Information on EC 1.15.1.1 - superoxide dismutase

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

EC NUMBER
COMMENTARY
1.15.1.1
-
RECOMMENDED NAME
GeneOntology No.
superoxide dismutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site is not conserved, differing from others of Mn-SOD and Fe-SOD; amino acid sequence alignment and comparison; mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison; mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism; three-dimensional structure
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
Cu2+-binding
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Q96UT6
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
P81527
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Anas platyrhynchos domestica
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure; amino acid sequence alignment and comparison
Q71S31
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure; amino acid sequence alignment and comparison
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
presence of a general acid and a general base in catalysis. Catalytic model requires histidine residues, metal-bound water molecules and two hydrated metal ions to operate in concert
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Acholeplasma laidlawii Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Anas platyrhynchos domestica CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Arthrospira platensis Fe-SOD, Aspergillus flavus CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs
Aspergillus niger 26
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Aspergillus niger CuZn-SOD, Aspergillus terreus CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism; mechanism; mechanism; three-dimensional structure
Bos taurus CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Brassica rapa subsp. campestris Fe-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism; mechanism
Caulobacter vibrioides CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Desulfovibrio gigas Fe-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Emericella nidulans CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism; mechanism
Escherichia coli Fe-SOD, Escherichia coli Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism; mechanism; mechanism
Geobacillus stearothermophilus Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Halobacterium salinarum NRL
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure; amino acid composition, comparison; amino acid composition, comparison
Homo sapiens CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
Paracoccus denitrificans CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Photobacterium damselae Fe-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison; mechanism; mechanism
Photobacterium leiognathi CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison; amino acid composition, comparison
Pisum sativum Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Pseudomonas carboxydohydrogena Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison; amino acid sequence alignment and comparison
Pseudomonas putida Fe-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Rhodobacter sphaeroides Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison; mechanism
Saccharomyces cerevisiae CuZn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure; amino acid composition, comparison; amino acid sequence alignment and comparison; mechanism
Saccharomyces cerevisiae Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid sequence alignment and comparison
Sinorhizobium meliloti Rm5000
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
amino acid composition, comparison
Solanum lycopersicum Fe-SOD, Spinacia oleracea Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
mechanism
Thermoplasma acidophilum Fe-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison
Thermus thermophilus Mn-SOD
-
-
2 O2.- + 2 H+ = O2 + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
ethylene biosynthesis III (microbes)
-
superoxide radicals degradation
-
SYSTEMATIC NAME
IUBMB Comments
superoxide:superoxide oxidoreductase
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cambialistic superoxide dismutase
Q9Y8H8
-
cMnSOD
C3W7U9
-
cMnSOD
C3W7V0
-
copper, zinc superoxide dismutase
-
-
copper, zinc superoxide dismutase
Penicillium marneffei
B6QEB3
-
copper-zinc superoxide dismutase
-
-
-
-
copper-zinc superoxide dismutase
-
-
copper/zinc superoxide dismutase
C5H405
-
copper/zinc-superoxide dismutase
Q6B7T0
-
CtSOD
Q1HEQ0
gene name
CtSOD
Chaetomium thermophilum HSAUP072651
Q1HEQ0
gene name
-
Cu, Zn SOD
Penicillium marneffei
B6QEB3
-
Cu, Zn-superoxide dismutase
Q1HEQ0
-
Cu, Zn-superoxide dismutase
Chaetomium thermophilum HSAUP072651
Q1HEQ0
-
-
Cu, ZnSOD
Q1HEQ0
-
Cu, ZnSOD
Chaetomium thermophilum HSAUP072651
Q1HEQ0
-
-
Cu,Zn superoxide dismutase
Q1HEQ0
-
Cu,Zn superoxide dismutase
-
-
Cu,Zn-SOD
-
-
-
-
Cu,Zn-SOD
-
-
Cu,Zn-SOD
-
-
Cu,Zn-SOD
A7BI63
-
Cu,Zn-SOD
Q1HDV5
-
Cu,Zn-superoxide dismutase
-
-
Cu,Zn-superoxide dismutase
-
-
Cu,Zn-superoxide dismutase
Rattus norvegicus Wistar
-
-
-
Cu,Zn-superoxide dismutase
-
-
Cu,ZnSOD
Burkholderia cenocepacia K56-2
-
-
-
Cu,ZnSOD
Q1HEQ0
-
Cu-Zn SOD
-
-
Cu-Zn SOD
-
-
Cu-Zn superoxide dismutase
-
-
-
-
Cu-Zn superoxide dismutase
-
-
Cu-Zn superoxide dismutase
-
-
Cu/Zn SOD
-
-
Cu/Zn SOD
Kluyveromyces marxianus NBIMCC 1984
-
-
-
Cu/Zn superoxide dismutase
-
-
Cu/Zn superoxide dismutase
Q5JCT2
-
Cu/Zn superoxide dismutase
P00441
-
Cu/Zn superoxide dismutase
-
-
Cu/Zn superoxide dismutase
B0B552
-
Cu/Zn superoxide dismutase
Kluyveromyces marxianus L3
B0B552
-
-
Cu/Zn superoxide dismutase
Kluyveromyces marxianus NBIMCC 1984
-
-
-
Cu/Zn superoxide dismutase 1
-
-
Cu/Zn-SOD
-
-
Cu/Zn-SOD
Aspergillus niger 26
-
-
-
Cu/Zn-SOD
-
-
Cu/Zn-SOD
-
-
Cu/Zn-SOD
Humicola lutea 103
-
-
-
Cu/Zn-SOD
B0B552
-
Cu/Zn-SOD
Kluyveromyces marxianus L3
B0B552
-
-
Cu/Zn-superoxide dismutase
-
-
Cu/Zn-superoxide dismutase
Aspergillus niger 26
-
-
-
Cu/Zn-superoxide dismutase
C7EXL1
-
Cu/Zn-superoxide dismutase
Beauveria bassiana 2860
C7EXL1
-
-
Cu/Zn-superoxide dismutase
-
-
Cu/Zn-superoxide dismutase
Humicola lutea 103
-
-
-
cuprein
-
-
-
-
CuZn superoxide dismutase
Q52JH6
-
CuZn superoxide dismutase 1
-
-
CuZn-SOD
-
-
CuZn-superoxide dismutase
-
-
CuZnSOD
D0UXW7
-
CuZnSOD
-
gene name
cytMnSOD
D3IU19
-
cytocuprein
-
-
-
-
cytosolic manganese superoxide dismutase
D3IU19
-
dismutase, superoxide
-
-
-
-
EC-SOD
-
-
EC-SOD
-
extracellular superoxide dismutase
EC-SOD
Homo sapiens CuZn-SOD, Homo sapiens Mn-SOD
-
extracellular superoxide dismutase
-
EC-SOD
-
-
ECSOD
C5H405
-
ECSOD
-
-
erythrocuprein
-
-
-
-
extracellular CuZnSOD
C5H405
-
extracellular superoxide dismutase
-
-
Fe-SOD
-
-
-
-
Fe-SOD
Q5UVY7
-
Fe-SOD
Sulfolobus solfataricus MT-4
-
-
-
Fe-superoxide dismutase
Q08713
-
Fe-superoxide dismutase
Q08713
-
-
Fe-type SOD
Q08713
-
Fe/Mn-type SOD
Q08713
-
Fe/MnSOD
-
-
-
ferrisuperoxide dismutase
-
-
-
-
FeSOD
B0L421, B2KYC6, B2KYC9
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
intracellular Cu-Zn superoxide dismutase
-
-
iron SOD
-
-
iron superoxide dismutase
B6ENP9
-
iron superoxide dismutase
-
-
iron superoxide dismutase
-
-
iron superoxide dismutase
Sulfolobus solfataricus MT-4
-
-
-
iron-containing superoxide dismutase
B0L421, B2KYC6, B2KYC9
-
iron-containing superoxide dismutase
-
-
iron-containing superoxide dismutase
-
-
-
iron-superoxide dismutase
Q5UVY7
-
iron-superoxide dismutase
-
-
iron-superoxide dismutase
Sulfolobus solfataricus MT-4
-
-
-
KmSod1p
B0B552
-
KmSod1p
Kluyveromyces marxianus L3
B0B552
-
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-, C3W7U9
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-, C3W7V0
-
manganese superoxide dismutase
Q2TV65
-
manganese superoxide dismutase
Danio rerio AB
Q2TV65
-
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
P04179
-
manganese superoxide dismutase
C7DRQ4
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-
-
manganese superoxide dismutase
-, C3W7V1
-
manganese superoxide dismutase
A3RLW7
-
manganese-containing superoxide dismutase
A6MHS2, Q6QHT3
-
manganese-containing superoxide dismutase
Bacillus cereus 905
A6MHS2, Q6QHT3
-
-
manganese-containing superoxide dismutase
-
-
manganese-containing superoxide dismutase
-
-
manganese-containing superoxide dismutase
-
-
-
manganese-containing superoxide dismutase
E9RHW0
-
mitMn-SOD
-
-
mitochondrial manganese superoxide dismutase
D3J1L2
-
Mn-containing superoxide dismutase
-
-
Mn-SOD
-
-
-
-
Mn-SOD
Aspergillus niger 26
-
-
-
Mn-SOD
Q2TV65
-
Mn-SOD
Danio rerio AB
Q2TV65
-
-
Mn-SOD
-
-
Mn-SOD
Humicola lutea 103
-
-
-
Mn-SOD
E9RHW0
-
Mn-type SOD
Q08713
-
Mn/Fe superoxide dismutase
Q7X4G4
-
MnSOD
A6MHS2
-
MnSOD
Bacillus cereus 905
A6MHS2
-
-
MnSOD
D0UXW8
-
MnSOD
Chaetomium thermophilum CT2
-
-
-
MnSOD
P04179
-
MnSOD
C7DRQ4
-
MnSOD1
Q6QHT3
-
mtMnSOD
D3J1L2
-
nectarin I
-
-
neelaredoxin
O29903
-
PASOD
Pyrobaculum aerophilum IM2
O93724
-
-
perMn-SOD
-
-
SOD
-
-
-
-
SOD
Q9Y8H8
-
SOD
Chaetomium thermophilum HSAUP072651
Q1HEQ0
-
-
SOD
B0L421, B2KYC6, B2KYC9
-
SOD
A7BI63
-
SOD
Kluyveromyces marxianus L3
B0B552
-
-
SOD
Penicillium marneffei
B6QEB3
-
SOD
Rhodothermus sp.
