0.00851
sulfite
-
25C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
0.00859
sulfite
-
25C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
0.00908
sulfite
-
25C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
0.00924
sulfite
-
25C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
0.00947
sulfite
-
25C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
0.00959
sulfite
-
25C, pH 8.75, 20 mM buffer, wild-type enzyme
0.00963
sulfite
-
25C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
0.00992
sulfite
-
25C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
0.011
sulfite
-
25C, pH 8.5, 100 mM buffer, wild-type enzyme
0.011
sulfite
-
wild-type, pH 8.0, 25C
0.012
sulfite
-
mutant Y83F, pH 8.0, 25C
0.012
sulfite
-
mutant D342K, pH 7.6, 25C
0.013
sulfite
-
mutant R472Q, 25C, pH 8.0
0.013
sulfite
-
mutant F57A, pH 8.0, 25C
0.0144
sulfite
-
mutant V474M, 25C, pH 9.0
0.0158
sulfite
-
25C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
0.016
sulfite
-
mutant R472Q, 25C, pH 8.5
0.0172
sulfite
-
mutant enzyme G473A, pH 7.4
0.021
sulfite
-
mutant R472M, 25C, pH 9.0
0.0214
sulfite
C5HG86
pH not specified in the publication, temperature not specified in the publication
0.022
sulfite
-
wild-type, 25C, pH 9.0
0.022
sulfite
-
mutant R472Q, pH 7.6, 25C
0.0221
sulfite
-
25C, pH 9.0, 20 mM buffer, wild-type enzyme
0.0221
sulfite
-
wild type enzyme, pH 9.0
0.0226
sulfite
-
using ferricyanide as electron acceptor
0.0226
sulfite
-
-
0.023
sulfite
-
mutant R472D/D342K, pH 7.6, 25C; mutant R472D, pH 7.6, 25C
0.026
sulfite
-
25C, pH 9.0, 100 mM buffer, wild-type enzyme
0.0319
sulfite
-
25C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
0.0319
sulfite
-
mutant V474M, 25C, pH 9.5
0.0338
sulfite
-
using ferricyanide as electron acceptor
0.034
sulfite
-
-
0.0354
sulfite
-
mutant V474M, 25C, pH 8.5
0.04
sulfite
-
mutant V474M, 25C, pH 10.0
0.042
sulfite
-
mutant R472M, pH 7.6, 25C
0.045
sulfite
-
mutant R472Q, 25C, pH 9.0
0.0487
sulfite
-
mutant enzyme G473A, pH 8.0
0.051
sulfite
-
-
0.051
sulfite
-
mutant R472D, pH 6.5, 25C
0.0529
sulfite
-
wild-type, 25C, pH 10.0
0.0536
sulfite
-
25C, pH 9.5, 100 mM buffer, wild-type enzyme
0.0537
sulfite
-
mutant R472M, 25C, pH 9.5
0.0557
sulfite
-
25C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
0.0614
sulfite
-
mutant Y343F/R472Q, 25C, pH 6.0
0.067
sulfite
-
wild-type, 25C, pH 9.5
0.0671
sulfite
-
25C, pH 9.5, 20 mM buffer, wild-type enzyme
0.0671
sulfite
-
wild type enzyme, pH 9.5
0.0692
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.0877
sulfite
-
mutant Y343F/R472Q, 25C, pH 7.0
0.094
sulfite
-
mutant R472M, 25C, pH 8.5
0.0945
sulfite
-
-
0.0947
sulfite
-
mutant Y343N, 25C, pH 7.0
0.0953
sulfite
-
mutant Y343N, 25C, pH 6.0
0.0967
sulfite
-
mutant R472Q, 25C, pH 9.5
0.0969
sulfite
-
mutant R472M, 25C, pH 10.0
0.107
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
0.107
sulfite
-
mutant enzyme G473A, pH 8.5
0.147
sulfite
-
25C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
0.17
sulfite
-
-
0.181
sulfite
-
mutant R472Q, 25C, pH 10.0
0.2827
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.0
0.297
sulfite
-
mutant Y343N, 25C, pH 8.0
0.31
sulfite
-
-
0.33
sulfite
-
mutant enzyme G473W, pH 7.0
0.39
sulfite
-
-
0.39
sulfite
-
-
0.59 - 1
sulfite
-
25C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
0.623
sulfite
-
mutant enzyme G473D, pH 7.0
0.712
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.5
0.774
sulfite
-
mutant enzyme G473A, pH 9.1
0.85
sulfite
-
mutant Y343N, 25C, pH 8.5
0.99
sulfite
-
mutant enzyme G473D, pH 6.5
1.063
sulfite
-
mutant enzyme G473D, pH 7.5
1.1
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 6.0
1.223
sulfite
-
mutant enzyme G473D, pH 8.0
1.39
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
1.42
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 7.0
1.54
sulfite
-
25C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
1.66
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
1.66
sulfite
-
mutant enzyme G473D, pH 6.0
1.91
