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
-
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
-
-
-
-
additional information
-
the enzyme also functions as a selenite oxidase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
-
sulfate reduction
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-
sulfite oxidation IV
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Sulfur metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
sulfite:oxygen oxidoreductase
A molybdohemoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-38-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NB1-3
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-
Manually annotated by BRENDA team
strain NB1-3
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Arthrobacter aurescens
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain NRRL B-14911
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-
Manually annotated by BRENDA team
strain NRRL B-14911
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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
-
-
Manually annotated by BRENDA team
pacific hake
-
-
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
DSMZ 10014; strain DSMZ 10014
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
synthetic construct
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain AT62
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
-
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
sodium sulfite + H2O + A
NaSO42- + AH2
show the reaction diagram
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
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
-
-
-
-
ir
sulfite + H2O + O2
sulfate + hydrogen peroxide
show the reaction diagram
-
-
-
-
?
sulfite + O2
sulfate + H2O
show the reaction diagram
-
-
-
-
?
sulfite + O2
sulfate + H2O2
show the reaction diagram
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
show the reaction diagram
sulfite + O2 + H2O
sulfate + hydrogen peroxide
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
?
-
-
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
-
crystal structure of the cytochrome b5 domain
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Molybdenum
-
molybdoenzyme
molybdopterin
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
synthetic construct
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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
K+
-
45-100 mM, 54-88% increase of activity
Molybdenum
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 hide
LITERATURE
IMAGE
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
-
EDC
2,6-dichloroindophenol
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inhibition of O2 consumption
arsenate
-
100 mM, EPR spectra
arsenite
cytochrome c
-
inhibition of O2 consumption
Diethylpyrocarbonate
-
modifies ten His per enzyme molecule
EDTA
-
20 mM, 50% inhibition
ferricyanide
Heavy metal ions
imidazole
-
0.1 mM, complete inhibition
K2HPO4
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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
KF
-
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
-
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
-
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
Sodium arsenate
-
7 mM, 50% inhibition
Sodium sulfate
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20 mM, 50% inhibition
sodium sulfite
-
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
additional information
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043 - 0.107
cytochrome c
0.698
ferricyanide
-
-
0.015
O2
0.00046 - 418
sulfite
additional information
additional information
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
-
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
-
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
-
20fold purified enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
7
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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 hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
substantial expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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wild type enzyme
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Manually annotated by BRENDA team
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10% of total activity, inside vesicles
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Manually annotated by BRENDA team
additional information
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subcellular localisation
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
gel filtration
38000
-
gel filtration
38940
-
calculated from sequence of cDNA
39100
-
SDS-PAGE
40000
-
gel filtration, predicted amino acid sequence
43000
-
His-tagged enzyme, SDS-PAGE
44300
-
gel filtration
45000
-
immuno-detection
71000
gel filtration
101000
-
wild type enzyme, sedimentation equilibrium analysis
113000
-
gel filtration
115000 - 120000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
monomer
pentamer
-
crystallography
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, apoenzyme at 2.6 A resolution
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vapor diffusion method, crystal structure of cytochrome b5 doamin at 1.2 A resolution
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isolated molybdenum- and heme-fragments
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
10 min stable
45 - 60
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half-lives of 10 min at 60C, 30 min at 55C, and 3 h at 45C, respectively
50
-
rapid inactivation
50 - 80
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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.
52
-
inactivation, protection by sulfate
54
-
reduced form has higher stability than oxidized form
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trypsin inactivates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, more than 2 months, without any loss of activity
-
-80C, several weeks
-
4C, 250-300 mM NaCl, several weeks, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
70-77% pure
-
75% pure
-
; by cation-exchange adsorber and ultra filtration, 20fold purified
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acetone fractionation, ion exchange chromatography and Sephadex gel filtration
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DEAE 52 column chromatography, Superdex X26 gel filtration and hydroxyapatite column chromatography
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His-Select HF nickel affinity gel column chromatography
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His-tagged enzyme expressed in Escheria coli
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isolation of heme-and molybdenum-containing fragments
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Ni-NTA column chromatography and Mono-Q column chromography
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nickel affinity chromatography
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nickelnitrilotriacetic acid superflow matrix followed by anion exchange chromatography on a SourceQ15 column
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on Ni-NTA resin
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partial
phenyl-Sepharose column chromatography and Superdex 200 16/60 FPLC column gel filtration
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recombinant protein from Escherichia coli
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recombinant R160Q
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Superdex 200 FPLC column gel filtration
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wild-type and mutant Y343F
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
constitutive overexpression
expressed in Escherichia coli strain TP1000
expressed in Escherichia coli strains BL21-CodonPlus(DE3)-RIL and TP1000
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expression in Escherichia coli
His-tagged SO expressed in Escherichia coli TP1000 cells containing plasmid pTG718
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overexpressed in transgenic poplar plants with SO2 gas
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recombinant R160Q
-
wild-type and mutant Y343F
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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introduction of predicted catalytic site residues of assimilatory nitrate reductase, markedly decreased ability to bind sulfite at pH 8.5
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
G473D/R212A
-
shows no intramolecular electron transfer rate
H90F
-
interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
H90Y
-
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
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
S370Y
-
SUOX deficiency
V474M
-
active site mutant, kinetic analysis
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
Y83F
-
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
-
silent mutation
C260S
-
silent mutation
C451S
-
silent mutation
additional information
Renatured/COMMENTARY