-
-
SOD
Sulfolobus solfataricus Gtheta
-
-
-
SOD
-
-
SOD 1
-
-
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SOD1
C7EXL1
-
SOD1
Beauveria bassiana 2860
C7EXL1
-
-
SOD1
-
-
SOD1
P00441
-
SOD1
Kluyveromyces marxianus L3
B0B552
-
-
SOD1
Rattus norvegicus Wistar
-
-
-
SOD2
-
-
SODA
Q2KN28
-
SODB1
Q381J5
-
SODB2
Q2KN30
-
SodC
Burkholderia cenocepacia K56-2
-
-
-
SodC
Q2KN29
-
SODF
-
-
-
-
SODS
-
-
-
-
SSO0316
P80857
locus name
SSO0316
P80857
locus name
-
superoxidase dismutase
-
-
-
-
superoxide dismutase
Amphiprora kufferathii, Pibocella sp.
-
-
superoxide dismutase
Pibocella sp. MH3
-
-
-
superoxide dismutase
Sulfitobacter sp.
-
-
superoxide dismutase
Sulfitobacter sp. MH1
-
-
-
superoxide dismutase 1
-
-
superoxide dismutase 1
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
MnSOD1
Bacillus cereus 905
Q6QHT3
-
-
additional information
-
the enzyme belongs to the superoxide dismutase family of important antioxidant metalloenzymes that catalyze superoxide radicals from cellular oxidative metabolism into hydrogen peroxideand molecular oxygen
CAS REGISTRY NUMBER
COMMENTARY
9054-89-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acholeplasma laidlawii Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
strain LFI1238, gene sodB
SwissProt
Manually annotated by BRENDA team
Amphiprora kufferathii
-
-
-
Manually annotated by BRENDA team
Anas platyrhynchos domestica
Cu,Zn-SOD; Peking duck
-
-
Manually annotated by BRENDA team
Anas platyrhynchos domestica CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
three types of Cu/ZNSOD
-
-
Manually annotated by BRENDA team
5 isozymes: SOD-II, SOD-III, SOD-IV, and SOD-V are Cu,Zn-SODs, SOD-I is a Mn-SOD
-
-
Manually annotated by BRENDA team
Arthrospira platensis Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
3 isozymes: Mn-SOD, Cu,Zn-SOD I and II
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Aspergillus flavus CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
SwissProt
Manually annotated by BRENDA team
Aspergillus fumigatus CuZn-SOD
Cu,Zn-SOD
SwissProt
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
strain 26
-
-
Manually annotated by BRENDA team
Aspergillus niger 26
strain 26
-
-
Manually annotated by BRENDA team
Aspergillus niger CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Aspergillus terreus CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Azotobacter chroococcum Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
MnSOD1; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-1
UniProt
Manually annotated by BRENDA team
MnSOD2; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-2
UniProt
Manually annotated by BRENDA team
Bacillus cereus 905
MnSOD1; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-1
UniProt
Manually annotated by BRENDA team
Bacillus cereus 905
MnSOD2; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-2
UniProt
Manually annotated by BRENDA team
IFO 3329; Mn-SOD
-
-
Manually annotated by BRENDA team
Bacillus circulans Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
superoxide dismutase paralog lacking two Cu ligands and without enzymic activity
-
-
Manually annotated by BRENDA team
; Fe-SOD, when grown anaerobically
-
-
Manually annotated by BRENDA team
Mn-SOD, O2-inducible
-
-
Manually annotated by BRENDA team
4 genes and 1 isozyme of MnSOD
UniProt
Manually annotated by BRENDA team
5 genes and 7 isozymes of CuZnSOD
UniProt
Manually annotated by BRENDA team
gene BbSod1
UniProt
Manually annotated by BRENDA team
Beauveria bassiana 2860
gene BbSod1
UniProt
Manually annotated by BRENDA team
isoform MnSOD, expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
silkworm
-
-
Manually annotated by BRENDA team
commercial prepapration, enzyme additionally catalyzes the reductive decomposition of S-nitroso-L-glutathione in presence of thiols
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
enzyme has a divalent-metal dependent nucleolytic activity, DNA-cleavage obeys Michaelis-Menten kinetics
Uniprot
Manually annotated by BRENDA team
isoform SOD1
-
-
Manually annotated by BRENDA team
Bos taurus CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; var. bullata sub var. gemmifera
-
-
Manually annotated by BRENDA team
Brassica oleracea CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Brassica rapa subsp. campestris Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
; strain K56-2
-
-
Manually annotated by BRENDA team
Burkholderia cenocepacia K56-2
strain K56-2
-
-
Manually annotated by BRENDA team
SOD-3 gene, Mn-SOD
Uniprot
Manually annotated by BRENDA team
Canis lupus familiaris CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn superoxide dismutase, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; strain CB15
-
-
Manually annotated by BRENDA team
Caulobacter vibrioides CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Chaetomium thermophilum CT2
strain CT2
-
-
Manually annotated by BRENDA team
Chaetomium thermophilum HSAUP072651
gene Ctsod
UniProt
Manually annotated by BRENDA team
Cinnamomum camphora Fe-SOD
Fe-SOD
Uniprot
Manually annotated by BRENDA team
cv. sugar baby
Uniprot
Manually annotated by BRENDA team
Cu,Zn-SOD
Uniprot
Manually annotated by BRENDA team
Citrus limon CuZn-SOD
Cu,Zn-SOD
Uniprot
Manually annotated by BRENDA team
Cu/ZnSOD; Cu/ZnSOD
SwissProt
Manually annotated by BRENDA team
expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
gene CuZnSOD
-
-
Manually annotated by BRENDA team
3 isozymes; Fe-SOD
-
-
Manually annotated by BRENDA team
Crithidia fasciculata Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
ATCC 50050, a heterotrophic dinoflagellate, a multi-copy gene family comprising genes sod1-sod17 encoding FeSODs
UniProt
Manually annotated by BRENDA team
FeSOD fragment; ATCC 50050, a heterotrophic dinoflagellate, a multi-copy gene family comprising genes sod1-sod17 encoding FeSODs
UniProt
Manually annotated by BRENDA team
isoform SOD2
-
-
Manually annotated by BRENDA team
Mn-SOD, and 2 isozymes of Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
expression in Escherichia coli with His-tag
-
-
Manually annotated by BRENDA team
strain AB
UniProt
Manually annotated by BRENDA team
Danio rerio AB
strain AB
UniProt
Manually annotated by BRENDA team
a grass specie adapted to the extreme climate of the Maritime Antarctic
-
-
Manually annotated by BRENDA team
Desulfovibrio gigas Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Dirofilaria immitis CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Drosophila melanogaster CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Emericella nidulans CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Empedobacter brevis CCM 2867