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
1.91
sulfite
-
mutant enzyme G473W, pH 6.0
2.03
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.034
sulfite
-
mutant enzyme G473W, pH 8.5
2.04
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
2.04
sulfite
-
mutant enzyme G473D, pH 8.5
2.14
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.0
2.46
sulfite
-
mutant Y343N, 25C, pH 9.0
3.34
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.0
3.684
sulfite
-
mutant enzyme G473A, pH 10.0
4.64
sulfite
-
mutant Y343N/R472M, 25C, pH 7.0
5.33
sulfite
-
-
8.6
sulfite
-
mutant Y322N/R450M, 25C, pH 7.0
9.37
sulfite
-
mutant Y343N, 25C, pH 9.5
10.41
sulfite
-
mutant enzyme G473W, pH 9.0
11.73
sulfite
-
mutant Y322N/R450M, 25C, pH 8.5
12
sulfite
-
mutant Y343N, 25C, pH 10.0
14
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.5
16.8
sulfite
-
mutant Y343N/R472M, 25C, pH 6.0
19.28
sulfite
-
mutant Y343N/R472M, 25C, pH 8.0
25.88
sulfite
-
mutant enzyme G473D, pH 9.1
39.9
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.5
42.99
sulfite
-
mutant Y343N/R472M, 25C, pH 8.5
55.5
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.0
59.6
sulfite
-
mutant Y343F/R472Q, 25C, pH 10.0
85.64
sulfite
-
mutant Y343N/R472M, 25C, pH 9.0
111
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.5
208
sulfite
-
mutant Y343N/R472m, 25C, pH 9.5
418
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 10.0
0.698
ferricyanide
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
variation of KM with pH
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
cytochrome c
-
mutant enzyme G473D, pH 6.0
0.48
cytochrome c
-
mutant enzyme G473D, pH 8.6
0.53
cytochrome c
-
mutant enzyme G473D, pH 6.5
0.59
cytochrome c
-
mutant enzyme G473D, pH 8.0
0.62
cytochrome c
-
mutant enzyme G473D, pH 7.5
0.78
cytochrome c
-
mutant enzyme G473D, pH 7.0
1.67
cytochrome c
-
mutant enzyme G473W, pH 6.0
1.95
cytochrome c
-
mutant enzyme G473W, pH 8.5
2.94
cytochrome c
-
mutant enzyme G473W, pH 7.0
3.83
cytochrome c
-
mutant enzyme G473A, pH 6.0
12.4
cytochrome c
-
wild type enzyme, pH 6.0
12.8
cytochrome c
-
mutant enzyme G473A, pH 7.0
18.1
cytochrome c
-
wild type enzyme, pH 7.0
25.4
cytochrome c
-
mutant enzyme G473A, pH 8.5
26.9
cytochrome c
-
wild type enzyme, pH 8.5
85
cytochrome c
-
-
0.14
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
0.14
sulfite
-
mutant enzyme G473D, pH 6.0
0.15
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.28
sulfite
-
mutant enzyme G473D, pH 6.5
0.4
sulfite
-
-
0.42
sulfite
-
mutant enzyme G473D, pH 9.1
0.46
sulfite
-
mutant R472M, 25C, pH 10.0
0.5
sulfite
-
mutant enzyme G473D, pH 7.0
0.52
sulfite
-
mutant R472Q, 25C, pH 10.0
0.54
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
0.54
sulfite
-
mutant enzyme G473D, pH 8.5
0.57
sulfite
-
mutant enzyme G473D, pH 7.5
0.58
sulfite
-
mutant enzyme G473D, pH 8.0
0.6
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
0.6
sulfite
-
mutant enzyme G473W, pH 6.0
0.75
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
0.97
sulfite
-
mutant Y343N/R472Q, 25C, pH 9.5
1.13
sulfite
-
mutant Y343N/R472Q, 25C, pH 7.0; mutant Y343N/R472Q, 25C, pH 9.0
1.33
sulfite
-
mutant Y343N/R472Q, 25C, pH 8.0
1.35
sulfite
-
mutant enzyme G473W, pH 9.0
1.35
sulfite
-
mutant Y343N/R472Q, 25C, pH 6.0
1.42
sulfite
-
mutant Y343N/R472Q, 25C, pH 8.5
1.44
sulfite
-
mutant Y343F/R472Q, 25C, pH 6.0
1.7
sulfite
-
mutant R472Q, 25C, pH 9.5
1.73
sulfite
-
mutant Y343F/R472Q, 25C, pH 7.0
1.8
sulfite
-
mutant enzyme G473W, pH 7.0
1.8
sulfite
-
mutant R472M, 25C, pH 9.5
1.9
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 6.0
2.05
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.0
2.06
sulfite
-
25C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
2.25
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.5
2.3
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.0
2.48
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.48
sulfite
-
mutant enzyme G473W, pH 8.5
2.52
sulfite
-
mutant Y322N/R450M, 25C, pH 8.5