CCM 2867
-
-
Manually annotated by BRENDA team
strain IFO 3317
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes IFO 3317
strain IFO 3317
-
-
Manually annotated by BRENDA team
Fe-SOD; Mn-SOD
-
-
Manually annotated by BRENDA team
Fe-SOD; strain B
-
-
Manually annotated by BRENDA team
manganese superoxide dismutase
-
-
Manually annotated by BRENDA team
manganese superoxide dismutase
Uniprot
Manually annotated by BRENDA team
Escherichia coli Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Escherichia coli Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
A-101, A-217, A-364
-
-
Manually annotated by BRENDA team
several FeSOD and MnSOD isozymes
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Gallus gallus CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Fe-SOD: 2 isozymes, contains also Zn2+ and Cu2+; Mn-SOD, Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
IFO 3268, Mn-SOD
-
-
Manually annotated by BRENDA team
isoform MnSOD
SwissProt
Manually annotated by BRENDA team
strain NRL, enzyme is oxygen-inducible
-
-
Manually annotated by BRENDA team
Halobacterium salinarum NRL
strain NRL, enzyme is oxygen-inducible
-
-
Manually annotated by BRENDA team
CCM 2833; Fe-SOD and Mn-SOD
-
-
Manually annotated by BRENDA team
Halomonas halmophila CCM 2833
CCM 2833
-
-
Manually annotated by BRENDA team
contains a single type A isozyme Fe-SOD encoded by gene sodB
-
-
Manually annotated by BRENDA team
Heterometrus fulvipes Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; Mn-SOD
-
-
Manually annotated by BRENDA team
CuZn-type enzyme, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
EC-SOD with Cu,Zn-SOD activity
-
-
Manually annotated by BRENDA team
gene sod-1
-
-
Manually annotated by BRENDA team
healthy Japanese and Caucasian individuals
-
-
Manually annotated by BRENDA team
isoform hSOD3, expression in Pichia pastoris
-
-
Manually annotated by BRENDA team
isoform MnSOD
-
-
Manually annotated by BRENDA team
isoform SOD1
-
-
Manually annotated by BRENDA team
manganese superoxide dismutase
-
-
Manually annotated by BRENDA team
MnSOD
UniProt
Manually annotated by BRENDA team
patients undergoing bypass graft surgery
-
-
Manually annotated by BRENDA team
patients with familial amyotrophic lateral scerosis FALS
-
-
Manually annotated by BRENDA team
patients with idiopathic pulmonary fibrosis/usual interstitial pneumonia
-
-
Manually annotated by BRENDA team
Homo sapiens CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Homo sapiens Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
strain 103, isozymes Cu/Zn-SOD and Mn-SOD
-
-
Manually annotated by BRENDA team
Humicola lutea 103
strain 103, isozymes Cu/Zn-SOD and Mn-SOD
-
-
Manually annotated by BRENDA team
fall webworm, gene sod
UniProt
Manually annotated by BRENDA team
SOD1; strain L3, gene KmSod1
UniProt
Manually annotated by BRENDA team
strain NBIMCC 1984
-
-
Manually annotated by BRENDA team
Kluyveromyces marxianus L3
SOD1; strain L3, gene KmSod1
UniProt
Manually annotated by BRENDA team
Kluyveromyces marxianus NBIMCC 1984
strain NBIMCC 1984
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Lens culinaris CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Leptolyngbya boryana Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
expression in potato
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; var. diptera
-
-
Manually annotated by BRENDA team
Marchantia paleacea CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Marinomonas sp.
strain NJ522
-
-
Manually annotated by BRENDA team
strain NJ522
-
-
Manually annotated by BRENDA team
cytMnSOD fragment; i.e. Penaeus japonicus
UniProt
Manually annotated by BRENDA team
mtMnSOD fragment; i.e. Penaeus japonicus
UniProt
Manually annotated by BRENDA team
Cu/Zn superoxide dismutase
SwissProt
Manually annotated by BRENDA team
Methanobacterium bryantii Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
strain AZ, strict anaerobic methanogenic archaeon
-
-
Manually annotated by BRENDA team
Methanobrevibacter arboriphilus AZ
strain AZ, strict anaerobic methanogenic archaeon
-
-
Manually annotated by BRENDA team
Fe-SOD, but features are similar to Mn-SOD
-
-
Manually annotated by BRENDA team
strain SK1, DSM 8269
-
-
Manually annotated by BRENDA team
strain SK1, DSM 8269
-
-
Manually annotated by BRENDA team
Microbacterium maritypicum NCMB 559
NCMB 559
-
-
Manually annotated by BRENDA team
scallop Mn-superoxide dismutase
-
-
Manually annotated by BRENDA team
homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice
-
-
Manually annotated by BRENDA team
infected with Salmonella typhimurium and Pseudomonas aeruginosa
-
-
Manually annotated by BRENDA team
male C57BL/6 mice
-
-
Manually annotated by BRENDA team
CCM 2873
-
-
Manually annotated by BRENDA team
Myroides odoratus CCM 2873
CCM 2873
-
-
Manually annotated by BRENDA team
adult, 3 isoforms
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; Mn-SOD
-
-
Manually annotated by BRENDA team
Neurospora crassa CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Neurospora crassa Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
nectarin I with Mn-SOD activity
-
-
Manually annotated by BRENDA team
isozyme Cu,Zn-SODIII
-
-
Manually annotated by BRENDA team
no activity in Colwellia sp.
strain MH2
-
-
Manually annotated by BRENDA team
no activity in Colwellia sp. MH3
strain MH2
-
-
Manually annotated by BRENDA team
strain GUH-2; structural intermediate between Mn-SOD and Fe-SOD, Zn-containing
-
-
Manually annotated by BRENDA team
Nocardia asteroides GUH-2
strain GUH-2
-
-
Manually annotated by BRENDA team
formerly Anabaena sp., strain PCC 7120
-
-
Manually annotated by BRENDA team
Fe-SOD; sub spec. macrophyllum
-
-
Manually annotated by BRENDA team
Nuphar lutea Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Penicillium marneffei
gene sodA
UniProt
Manually annotated by BRENDA team
intracellular parasite of the Eastern oyster crassostrea virginica
-
-
Manually annotated by BRENDA team
Fe-SOD; subsp. piscicida, formerly Pasteurelle piscicida
SwissProt
Manually annotated by BRENDA team
Photobacterium damselae Fe-SOD
Fe-SOD
SwissProt
Manually annotated by BRENDA team
Cu,Zn-SOD; strain ATCC25521
-
-
Manually annotated by BRENDA team
Photobacterium leiognathi ATCC25521
strain ATCC25521
-
-
Manually annotated by BRENDA team
Photobacterium leiognathi CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
isolated from Euphorbia characias, isozymes SODI, SODII
-
-
Manually annotated by BRENDA team
expression of three enzyme isoforms
-
-
Manually annotated by BRENDA team
Pibocella sp.
strain MH3
-
-
Manually annotated by BRENDA team
Pibocella sp. MH3
strain MH3
-
-
Manually annotated by BRENDA team
4 isozymes: SOD-I, SOD-II, SOD-III, SOD-IV
-
-
Manually annotated by BRENDA team
expression in tobacco leaves, enzyme has superoxide dismutase activity, but no oxalate oxidase activity
SwissProt
Manually annotated by BRENDA team
Pisum sativum Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Planomicrobium okeanokoites NCMB 561
NCMB 561
-
-
Manually annotated by BRENDA team
Porphyridium purpureum Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
metal content depends on O2-concentration; structural intermediate between Mn-SOD and Fe-SOD
-
-
Manually annotated by BRENDA team
structural intermediate between Mn-SOD and Fe-SOD
-
-
Manually annotated by BRENDA team
structural intermediate between Mn-SOD and Fe-SOD
-
-
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
Mn-SOD; strain DSM 1083
-
-
Manually annotated by BRENDA team
Pseudomonas carboxydohydrogena Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
MnSOD encoded by gene sodA, and FeSOD encoded by gene sodB
-
-
Manually annotated by BRENDA team
strains KT2440 and PAO1, gene sodB
-
-
Manually annotated by BRENDA team
Pseudomonas putida Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Pyrobaculum aerophilum IM2
-
SwissProt
Manually annotated by BRENDA team
Radix lethospermi
-
-
-
Manually annotated by BRENDA team
180 female Hanover Wistar rats
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; Mn-SOD
-
-
Manually annotated by BRENDA team
isoform MnSOD
-
-
Manually annotated by BRENDA team
male rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Rattus norvegicus CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Rattus norvegicus Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
male rats
-
-
Manually annotated by BRENDA team
aerobically grown; Mn-SOD
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Rhodothermus sp.
strain XMH10
-
-
Manually annotated by BRENDA team
strain XMH10
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD; Mn-SOD
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CuZn-SOD
Cu,Zn-SOD
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
a human pathogenic fungus, strain 90.4595, gene sodC
-
-
Manually annotated by BRENDA team
strain Rm5000; structural intermediate between Mn-SOD and Fe-SOD
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti Rm5000
strain Rm5000
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD: 2 isozymes I and II
-
-
Manually annotated by BRENDA team
Solanum lycopersicum Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Spinacia oleracea Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
2 isoenzymes I and II
-
-
Manually annotated by BRENDA team
Mn-SOD and Fe-SOD
-
-
Manually annotated by BRENDA team
Sulfitobacter sp.
strain MH1
-
-
Manually annotated by BRENDA team
Sulfitobacter sp. MH1
strain MH1
-
-
Manually annotated by BRENDA team
strain DSM 639
-
-
Manually annotated by BRENDA team
strain DSM 639, gene adk
-
-
Manually annotated by BRENDA team
oxygen-inducible, extracellular Fe-SOD; strain Gtheta
-
-
Manually annotated by BRENDA team
strain MT-4, ATCC 49255
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus Gtheta
strain Gtheta
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT-4
strain MT-4, ATCC 49255
-
-
Manually annotated by BRENDA team
MnSOD
SwissProt
Manually annotated by BRENDA team
var. levisporus
Q1HDV5
UniProt
Manually annotated by BRENDA team
var. levisporus, gene sod
UniProt
Manually annotated by BRENDA team
Thermomyces lanuginosus P134
strain P134
-
-
Manually annotated by BRENDA team
Thermoplasma acidophilum Fe-SOD
Fe-SOD
-
-
Manually annotated by BRENDA team
Thermus aquaticus Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Mn-SOD; strain HB8
-
-
Manually annotated by BRENDA team
recombinant protein, isolation as metal-free apoprotein
-
-
Manually annotated by BRENDA team
Thermus thermophilus Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
iron superoxide dismutase A
SwissProt
Manually annotated by BRENDA team
iron superoxide dismutase B1
SwissProt
Manually annotated by BRENDA team
iron superoxide dismutase B2
SwissProt
Manually annotated by BRENDA team
iron superoxide dismutase C
Q2KN29
SwissProt
Manually annotated by BRENDA team
isolated from a hot spring sample
-
-
Manually annotated by BRENDA team
Virgibacillus halodenitrificans Mn-SOD
Mn-SOD
-
-
Manually annotated by BRENDA team
Cu,Zn-SOD: 3 isozymes AA, AB, BB
-
-
Manually annotated by BRENDA team
SOD-I
-
-
Manually annotated by BRENDA team
SOD-III; SOD-II, SOD-IV both belonging to Cu,Zn-SODs
-
-
Manually annotated by BRENDA team
Zea mays SOD-I
SOD-I
-
-
Manually annotated by BRENDA team
Zea mays SOD-III
SOD-III
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the exogenous manganese superoxide dismutase is able to modify the intracellular level of reactive oxygen species by eliminating superoxide anion and producing hydrogen peroxide. The cell viability of the two tumoral cell lines, porcine aortic endothelial cells and B16F0 mouse melanoma cells, exposed to the enzyme, is not significantly affected but the cell multiplication is arrested. The enzyme is involved in the control of several biological processes including cell proliferation
physiological function
-, Q5UVY7
SOD detoxifies the highly reactive superoxide anions to hydrogen peroxide and molecular oxygen
physiological function
Q9Y8H8
superoxide dismutases play a protective role against oxidative stress by catalyzing disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen
physiological function
-
protection by recombinant Cp-icCuZnSOD against alcohol-injury in human hepatocyte L02 cell line
physiological function
-
expression and activity of the mitochondrial P450 system along with substrate availability may contribute to mitochondrial function regulation via activation of IMS SOD1. Activation of intermembrane space SOD1 after incubation of rat liver intact mitochondria with P450 substrates significantly prevents the loss of aconitase activity in the mitochondrial matrix, general mechanism for the SOD1 activation mediated by P450 enzymes, overview
physiological function
-
manganese superoxide dismutase enzymes catalyze superoxide disproportionation by a mechanism that is more complex than those of the other SOD types. In particular the reduction of superoxide can proceed via one of two pathways. One pathway dominates when the O2- concentration is low relative to the enzyme concentration, and the other pathway dominates when the ratio [O2-]/[MnSOD] is high, overview
physiological function
Q6B7T0, -
the enzyme may play essential roles for survival of the parasite not only by protecting itself from endogenous oxidative stress, but also by detoxifying oxidative killing of the parasite by host immune effector cells
physiological function
D0UXW7, D0UXW8
different SOD isozymes might play different roles in the developmental and tissue-specific regulation, the higher SOD activity in the middle part of the shoots can scavenge the fast-producing reactive oxygen species because it is the most abundant cell-division region; different SOD isozymes might play different roles in these developmental, the higher SOD activity in the middle part of the shoots can scavenge the fast-producing reactive oxygen species because it is the most abundant cell-division region
physiological function
O29903
detoxification of superoxide
physiological function
Rattus norvegicus Wistar
-
expression and activity of the mitochondrial P450 system along with substrate availability may contribute to mitochondrial function regulation via activation of IMS SOD1. Activation of intermembrane space SOD1 after incubation of rat liver intact mitochondria with P450 substrates significantly prevents the loss of aconitase activity in the mitochondrial matrix, general mechanism for the SOD1 activation mediated by P450 enzymes, overview
-
malfunction
-
MnSOD ala16val polymorphism is associated with various diseases including breast cancer
additional information
-
CpSOD contains an intracellular disulfide bond and two CuZnSOD family signatures
additional information
-
the chimeric protein MnSOD-VHb is a dimer, in which the two subunits are associated via interaction between the SOD portions, since MnSOD monomers show a 40fold reduction in activity, but our chimeric MnSOD-VHb retained 84% activity compared to native MnSOD
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD, cambialistic nature of SmSOD, overview
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD, cambialistic nature of SmSOD, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Q2TV65
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
C7DRQ4, -
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-, B6ENP9
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
superoxide dismutase is a key enzyme for the protection of aerobic organisms against toxic radicals produced during oxidative processes, dismutation of superoxide in a two-step reaction: 1. O2.- + Fe3+-SOD = O2 + Fe2+-SOD, 2. O2.- + Fe2+-SOD + 2 H+ = H2O2 + Fe3+-SOD
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
activity determination by the epinephrine assay: at alkaline pH, superoxide anion O2- causes the oxidation of epinephrine to adrenochrome, SOD competes with this reaction by decreasing the adrenochrome formation
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
C7DRQ4, -
enzyme activity assay by measurement of inhibition of reduction of cytochrome c by O2- produced by the xanthine oxidase/xanthine reaction
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
enzyme activity determination by xanthine-xanthine oxidase-nitro blue tetrazolium assay
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Kluyveromyces marxianus NBIMCC 1984
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Danio rerio AB
Q2TV65
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Sulfolobus solfataricus Gtheta
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
Q9Y8H8
-, the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
nitro blue tetrazolium + ?
?
show the reaction diagram
-
-
-
-
?
nitro blue tetrazolium + ?