2.8
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 10.0
2.96
sulfite
-
mutant Y343F/R472Q, 25C, pH 10.0
3 - 6
sulfite
-
mutant Y83F, pH 8.0, 25C
3.11
sulfite
-
25C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
3.17
sulfite
-
mutant Y343N, 25C, pH 6.0
3.26
sulfite
-
25C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
3.4
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 7.0
3.45
sulfite
-
mutant R472M, 25C, pH 9.0
3.5
sulfite
-
mutant R472M, 25C, pH 8.0
3.58
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.0
3.6
sulfite
-
mutant R472M, 25C, pH 7.0
3.8
sulfite
-
mutant R472M, 25C, pH 8.5
3.9
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.5
4.14
sulfite
-
25C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
4.15
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
4.15
sulfite
-
mutant enzyme G473A, pH 6.0
4.24
sulfite
-
mutant R472Q, 25C, pH 9.0
4.38
sulfite
-
mutant Y343N, 25C, pH 10.0
4.59
sulfite
-
25C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
4.6
sulfite
-
mutant R472Q, 25C, pH 8.5
4.83
sulfite
-
mutant Y322N/R450M, 25C, pH 7.0
4.9
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.5
5
sulfite
-
mutant R472M, 25C, pH 6.0
5.23
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.5
5.6
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.0
5.7
sulfite
-
mutant R472D, pH 6.5, 25C
5.8
sulfite
-
mutant R472Q, 25C, pH 7.0
5.96
sulfite
-
mutant V474M, 25C, pH 6.0
6.35
sulfite
-
25C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
7
sulfite
-
mutant Y83A, pH 8.0, 25C
7.17
sulfite
-
25C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
8.1
sulfite
-
mutant Y343N, 25C, pH 9.5
8.2
sulfite
-
mutant R472Q, 25C, pH 6.0
8.21
sulfite
-
25C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
8.51
sulfite
-
25C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
8.59
sulfite
-
25C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
8.72
sulfite
-
25C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
9.08
sulfite
-
25C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
9.2
sulfite
-
25C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
9.24
sulfite
-
25C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
9.3
sulfite
-
mutant R472Q, 25C, pH 8.0
9.47
sulfite
-
25C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
9.63
sulfite
-
25C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
9.92
sulfite
-
25C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
9.99
sulfite
-
25C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
10.5
sulfite
-
25C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
11.4
sulfite
-
mutant V474M, 25C, pH 7.0
12.1
sulfite
-
25C, pH 7.0, 100 mM buffer, wild-type enzyme
12.4
sulfite
-
mutant V474M, 25C, pH 10.0
12.8
sulfite
-
mutant Y343N, 25C, pH 7.0
13
sulfite
-
wild-type, 25C, pH 10.0
13
sulfite
-
mutant F79A, pH 8.0, 25C
13.2
sulfite
-
25C, pH 6.0, 20 mM buffer, wild-type enzyme
13.2
sulfite
-
wild type enzyme in 20 mM Tris at pH 6.0
13.2
sulfite
-
wild type enzyme, pH 6.0
13.2
sulfite
-
wild-type, 25C, pH 6.0
13.75
sulfite
-
mutant Y343N, 25C, pH 8.0
14.1
sulfite
-
mutant R472D, pH 7.6, 25C
15.1
sulfite
-
mutant enzyme G473A, pH 10.0
15.5
sulfite
-
mutant Y343N, 25C, pH 9.0
15.8
sulfite
-
mutant V474M, 25C, pH 8.5
15.9
sulfite
-
mutant enzyme G473A, pH 7.0
16
sulfite
-
mutant F57A, pH 8.0, 25C
16.9
sulfite
-
mutant Y343N, 25C, pH 8.5
17.1
sulfite
-
mutant V474M, 25C, pH 9.5
17.2
sulfite
-
25C, pH 7.5, 100 mM buffer, wild-type enzyme
17.7
sulfite
-
25C, pH 6.5, 20 mM buffer, wild-type enzyme
17.7
sulfite
-
wild type enzyme, pH 6.5
17.8
sulfite
-
mutant V474M, 25C, pH 8.0
18.5
sulfite
-
mutant R472K, pH 7.6, 25C
19
sulfite
-
mutant F57Y, pH 8.0, 25C; mutant H90F, pH 8.0, 25C
19.6
sulfite
-
mutant V474M, 25C, pH 9.0
21.6
sulfite
-
mutant enzyme G473A, pH 7.4
23
sulfite
-
mutant D342K, pH 7.6, 25C
23.6
sulfite
-
25C, pH 8.75, 20 mM buffer, wild-type enzyme
24.2
sulfite
-
25C, pH 7.0, 20 mM buffer, wild-type enzyme
24.2
sulfite
-
wild type enzyme, pH 7.0
24.2
sulfite
-
wild-type, 25C, pH 7.0
24.6
sulfite
-
25C, pH 9.5, 100 mM buffer, wild-type enzyme
24.7
sulfite
-
25C, pH 7.5, 20 mM buffer, wild-type enzyme
24.7
sulfite
-
wild type enzyme, pH 7.5
24.8
sulfite
-
25C, pH 8.25, 20 mM buffer, wild-type enzyme
25
sulfite
-
25C, pH 8.0, 100 mM buffer, wild-type enzyme
25.7
sulfite
-
25C, pH 9.0, 20 mM buffer, wild-type enzyme
25.7
sulfite
-
wild type enzyme, pH 9.0
25.7
sulfite
-
wild-type, 25C, pH 9.0
25.9
sulfite
-
25C, pH 8.0, 20 mM buffer, wild-type enzyme
25.9
sulfite
-
wild type enzyme, pH 8.0
25.9
sulfite
-
wild-type, 25C, pH 8.0
26.2
sulfite
-
mutant enzyme G473A, pH 8.0
26.3
sulfite
-
25C, pH 9.5, 20 mM buffer, wild-type enzyme
26.3
sulfite
-
wild type enzyme, pH 9.5
26.3
sulfite
-
wild-type, 25C, pH 9.5
26.6
sulfite
-
mutant R472Q, pH 7.6, 25C
26.9
sulfite
-
25C, pH 8.5, 100 mM buffer, wild-type enzyme; 25C, pH 8.5, 20 mM buffer, wild-type enzyme
26.9
sulfite
-
wild type enzyme in 20 mM Tris at pH 8.5
26.9
sulfite
-
wild type enzyme, pH 8.5
26.9
sulfite
-
wild-type, 25C, pH 8.5
26.9
sulfite
-
wild-type, pH 8.0, 25C
27
sulfite
-
25C, pH 8.25, 100 mM buffer, wild-type enzyme
27
sulfite
-
wild-type, pH 8.0, 25C
27
sulfite
-
mutant R472M, pH 7.6, 25C
28.1
sulfite
-
25C, pH 9.0, 100 mM buffer, wild-type enzyme
28.4
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
28.4
sulfite
-
mutant enzyme G473A, pH 8.5
31.9
sulfite
-
mutant enzyme G473A, pH 9.1
36.1
sulfite
-
wild-type, 25C, pH 7.0
42
sulfite
-
mutant H90Y, pH 8.0, 25C
47
sulfite
-
mutant R472D/D342K, pH 7.6, 25C
53.32
sulfite
-
-
73
sulfite
-
wild-type, 25C, pH 8.5
4500
sulfite
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00047
sulfite
-
mutant Y343N/R472M, 25C, pH 9.5
92
0.00067
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 10.0
92
0.0013
sulfite
-
mutant Y343N/R472M, 25C, pH 9.0
92
0.0033
sulfite
-
mutant Y343N/R472m, 25C, pH 8.5
92
0.0047
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.5
92
0.0049
sulfite
-
mutant Y343F/R472Q, 25C, pH 10.0
92
0.0069
sulfite
-
mutant Y343N/R472m, 25C, pH 8.0
92
0.008
sulfite
-
mutant Y343N/R472M, 25C, pH 6.0
92
0.01
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 9.0
92
0.0124
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.5
92
0.0244
sulfite
-
mutant Y343N/R472M, 25C, pH 7.0
92
0.0279
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.5
92
0.036
sulfite
-
mutant Y343N, 25C, pH 10.0
92
0.069
sulfite
-
mutant Y343F/R472Q, 25C, pH 9.0
92
0.0866
sulfite
-
mutant Y343N, 25C, pH 9.5
92
0.167
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 8.0
92
0.173
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 6.0
92
0.214
sulfite
-
mutant Y322N/R450M, 25C, pH 8.5
92
0.237
sulfite
-
mutant Y343N/R472M/V474M, 25C, pH 7.0
92
0.316
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.5
92
0.632
sulfite
-
mutant Y343N, 25C, pH 9.0
92
0.725
sulfite
-
mutant Y343F/R472Q, 25C, pH 8.0
92
1.97
sulfite
-
mutant Y343F/R472Q, 25C, pH 7.0
92
1.99
sulfite
-
mutant Y343N, 25C, pH 8.5
92
2.35
sulfite
-
mutant Y343F/R472Q, 25C, pH 6.0
92
3.33
sulfite
-
mutant Y343N, 25C, pH 6.0
92
4.63
sulfite
-
mutant Y343N, 25C, pH 8.0
92
8.6
sulfite
-
wild-type, 25C, pH 7.0
92
11
sulfite
-
mutant R472D, pH 6.5, 25C
92
13.5
sulfite
-
mutant Y343N, 25C, pH 7.0
92
30.8
sulfite
-
mutant V474M, 25C, pH 10.0
92
53.6
sulfite
-
mutant V474M, 25C, pH 9.5
92
136
sulfite
-
mutant V474M, 25C, pH 9.0
92
246
sulfite
-
wild-type, 25C, pH 10.0
92
392
sulfite
-
wild-type, 25C, pH 9.5
92
446
sulfite
-
mutant V474M, 25C, pH 8.5
92
558
sulfite
-
mutant V474M, 25C, pH 8.0
92
610
sulfite
-
mutant R472D, pH 7.6, 25C
92
640
sulfite
-
mutant R472M, pH 7.6, 25C
92
851
sulfite
-
mutant V474M, 25C, pH 7.0
92
1160
sulfite
-
wild-type, 25C, pH 9.0
92
1200
sulfite
-
mutant R472Q, pH 7.6, 25C
92
1300
sulfite
-
mutant V474M, 25C, pH 6.0
92
1900
sulfite
-
mutant D342K, pH 7.6, 25C
92
2000
sulfite
-
mutant R472D/D342K, pH 7.6, 25C
92
2400
sulfite
-
wild-type, pH 8.0, 25C
92
3260
sulfite
-
wild-type, 25C, pH 8.5
92
5800
sulfite
-