?
show the reaction diagram
-
-
-
-
?
Nitroblue Tetrazolium + ?
?
show the reaction diagram
Marinomonas sp., Marinomonas sp. NJ522
-
enzyme inhibits superoxide-induced reduction of colorless Nitroblue Tetrazolium dye to its oxidized blue formazan form
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
r
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q96UT6
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
r
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q71S31
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q9Y8D9
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
P81527
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Anas platyrhynchos domestica
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
O82519
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
P84612
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Radix lethospermi
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-, Q7X4G4
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q8MUI5, -
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q65Y02
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q0PKG3
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q71S33, -
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q96UT6
Mn-SOD, expression is strongly stimulated during stationary phase in cell culture, enzyme is atypical and plays an important role in cell protection against reactive oxygen in the cytosol in the stationary phase
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rattus norvegicus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rattus norvegicus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Drosophila melanogaster CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Drosophila melanogaster CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Azotobacter chroococcum Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermus thermophilus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermus thermophilus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Spinacia oleracea Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Halomonas halmophila CCM 2833
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Gallus gallus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Acholeplasma laidlawii Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Methanobrevibacter arboriphilus AZ
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pisum sativum Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pisum sativum Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pisum sativum Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Empedobacter brevis CCM 2867
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Solanum lycopersicum Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Emericella nidulans CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Methanobacterium bryantii Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Brassica oleracea CuZn-SOD
-
-
-
r
O2- + H+
O2 + H2O2
show the reaction diagram
Leptolyngbya boryana Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium damselae Fe-SOD
P81527
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Arthrospira platensis Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Lens culinaris CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi CuZn-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Caulobacter vibrioides CuZn-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Caulobacter vibrioides CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Porphyridium purpureum Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Marchantia paleacea CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pseudomonas putida Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pseudomonas putida Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Aspergillus niger CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Nocardia asteroides GUH-2
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Planomicrobium okeanokoites NCMB 561
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi ATCC25521
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Canis lupus familiaris CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bacillus circulans Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Desulfovibrio gigas Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Neurospora crassa CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Neurospora crassa CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Zea mays SOD-III
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Mn-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Fe-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Paracoccus denitrificans CuZn-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Paracoccus denitrificans CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermus aquaticus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Nuphar lutea Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Myroides odoratus CCM 2873
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
-
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
r
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rhodobacter sphaeroides Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Zea mays SOD-I
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Microbacterium maritypicum NCMB 559
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Paracoccus denitrificans Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Dirofilaria immitis CuZn-SOD
-
-, defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Enterobacter aerogenes IFO 3317
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Aspergillus flavus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Crithidia fasciculata Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Pseudomonas carboxydohydrogena Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
show the reaction diagram
Sinorhizobium meliloti Rm5000
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Heterometrus fulvipes Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Virgibacillus halodenitrificans Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermomyces lanuginosus P134
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Neurospora crassa Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermoplasma acidophilum Fe-SOD
-
-
-, Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rattus norvegicus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rattus norvegicus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Rattus norvegicus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Brassica rapa subsp. campestris Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Homo sapiens Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Halobacterium salinarum NRL
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Anas platyrhynchos domestica CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Aspergillus terreus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Aspergillus fumigatus CuZn-SOD
Q9Y8D9
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Sulfolobus solfataricus Gtheta
-
-, defense against oxidants
-
?
O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate
?
show the reaction diagram
A7BI63
i.e. WST-1, activity assay detection method
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
P04179
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
P00441
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Q6QGY4
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Q1HDV5, -
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A6MHS2, -, Q6QHT3
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Rhodothermus sp.
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-, Q52JH6
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Penicillium marneffei
B6QEB3
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
B0L421, B2KYC6, B2KYC9, -
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A7BI63
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
B0B552, -
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
a key enzyme for fighting oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
B0L421, B2KYC6, B2KYC9, -
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
Deinococcus radiodurans Mn-SOD is most effective at high superoxide fluxes found under conditions of high radioactivity compared to te enzyme of Escherichia coli and Homo sapiens
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments, thereby preventing activation of polymorphic neutrophil chemotaxis by fragmented hyaluronic acid, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid via its matrix-binding domain and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
enzyme inhibition by tetrathiomolybdate leads to antiangiogenic and antitumour effects in mice
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
extracellular superoxide dismutase accelerates endothelial recovery and inhibits in-stent restenosis in stented atherosclerotic Watanabe heritable hyperlipidemic rabbit aorta. Extracellular superoxide dismutase, EC-SOD, is a major component of antioxidative defense in blood vessels, and exogenously delivered EC-SOD protects against balloon-induced neointima formation and constrictive remodeling and has powerful cardioprotective properties, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A6MHS2, -, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A6MHS2, -, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in mice with combined leptin and LDL-receptor deficiency, and in THP-1 macrophages and foam cells in vitro, thus, SOD1 is a potentially important mediator of the prevention of oxLDL accumulation within atherosclerotic plaques, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A7BI63
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Penicillium marneffei
B6QEB3
the enzyme contributes to the virulence of many human-pathogenic fungi through its ability to neutralize toxic levels of reactive oxygen species generated by the host
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme mutation E93A leads to a decrease in muscle cdk5 activity accompanied by a significant reduction in MyoD and cyclin D1 levels causing amyotrophic lateral sclerosis, a primarily a motor neuron disorder with early muscle denervation preceding motor neuron loss, the progressive deterioration of muscle function is potentiated by altered muscle biochemistry in these mice at a very young, presymptomatic age, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
P04179
the conserved, active-site residue Tyr34 mediates product inhibition
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Bacillus cereus 905
A6MHS2, Q6QHT3
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Bacillus cereus 905
A6MHS2, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Bacillus cereus 905
A6MHS2, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Kluyveromyces marxianus L3
B0B552
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Burkholderia cenocepacia K56-2
-
-, periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Aspergillus niger 26
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Humicola lutea 103
-
-
-
-
?
pyrogallol + ?
?
show the reaction diagram
Q8J0N2
-
-
-
?
pyrogallol + ?
?
show the reaction diagram
-
enzyme inhibits the autooxidation of pyrogallol
-
-
?
pyrogallol + ?
?
show the reaction diagram
Q8J0N2
enzyme inhibits the autooxidation of pyrogallol
-
-
?
riboflavin + ?
?
show the reaction diagram
-
-
-
-
?
riboflavin + ?
?
show the reaction diagram
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
O29903
-, detoxification of superoxide
-
-
?
additional information
?
-
-
enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
-
-
-
additional information
?
-
-
addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
-
-
-
additional information
?
-
-
dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
-
-
-
additional information
?
-
-
Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
-
-
-
additional information
?
-
-
enzyme is involved in pathogenesis of the parasite by protecting it from oxidative killing
-
-
-
additional information
?
-
-
enzyme Sod2 is a major component of the antioxidant defense system, and adaptation to elevated growth temperatures is also dependent on enzyme activity
-
-
-
additional information
?
-
-
higher levels of oxidative stress may induce changes in photochemicla efficiency of photosystem II
-
-
-
additional information
?
-
-
MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
-
-
-
additional information
?
-
-
superoxide dismutase activity in Pseudomonas putida affects utilization of sugars and growth on root surfaces, role of SOD in root colonization and oxidative stress, overview
-
-
-
additional information
?
-
-
the enzyme is required for virulence of the organism, e.g. in silkworm Bombyx mori, with iron-SOD being more important, overview
-
-
-
additional information
?
-
-
covalent modification of the conserved Tyr41 in the active site, Tyr41 and His155 are involved in catalysis, hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, Y41 and H155 are important for the structural and functional properties of SOD, overview
-
-
-
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
-
additional information
?
-
P80857
native and recombinant enzyme ossess a covalent modification of the conserved Tyr41 in the active site, Tyr41 plays an important role in the enzyme activity and the maintenance of the structural architecture of SOD, overview
-
-
-
additional information
?
-
-
unusual covalent modification of the conserved Tyr41 in the active site, interactions Tyr41-His155, overview
-
-
-
additional information
?
-
-
EC-SOD protects the lung in both bleomycin- and asbestos-induced models of pulmonary fibrosis
-
-
-
additional information
?
-
-
inverse relationship between SOD1 expression and ox-LDL in plaque plays a role in oxidative stress contributes to post-ischaemic injury in the heart, increasing SOD1 protects against this increased oxidative stress
-
-
-
additional information
?