mutant R472K, pH 7.6, 25C
92
5950
sulfite
-
wild-type, 25C, pH 8.0
92
8690
sulfite
-
wild-type, 25C, pH 8.5
92
8900
sulfite
-
wild-type, 25C, pH 7.0
92
10000
sulfite
-
wild-type, 25C, pH 6.0
92
27000
sulfite
-
mutant Y322N/R450M, 25C, pH 7.0
92
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0162
-
crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.0322
-
crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.1006
-
crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.1457
-
crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.191
-
crude cell extract
0.2032
-
crude extract, at 25C, pH 8.0, in 25 mM Tris-HCl
0.4036
-
-
9.2
-
; crude extract
56.67
-
after 297fold purification
188
-
20fold purified enzyme
additional information
-
comparison of activity in different cells and tissues
additional information
-
activity in different organelles
additional information
-
activity in different organelles
additional information
-
activity in different organelles
additional information
-
activity in different organelles; comparison of activity in different cells and tissues
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
-
7
-
below: less than 50% of maximal activity
additional information
-
presence of coordinated sulfate in the sulfite reduced low-pH form of the plant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression in all brain regions examined: cerebellum, cerebral cortex, medulla, spinal cord, ocipital pole, frontal lobe, amygdala, caudate nucleus, corpus callosum, hippocampus, thalamus, temporal lobe, putamen. The cerebral cortex shows the highest level of expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
-
substantial expression
Manually annotated by BRENDA team
-
substantial expression
Manually annotated by BRENDA team
-
SO shows constitutive expression without any pronounced diurnal rhythm. No difference at the protein level in younger or older rosette or stem leaves
Manually annotated by BRENDA team
-
perpheral blood, little expression
Manually annotated by BRENDA team
-
strong activity
Manually annotated by BRENDA team
-
substantial expression
Manually annotated by BRENDA team
-
rats maintained on standard rat chow and tap water exhibit high level of hepatic SOX activity
Manually annotated by BRENDA team
-
leucocyte, little expression
Manually annotated by BRENDA team
-
substantial expression
Manually annotated by BRENDA team
-
vasculatures and tips
Manually annotated by BRENDA team
-
substantial expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
activity in tissues and cells
Manually annotated by BRENDA team
additional information
-
activity in tissues and cells
Manually annotated by BRENDA team
additional information
-
distribution in fish organs
Manually annotated by BRENDA team
additional information
-
young inflorescences
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
10% of total activity, inside vesicles
-
Manually annotated by BRENDA team
-
mutant enzyme C102S
-
Manually annotated by BRENDA team
Thermus thermophilus AT62
-
-
-
-
Manually annotated by BRENDA team
-
nearly exclusively in
Manually annotated by BRENDA team
additional information
-
subcellular localisation
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
-
gel filtration
393025
38000
-
gel filtration
668531
38940
-
calculated from sequence of cDNA
669129
39100
-
SDS-PAGE
668531
40000
-
gel filtration, predicted amino acid sequence
393031
43000
-
His-tagged enzyme, SDS-PAGE
669129
43300
-
calculated from sequence of cDNA
670497
43300
-
sequence analysis
694617
44300
-
gel filtration
669129
45000
-
immuno-detection
694666
71000
M4MVJ1
gel filtration
725075
101000
-
wild type enzyme, sedimentation equilibrium analysis
667714
113000
-
gel filtration
698227
115000 - 120000
-
gel filtration
392999
115000 - 120000
-
sedimentation equilibrium centrifugation
393004
115000 - 120000
-
sedimentation equilibrium centrifugation, gel filtration
393015
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
C5HG86
x * 45000, SDS-PAGE
?