-
-
pharmacokinetics of single and multiple doses of recombinant human superoxide dismutase covalently linked to lecithin in healthy Japanese and Caucasian volunteers are nonlinear with dose, showing a relatively long half-life of PC-SOD of over 24 hours, overview
-
-
-
additional information
?
-
-
pharmacokinetics, safety and tolerability of single rising doses up to 80 mg of recombinant human superoxide dismutase covalently linked to lecithin in healthy white volunteers, overview
-
-
-
additional information
?
-
B0B552, -
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
-
additional information
?
-
-
SOD inhibits the autoxidation of pyrogallol
-
-
-
additional information
?
-
-
enzyme activity determination by NBT reduction
-
-
-
additional information
?
-
Q6QGY4
SOD activity measurement by the ferricytochrome c method, using xanthine/xanthine oxidase as the source of superoxide radicals
-
-
-
additional information
?
-
-
SOD activity measurement using the nitroblue tetrazolium
-
-
-
additional information
?
-
-
the enzyme is involved in activation and modulation of phospho-extracellular signal-regulated kinases proteins and in the control of several biological processes including cell proliferation
-
-
-
additional information
?
-
-
coupled assay method using inhibition of the autooxidation of pyrogallol
-
-
-
additional information
?
-
-
enzyme activity assay using nitroblue tetrazolium and riboflavin
-
-
-
additional information
?
-
-
SOD enzyme activity measurement is based on the inhibition of nitroblue tetrazolium reduction by superoxide radical generated by xanthine/xanthine oxidase
-
-
-
additional information
?
-
Rattus norvegicus CuZn-SOD
-
dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
-
-
-
additional information
?
-
Bos taurus CuZn-SOD
-
enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
-
-
-
additional information
?
-
Bos taurus CuZn-SOD
-
addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
-
-
-
additional information
?
-
Kluyveromyces marxianus L3
B0B552
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
-
additional information
?
-
Aspergillus niger 26
-
SOD activity measurement using the nitroblue tetrazolium
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Q2TV65
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
C7DRQ4, -
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-, B6ENP9
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
superoxide dismutase is a key enzyme for the protection of aerobic organisms against toxic radicals produced during oxidative processes
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Kluyveromyces marxianus NBIMCC 1984
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Danio rerio AB
Q2TV65
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
Sulfolobus solfataricus Gtheta
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
Q9Y8H8
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Q96UT6
Mn-SOD, expression is strongly stimulated during stationary phase in cell culture, enzyme is atypical and plays an important role in cell protection against reactive oxygen in the cytosol in the stationary phase
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Bos taurus CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Photobacterium leiognathi CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Caulobacter vibrioides CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Caulobacter vibrioides CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Escherichia coli Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Paracoccus denitrificans CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Dirofilaria immitis CuZn-SOD
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Geobacillus stearothermophilus Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Thermoplasma acidophilum Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Saccharomyces cerevisiae Mn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
Sulfolobus solfataricus Gtheta
-
defense against oxidants
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
P04179
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
P00441
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Q6QGY4
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Q1HDV5, -
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Rhodothermus sp.
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-, Q52JH6
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
B0B552, -
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
a key enzyme for fighting oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
B0L421, B2KYC6, B2KYC9, -
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
Deinococcus radiodurans Mn-SOD is most effective at high superoxide fluxes found under conditions of high radioactivity compared to te enzyme of Escherichia coli and Homo sapiens
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments, thereby preventing activation of polymorphic neutrophil chemotaxis by fragmented hyaluronic acid, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid via its matrix-binding domain and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
enzyme inhibition by tetrathiomolybdate leads to antiangiogenic and antitumour effects in mice
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
extracellular superoxide dismutase accelerates endothelial recovery and inhibits in-stent restenosis in stented atherosclerotic Watanabe heritable hyperlipidemic rabbit aorta. Extracellular superoxide dismutase, EC-SOD, is a major component of antioxidative defense in blood vessels, and exogenously delivered EC-SOD protects against balloon-induced neointima formation and constrictive remodeling and has powerful cardioprotective properties, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A6MHS2, -, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A6MHS2, -, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in mice with combined leptin and LDL-receptor deficiency, and in THP-1 macrophages and foam cells in vitro, thus, SOD1 is a potentially important mediator of the prevention of oxLDL accumulation within atherosclerotic plaques, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
A7BI63
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Penicillium marneffei
B6QEB3
the enzyme contributes to the virulence of many human-pathogenic fungi through its ability to neutralize toxic levels of reactive oxygen species generated by the host
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme mutation E93A leads to a decrease in muscle cdk5 activity accompanied by a significant reduction in MyoD and cyclin D1 levels causing amyotrophic lateral sclerosis, a primarily a motor neuron disorder with early muscle denervation preceding motor neuron loss, the progressive deterioration of muscle function is potentiated by altered muscle biochemistry in these mice at a very young, presymptomatic age, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Bacillus cereus 905
A6MHS2, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Bacillus cereus 905
A6MHS2, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Kluyveromyces marxianus L3
B0B552
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Burkholderia cenocepacia K56-2
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Aspergillus niger 26
-
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
Humicola lutea 103
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
O29903
detoxification of superoxide
-
-
?
additional information
?
-
-
Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
-
-
-
additional information
?
-
-
enzyme is involved in pathogenesis of the parasite by protecting it from oxidative killing
-
-
-
additional information
?
-
-
enzyme Sod2 is a major component of the antioxidant defense system, and adaptation to elevated growth temperatures is also dependent on enzyme activity
-
-
-
additional information
?
-
-
higher levels of oxidative stress may induce changes in photochemicla efficiency of photosystem II
-
-
-
additional information
?
-
-
MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
-
-
-
additional information
?
-
-
superoxide dismutase activity in Pseudomonas putida affects utilization of sugars and growth on root surfaces, role of SOD in root colonization and oxidative stress, overview
-
-
-
additional information
?
-
-
the enzyme is required for virulence of the organism, e.g. in silkworm Bombyx mori, with iron-SOD being more important, overview
-
-
-
additional information
?
-
-
EC-SOD protects the lung in both bleomycin- and asbestos-induced models of pulmonary fibrosis
-
-
-
additional information
?
-
-
inverse relationship between SOD1 expression and ox-LDL in plaque plays a role in oxidative stress contributes to post-ischaemic injury in the heart, increasing SOD1 protects against this increased oxidative stress
-
-
-
additional information
?
-
-
pharmacokinetics of single and multiple doses of recombinant human superoxide dismutase covalently linked to lecithin in healthy Japanese and Caucasian volunteers are nonlinear with dose, showing a relatively long half-life of PC-SOD of over 24 hours, overview
-
-
-
additional information
?
-
-
pharmacokinetics, safety and tolerability of single rising doses up to 80 mg of recombinant human superoxide dismutase covalently linked to lecithin in healthy white volunteers, overview
-
-
-
additional information
?
-
B0B552, -
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
-
additional information
?
-
-
SOD inhibits the autoxidation of pyrogallol
-
-
-
additional information
?
-
-
the enzyme is involved in activation and modulation of phospho-extracellular signal-regulated kinases proteins and in the control of several biological processes including cell proliferation
-
-
-
additional information
?
-
Kluyveromyces marxianus L3
B0B552
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
a liganding water molecule is evident
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Al3+
-
activates by 10% at 10 mM
Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Co2+
-
Co(II) can substitute for zinc in erythrocytes
Co2+
-
Co2+ binds at zinc site
Co2+
-
27% stimulation of activity
copper
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
copper
Radix lethospermi
-
-
copper
-
1 atom per subunit
copper
-
coexpression with yeast copper chaperone, copper supplement of medium, about 1 atom per subunit
copper
-
-
copper
-
peculiar axial geometry of copper active sitewith low accessibility to external chelating agents
copper
Q8J0N2
0.68 mol per mol of subunit
copper
Q8J0N2
recombinant enzyme, 0.9 mol per mol of subunit, native enzyme, 0.86 mol per mol of subunit
copper
-
wild-type, 0.98 atoms per subunit, mutant H43R, 1.42, mutant A4V, 1.06 atoms per subunit
Cu
-
a Cu/Zn superoxide dismutase
Cu
C5H405
extracellular CuZnSOD
Cu
-
a Cu/Zn-SOD
Cu
-
a Cu,Zn superoxide dismutase
Cu
-
a Cu-Zn SOD, activates
Cu2+
-
heart: 1.64 mol of Cu per mol of enzyme, erythrocyte: 1.84 mol of Cu per mol of enzyme
Cu2+
-
no copper
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.1 mol per mol of Cu,Zn-SOD
Cu2+
-
-
Cu2+
-
1 gatom per mol of enzyme
Cu2+
-
1.63-1.78 mol per mol of isoenzyme I; 1.86-1.97 mol per mol of isoenzyme II
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.7 mol per mol of enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
SOD-1, SOD-2 and SOD-4
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
mitochondrial cyanide-sensitive enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1 gatom per mol of enzyme
Cu2+
Anas platyrhynchos domestica
-
-
Cu2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Cu2+
-
Cu,Zn-SOD mutant H63C
Cu2+
Q71S31
-
Cu2+
-
a Cu,ZnSOD
Cu2+
-
the concentration of enzyme bound Cu2+ is 1.63 mg/l, the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], replacement of natural cofactor Cu2+ by isotopically enriched 65Cu, method, overview
Cu2+
-
a Cu,Zn-SOD
Cu2+
A7BI63
a Cu,Zn-SOD
Cu2+
B0B552
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes, D84 is also involve in Cu2+ binding
Cu2+
-
isozyme Cu/Zn-SOD
Cu2+
-
isozyme Cu/Zn-SOD
Cu2+
Q1HDV5, -
a Cu,Zn-SOD
Cu2+
-
a CuZn-SOD
Cu2+
-
a Cu,Zn-SOD
Cu2+
-
a Cu,ZnSOD
Cu2+
-
a Cu,ZnSOD with 1.07 Cu2+ per enzyme subunit, binding structure, position of Cu2+ in the Zn2+-deficient enzyme A chain active site, overview, physiologic function in Cu,Zn-SOD, overview
Cu2+
Penicillium marneffei
B6QEB3
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Cu2+
-
a Cu,Zn-SOD
Cu2+
-, Q52JH6
a Cu,ZnSOD
Cu2+
-
a Cu,Zn-SOD
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
C7EXL1
a CuZn-superoxide dismutase
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
-
activates by 16% at 10 mM
Cu2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His46, His48, His63, and His120 for Cu2+ binding
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
Q6B7T0, -
a CuZn-superoxide dismutase
Cu2+
D0UXW7, D0UXW8
7 isozymes of CuZnSOD
Fe
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Fe2+
-
iron-SOD variant
Fe2+
Q08713
Fe/Mn-type SOD, the Fe-type enzyme contains Gln85
Fe2+
-
the homodimeric enzyme contains 0.7 atom of iron per subunit
Fe2+
P80857
Fe/Mn-type SOD
Fe2+
-
bound by His33, His84, His174, and Asp170, coordination in the active site, overview
Fe2+
-
Fe-type SOD, helices alpha1 and alpha2 contribute one metal ligand each, i.e. His33 and His84, binding structure, the iron is ligated by Nepsilon2 of His33, His84 and His174, by Odelta1 of Asp170, and a solvent molecule forming a distorted trigonal bipyramidal coordination sphere, overview
Fe2+
-
Fe-SOD contains 1 Fe2+ per subunit
Fe2+
Rhodothermus sp.
-
a Fe-SOD
Fe2+
-
a Fe,Mn-SOD, the purified enzyme contains 1.1 g-atom of Fe per mol enzyme
Fe2+
B0L421, B2KYC6, B2KYC9, -
all isozymes in the organism are FeSODs; all isozymes in the organism are FeSODs; all isozymes in the organism are FeSODs
Fe2+
-
FeSOD isozymes
Fe2+
-
the enzyme is an iron SOD with 0.9 Fe/subunit
Fe2+
Q9Y8H8
the SOD is active with Fe2+ and Mn2+, Fe2+ activates 6fold, binding structure, overview
Fe2+
O93724
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
0.9 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme; 2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
-
contains no iron
Iron
-
accepts iron and/or manganese as cofactor
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme; each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis
Iron
-
1.6 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme; 2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
Q96UT6
0.4 mol per mol of mn-SOD
Iron
O82519
0.5-1.0 atom Fe2+ per subunit
Iron
-
0.24 mol Fe2+ per mol of subunit
Iron
-, Q7X4G4
30% of the activity with manganese
Iron
-
1 atom per subunit
Iron
-
no change in the geometry of the FeII site occurs over a wide pH range
Iron
-
0.35 mol per mol of subunit, required both for activity and stability of enzyme tetramer
Iron
P0AGD3
spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzymes active site
Iron
-
1.1 mol per mol of subunit
Iron
P84612
0.75 atoms per subunit
Iron
-
when mitochondrial iron homeostasis is disrupted, iron accumulates in a reactive form and competes with manganese, inactivating the enzyme. The ability to control the iron pool within mitochondria is critical to maintaining enzyme activity
Iron
Q5K650, -
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Iron
-
iron-superoxide dismutase, FeSOD, encoded by gene sodB
Iron
-
Fe-type SodB
Iron
-
contains one iron atom per dimer, the protein contains a mononuclear iron center
Iron
O29903
the enzyme is a tetramer with 4 iron centers, one iron per monomer
Manganese
-, Q7X4G4
most effcient metal ion
Manganese
-
less than 0.1 mol per mol of subunit
Manganese
-
kinetic study on metal binding mechanism. Apo-enzyme metallation kinetics are gated, zero order in metal ion for both native Mn2+ and nonnative Co2+. Cobalt-binding reveals two exponential kinetic processes. Sensitivity of metallated protein to exogenously added chelator decreases with time, consistent with annealing of an initially formed metalloprotein complex
Manganese
Q5K650, -
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Manganese
P00448
analysis of manganese(II) high-field electron paramagnetic resonance spectrum. In the -248C to -73C range, the zero-field interaction steadily decreases with increasing temperature. Above -33C, a distinct six-line component is detected derived from a hexacoordinate Mn(II) center resulting from coordination of normally five-coordinate Mn(II) by a water molecule. comparison with Mn(II) centers in concanavalin A and R. spheroides photosynthetic center
Manganese
-
mitochondrial localization is essential for insertion of manganese to protein. Insertion is only possible with a newly synthesized polypeptide and seems to be driven by the protein unfolding process associated with mitochondrial import
Manganese
Q71S33, -
putatively coordinated by H27, H81, D167, H171
Manganese
-
manganese-superoxide dismutase, MnSOD, encoded by gene sodA
Manganese
-
Mn-type SodA
Manganese
-
when the Deinococcus radiodurans Mn2+SOD reacts with a substoichiometric amount of superoxide, Deinococcus radiodurans Mn3+SOD is produced
Manganese
-
a MnSOD
Mg2+
-
73% stimulation of activity
Mg2+
-
up to 48% activation
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn
-, C3W7U9
manganese superoxide dismutase; manganese superoxide dismutase
Mn
C3W7V0, -
manganese superoxide dismutase; manganese superoxide dismutase
Mn
C3W7V1, -
manganese superoxide dismutase; manganese superoxide dismutase
Mn
Q2TV65
a MnSOD
Mn
D3IU19, D3J1L2, -