-
? * 55000, SDS-PAGE, heterogenous behaviour in sedimentation equilibrium experiments
?
-
? * 46000, SDS-PAGE
dimer
-
-
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
SDS-PAGE
dimer
-
2 * 50545, amino acid sequence
dimer
-
2 * 55000-60000, SDS-PAGE
dimer
-
56000 + 46500, SDS-PAGE
dimer
-
2 * 40250, gel filtration
dimer
-
2 * 52000, wild type enzyme, sedimentation equilibrium analysis
dimer
-
wild type enzyme, mutant enzymes G473A and A208D
dimer
-
2 x 56000, gel filtration, SDS-PAGE
dimer
M4MVJ1
2 * 42669, mass spectrometry, 2 * 42791, calculated
homodimer
-
2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
monomer
-
1 * 40000, gel filtration, predicted amino acid sequence
monomer
-
1 * 43300
monomer
-
1 * 52000, mutant G473D, calculation from amino acid sequence, 1 * 53500, mutant G473D, gel filtration and sedimentation equilibrium analysis, 1 * 54500, mutant G473W, sedimentation equilibrium analysis, 1 * 66600, double mutant R212A/G473D, sedimentation equilibrium analysis
pentamer
-
crystallography
monomer
-
mutant enzymes G473D and G473W
additional information
-
after tryptic cleavage: 9500, heme-containing fragment, gel filtration with guanidine-HCl, 47400, molybdenum-containing fragment, SDS-PAGE
additional information
-
study of domains
additional information
-
study on precursor and processing
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, apoenzyme at 2.6 A resolution
-
vapor diffusion method, crystal structure of cytochrome b5 doamin at 1.2 A resolution
-
isolated molybdenum- and heme-fragments
-
crystal structure of (3,5-dimethyltrispyrazol-1-yl)borate MoO(2-mercaptobenzyl alcohol), the first oxomolybdenum monothiolate to possess an Oax-Mo-Sthiolate-C dihedral angle of ca. 90
synthetic construct
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
-
quite stable, but unstable below pH 7.0
393016
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
10 min stable
392999
45 - 60
-
half-lives of 10 min at 60C, 30 min at 55C, and 3 h at 45C, respectively
669129
50 - 80
-
The enzyme retains 100% of residual activity up to 7 h of incubation at 50C. Half life times of the enzyme at 60, 70 and 80C are respectively 8, 6.5 and 1.5 h. The enzyme retains 30% of activity at 25C and 45% at 90C.
668531
50
-
rapid inactivation
392999
52
-
inactivation, protection by sulfate
393014
54
-
reduced form has higher stability than oxidized form
393003
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 250-300 mM NaCl, several weeks, stable
-
-20C, more than 2 months, without any loss of activity
-
-80C, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Mono-Q column chromography
-
nickelnitrilotriacetic acid superflow matrix followed by anion exchange chromatography on a SourceQ15 column
-
75% pure
-
His-Select HF nickel affinity gel column chromatography
-
nickel affinity chromatography
-
70-77% pure
-
His-tagged enzyme expressed in Escheria coli
-
on Ni-NTA resin
-
phenyl-Sepharose column chromatography and Superdex 200 16/60 FPLC column gel filtration
-
recombinant protein from Escherichia coli
-
recombinant R160Q
-
Superdex 200 FPLC column gel filtration
-
wild-type and mutant Y343F
-
acetone fractionation, ion exchange chromatography and Sephadex gel filtration
-
isolation of heme-and molybdenum-containing fragments
-
; by cation-exchange adsorber and ultra filtration, 20fold purified
-
DEAE 52 column chromatography, Superdex X26 gel filtration and hydroxyapatite column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
constitutive overexpression
-
expressed in Escherichia coli strain TP1000
-
overexpressed in transgenic poplar plants with SO2 gas
-
expressed in Escherichia coli strains BL21-CodonPlus(DE3)-RIL and TP1000
-
expressed in Escherichia coli strain TP1000
-
His-tagged SO expressed in Escherichia coli TP1000 cells containing plasmid pTG718
-
recombinant R160Q
-
wild-type and mutant Y343F
-
expression in Escherichia coli
M4MVJ1
constitutive overexpression
-
expressed in Escherichia coli strain TP1000
-
expression in Escherichia coli
C5HG86
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
sulfate oxidase SO activity and sulate-oxidase-dependent H2O2-generating activity in Hibiscus chlorotic ringspot virus-infected leaves increases about 4.5fold compared with that in mock-inoculated kenaf plants
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C102S
-
different location compared to the wild type enzyme
R138Q
-
the side chain nitrogen of the Gln appears to be within the coordination sphere of the Mo
Y322F/R450M
-
introduction of predicted catalytic site residues of assimilatory nitrate reductase, markedly decreased ability to bind sulfite at pH 8.5
A208D
-
the intramolecular electron transfer rate constants at pH 6.0 are decreased by 3 orders of magnitude relative to that of the wild type, the active site structure of the Mo(V) form of A208D is different from that of the wild type
A208D
-
SUOX deficiency
C207S
-
C207 essential for enzyme activity, probably as ligand of Mo
D342K
-
significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
F57A
-
the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
F57Y
-
the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
F79A
-
the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
G473A
-
dimer
G473A
-
mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type
G473D
-
monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation
G473D
-
monomer, the Mo(V) active site structure is similar to that of the wild type, and the IET rate constant is only 2.6fold smaller than that of the wild type
G473D
-
SUOX deficiency
G473D/R212A
-
shows no intramolecular electron transfer rate
G473W
-
monomer
G473W
-
monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation
H90F
-
interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
R160K
-
the intramolecular electron transfer rate constant for the mutant enzyme is about one-fourth that of the wild-type enzyme
R160Q
-
sulfite-oxidase deficient patient
R160Q
-
the intramolecular electron transfer rate constant for the mutant enzyme at pH 6.0 is decreased by nearly 3 orders of magnitude relative to wild-type enzyme. The intramolecular electron transfer is rate-limiting in the catalytic cycle of the mutant, fatal impact of this mutation in patients with this genetic disorder
R160Q
-
at least three different Mo(V) species of R160Q exist as a function of pH (low pH type 1 and type 2, and high-pH). Mo(V) species with a blocked form of sulfite oxidase, with sulfate coordinated to the Mo center is the only species at pH higher or equal as 6 and remains a significant form at physiological pH, is six-coordinate and has a nearby exchangeable proton that is likely to be hydrogen-bonded to an oxygen of the sulfate ligand. The blocked structure of R160Q represents a catalytic dead end that contributes to the lethality of this mutant under physiological conditions
R160Q
-
clinical mutant, has a six-coordinate pseudooctahedral active site with coordination of glutamine Oepsilon to molybdenum
R160Q
-
mutation increases the Km for sulfite and decreases the kcat, resulting in a 1000fold decrease in catalytic efficiency. Reveals an increase in coordination number for the Mo, from 5 to 6
R212A/G473D
-
mutant is able to oligomerize but has undetectable activity, significant random-coil formation
R472D
-
significant decrease in the intramolecular electron transfer rate constant, and the redox potentials of both metal centers are affected
R472D/D342K
-
mutation reverses the charges of the salt bridge components, large decrease in intramolecular electron transfer rate constant
R472K
-
40% increase in catalytic efficiency
R472M
-
introduction of predicted catalytic site residues of assimilatory nitrate reductase, kinetic analysis
R472M
-
significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
R472Q
-
introduction of predicted catalytic site residues of assimilatory nitrate reductase, kinetic analysis
R472Q
-
significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
S370Y
-
SUOX deficiency
V474M
-
active site mutant, kinetic analysis
Y343F
-
in the mutant enzyme using cytochrome c as electron acceptor, turnover number is somewhat impaired, 34% of the wild-type activity at pH 8.5. The KM-value for the mutant enzyme shows a 5fold increase over wild-type. Reduction of the molybdenum center of the Y343 F variant by sulfite is more significantly impaired at high pH than at low pH
Y343F
-
increase in the Km-value for sulfite and a decrease in turnover number results in a 23fold attenuation in the specificity constant turnover (ratio of number to KM-value for sulfite) at optimum pH value of 8.25
Y343F
-
under low pH conditions the active site of Y343F is in the blocked form, with the Mo(V) center coordinated by sulfate. The Y343F mutation increases the apparent pKa of the transition from the low pH to high pH forms by ca. 2 pH units. An additional low pH form that has no exchangeable protons
Y343F/R472Q
-
active site mutant, kinetic analysis
Y343N
-
active site mutant, kinetic analysis
Y343N/R472M
-
active site mutant, kinetic analysis
Y343N/R472M/V474M
-
active site mutant, kinetic analysis
Y343X
-
isolated sulfite oxidase deficiency, shows early neonatal leukoencephalopathy and extensive symmetric cerebral injury especially white matter and basal ganglia
Y83A
-
mutation is located on the surface of the heme domain, but not in direct contact with the heme or the propionate groups, little effect on either intramolecular electron transfer or the heme potential
C207S
-
C207 essential for enzyme activity
C242S
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silent mutation
C260S
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silent mutation
additional information
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a 1 bp insertion located in exon 4 of the bovine SUOX gene (c.363-364insG) is the causative mutation for arachnomelia
H90Y
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interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
additional information
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optimized expression in Escherichia coli, untagged and His-tagged enzyme, expression in presence of tungstate
additional information
P51687
isolated sulfite oxidase deficiency, extensive brain damage in the gray matter and more pronounced damage in the white matter, without subsequent recovery. Early onset of energetic and metabolic imbalance. Impaired energetic status and accumulated metabolites
additional information
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SUOX deficiency is typically inherited as a recessive autosomal trait for which there is no known therapy and typically results in death in infancy
Y83F
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mutation is located on the surface of the heme domain, but not in direct contact with the heme or the propionate groups, little effect on either intramolecular electron transfer or the heme potential
additional information
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in tobacco mutants lacking the molybdenum cofactor and, therefore, also lacking active peroxisomal sulfite oxidase, the total sulfite oxidizing capacity of cell extracts decreased to 40% of the wild-type
C451S
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silent mutation
additional information
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SOX activity in SOX-deficient animals is significantly reduced by 95-99%. In SOX-deficient rats, sulfite treatment causes a significant increase in the plasma lipid hydroperoxide and total oxidant status levels, while -SH content of rat plasma significantly decreases compared to the control. Significant decrease in plasma total antioxidant capacity level by sulfite treatment
additional information
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SOX activity is almost devoid in SOX-deficient rats with respect to controls. In SOX-deficient rats, plasma levels of selenium, iron, and zinc are unaffected by sulfite. Plasma level of Mn is decreasing, while plasma Cu level is increased. Treating SOX-deficient groups with sulfite does not alter plasma level of Mn but makes plasma level of Cu back to its normal level. In SOX-deficient rats, plasma ceruloplasmin ferroxidase activities are lower compared to normal control without sulfite treatment
additional information
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SOX-deficient rats, exposure to sulfite has no effect on hippocampus antioxidant enzymes superoxidase dismutase, catalase, and glutathione peroxidase
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in vitro insertion of molybdopterin into aposulfite oxidase and conversion of molybdopterin into molybdenum cofactor
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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electroimmobilisation into polypyrrole film, use for amperometric detection of sulfite
food industry
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artificial ETC composed of cytochrome c and sulfite oxidase formed by the layer-by-layer technique using a polyelectrolyte. The multilayer technology, e.g. sulfite oxidase-cyt c multilayer electrode may act as an anode in a bio-fuel cell and furthermore such multilayers may be exploited as a biosensor for the detection of sulfite, which is used as a preservative in wine and other foodstuffs
medicine
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deficiency in SO, due to either a defect in molybdopterin cofactor biosynthesis or a mutation in the apo-enzyme gene itself, leads to dramatic neurological problems that can cause death in early infancy
medicine
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low plasma total homocysteine is a valuable early indicator of sulfite oxidase dysfunction, providing a crucial first-line screen, whereas plasma cystine is not always informative in the first few days of life
agriculture
C5HG86
over-expression in tobacco plants enhances their tolerance to sulfite stress. The plants show much less damage, less sulfite accumulation, but greater amounts of sulfate. H2O2 accumulation levels by histochemical detection and quantitative determination in the overexpressing plants are much less than those in the wild-type upon sulfite stress. Reductions of catalase levels detected in the overexpressing lines are considerably less than in the wild-type plants
additional information
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plants can utilize sulfite oxidase in a sulfite oxidative pathway to cope with sulfite overflow. Protects plants from toxic doses of SO2 gas
additional information
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SO may play a role in protecting catalase from sulfite damage. SO may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
additional information
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SO may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
medicine
P51687
magnetic resonance imaging and magnetic resonance spectroscopy measurements may help differentiate isolated sulfite oxidase deficiency from hypoxic-ischemic condition in patients in whom this diagnosis is not clinically suspected and may lead to further genetic antenatal inquiry that may prevent the birth of other infants affected with this severe and incurable congenital disease
additional information
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layer-by-layer assembly of globular proteins is feasible without use of polymers as counterpolyelectrolyte, which is interesting for the construction of third-generation biosensors. The assembly is made by co-adsorption of the enzyme SOx and the electron transfer protein cytochrome c
additional information
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sulfite oxidase may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
additional information
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sulfite treatment may cause oxidative stress and competent animals in SOX cope with this stressful conditions by increase in all antioxidant enzyme activities
additional information
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sulfite treatment may cause oxidative stress, and SOX normal animal copes with this stressful condition due to oxidative/antioxidative balance, whereas SOX-deficent rats, which are an exaggerated model for the normal human situation, cannot handle the sulfite-dependent oxidative stress
additional information
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plants can utilize sulfite oxidase in a sulfite oxidative pathway to cope with sulfite overflow. Protects plants from toxic doses of SO2 gas
food industry
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biosensor for detection of sulfite in food and beverages, useful for establishing biosensor systems for detection of sulfite in food and beverages considering the high sensitivity of biosensors and the increasing demand for such biosensor devices
additional information
synthetic construct
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alternative functional model ([Mo(TmMe)(O)2Cl]) of the metalloenzyme sulfite oxidase undergoes oxygen atom transfer chemistry and performs the primary function of the enzyme, sulfite oxidation