cytosolic MnSOD isozymes, Mn binding sequence is DVWHHAYY; mitochondrial MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
A3RLW7, -
a manganese superoxide dismutase, contains 0.00246 mg Mn/mg protein, binding involves conserved residues H88, H136, D222, and H226
Mn
-
a Mn-SOD
Mn
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Mn2+
-
contains no manganese
Mn2+
-
isoform I, 1.85 atoms manganese per mol of enzyme
Mn2+
-
0.05 mol per mol of enzyme
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
0.22 mol per mol of enzyme
Mn2+
-
2.2 mol per mol of enzyme
Mn2+
-
1.5 mol per mol of enzyme
Mn2+
-
1.7 mol per mol of enzyme
Mn2+
-
4 mol per mol of enzyme
Mn2+
-
1.22 mol per mol of enzyme
Mn2+
-
-
Mn2+
-
contains no manganese
Mn2+
-
accepts iron and/or manganese as cofactor
Mn2+
-
0.5 mol per mol of subunit
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
3.69 mol per mol of enzyme
Mn2+
-
1 atom per subunit
Mn2+
-
2 atoms of manganese per molecule
Mn2+
-
1.22 mol per mol of enzyme
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
-
2 atoms of manganese per molecule
Mn2+
-
1 atom per subunit
Mn2+
-
less than 0.2 mol per mol of enzyme
Mn2+
Q96UT6
0.9 Mn per mol of enzyme
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
-
0.89 mol per mol of liver Mn-SOD
Mn2+
-
0.75 mol per mol of subunit; accepts iron and/or manganese as cofactor
Mn2+
-
0.5 mol per mol of subunit; specific for
Mn2+
-
1 atom per subunit
Mn2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn2+
-
manganese-SOD variant
Mn2+
Q08713
Fe/Mn-type SOD, the Mn-type enzyme contains Gly85
Mn2+
P80857
Fe/Mn-type SOD
Mn2+
-
isozyme Mn-SOD
Mn2+
-
a Mn-SOD
Mn2+
A6MHS2, -, Q6QHT3
isozyme MnSOD2, encoded by gene sodA-2; Mn-SOD isozyme MnSOD1, encoded by gene sodA-1, MnSOD1 is expressed at lower level compared to MnSOD2
Mn2+
-
isozyme SODI is a Mn-SOD
Mn2+
-
a Fe,Mn-SOD, the purified enzyme contains 0.7 g-atom of Mn per mol enzyme
Mn2+
-
a Mn-SOD
Mn2+
C7DRQ4, -
a MnSOD, activates, binding sequence is DVWEHAYY
Mn2+
-
0.00205 mg/mg of protein
Mn2+
-
MnSOD isozymes
Mn2+
E9RHW0
a manganese-containing superoxide dismutase
Mn2+
-
activates by 12% at 10 mM, Mn-containing superoxide dismutase
Mn2+
Q9Y8H8
the SOD is active with Fe2+ and Mn2+, Mn2+ activates 20fold, binding structure, overview
Mn2+
-
MnSOD
Mn2+
D0UXW7, D0UXW8
1 isozyme of MnSOD
Zinc
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
Zinc
Radix lethospermi
-
-
Zinc
-
0.5 atoms per subunit
Zinc
-
-
Zinc
-
-
Zinc
Q8J0N2
1.02 mol per mol of subunit
Zinc
Q8J0N2
recombinant enzyme, 0.51 mol per mol of subunit, native enzyme, 1.01 mol per mol of subunit
Zinc
-
wild-type, 1.08 atoms per subunit, mutant H43R, 1.11, mutant A4V, 1.43 atoms per subunit
Zn
-
in solution, 1 mol per mol of protein. In crystal, a second Zn is bound at the interface between the two enzyme molecules leading to the formation of covalently bound enzyme dimers
Zn
-
a Cu/Zn superoxide dismutase
Zn
C5H405
extracellular CuZnSOD
Zn
-
a Cu/Zn-SOD
Zn
-
a Cu,Zn superoxide dismutase
Zn
-
a Cu-Zn SOD
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
no zinc
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
-
2.2 mol per mol of enzyme
Zn2+
-
1.5 mol per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
-
1.2 mol per mol of enzyme
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
-
-
Zn2+
-
1.3 mol per mol of Cu,Zn-SOD
Zn2+
-
-
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
-
1.34-1.81 mol per mol of isoenzyme I; 1.9-20.0 mol per mol of isoenzyme II
Zn2+
-
1.6 mol per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.5 mol per mol of enzyme
Zn2+
-
SOD-1, SOD-2 and SOD-4
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme; mitochondrial cyanide-sensitive enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
0.85 mol per mol of enzyme
Zn2+
Anas platyrhynchos domestica
-
-
Zn2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Zn2+
Q71S31
-
Zn2+
-
a Cu,ZnSOD
Zn2+
-
the concentration of enzyme bound Zn2+ is 1.68 mg/l, the Zn ion plays a structural role, replacement of natural cofactor Zn2+ by isotopically enriched 68Zn, method, overview
Zn2+
-
a Cu,Zn-SOD
Zn2+
A7BI63
a Cu,Zn-SOD
Zn2+
B0B552
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes
Zn2+
-
isozyme Cu/Zn-SOD
Zn2+
-
isozyme Cu/Zn-SOD
Zn2+
Q1HDV5, -
a Cu,Zn-SOD
Zn2+
-
a CuZn-SOD
Zn2+
-
a Cu,Zn-SOD
Zn2+
-
a Cu,ZnSOD
Zn2+
-
a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview
Zn2+
Penicillium marneffei
B6QEB3
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Zn2+
-
a Cu,Zn-SOD
Zn2+
-, Q52JH6
a Cu,ZnSOD
Zn2+
-
a Cu,Zn-SOD
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
C7EXL1
a CuZn-superoxide dismutase
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
-
activates by 48% at 10 mM
Zn2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His63, His71, His80, and Asp83 for Zn2+ binding
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
Q6B7T0, -
a CuZn-superoxide dismutase
Zn2+
D0UXW7, D0UXW8
7 isozymes of CuZnSOD
Mn2+
O93724
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
metal content of the enzyme depends on the growth condition: anaerobic culture condition promote a higher Fe-content, aerobic conditions promote a higher Mn-content
additional information
-
Cu2+-binding site
additional information
-
relevance of the zinc imidazolate bond to the redox properties
additional information
-
role of copper and zinc in protein conformation and activity
additional information
-
Cu2+ is not necessarily required
additional information
-
Cu2+ and Zn2+ binding sites are very close to each other
additional information
Q96UT6
Mn-SOD contains as well Fe3+, but is only active with manganese
additional information
-
no effect: Cu2+, Ca2+
additional information
-
no effect: Cu2+, Co2+, Ca2+
additional information
P84612
protein contains no manganese
additional information
P80857
metal content analysis of the recombinant enzyme
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
additional information
-
the enzyme contains 7 metal binding sites
additional information
A7BI63
the enzyme contains 6 metal binding sites
additional information
B0L421, B2KYC6, B2KYC9, -
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
-
the enzyme contains no iron
additional information
-
the purified enzyme contains no Fe
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4,6-Trinitrobenzenesulfonate
-
0.5 M, pH 9.0, 25C, native wild-type enzyme: half-life 3.5 min, recombinant wild-type enzyme: half-life: 5.1 min, recombinant mutant H30A: half-life 5.5 min, recombinant mutant K170R half-life 101 min
4-chloromercuribenzoate
-
26.6% inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoate)
-
Mn-SOD
amitriptyline
-
-
beta-naphthoquinone-4-sulfonic acid
-
-
chloride
-
-
Chloroform
-
Mn-SOD
CN-
-
no inhibition
CN-
-
no inhibition
CN-
-
no inhibition
CN-
-
no inhibition
CN-
-
Cu,Zn-SOD
CN-
-
slight inhibition, Mn-SOD
CN-
-
extracellular enzyme
CN-
-
Cu,Zn-SOD; no inhibition Mn-SOD
CN-
-
no inhibition
CN-
-
SOD-2 and SOD-4 inhibited, SOD-3 not inhibited
CN-
-
contains a cyanide-sensitive enzyme in cytosol and mitochondrial intermembrane space and one cyanide-insensitive enzyme in mitochondrial matrix; Cu,Zn-SOD; no inhibition Mn-SOD
CN-
-
no inhibition Mn-SOD
CN-
-
at 1-3 mM, complete inhibition; Cu,Zn-SOD
CN-
-
no inhibition
CN-
-
no inhibition Mn-SOD
CN-
Q96UT6
slight inhibition, Mn-SOD
CN-
P81527
no inhibition
CN-
-
Cu,Zn-SOD
CN-
-
no inhibition: Fe-SOD
CN-
-
no inhibition Mn-SOD
Co2+
-
inhibits by 25% at 10 mM
concanavalin A
-
inhibition in vivo and in vitro, essentially dependent on calcium chloride
-
cyanide
Radix lethospermi
-
-
cyanide
-
the isoenzyme Cu/Zn-SOD is cyanide-sensitive, while the Mn-SOD is not
diethyl dicarbonate
-
at 2.5 mM
diethyldithiocarbamate
-
slightly
diethyldithiocarbamate
-
strong inhibition, extracellular enzyme
diethyldithiocarbamate
-
Mn-SOD; slightly
diethyldithiocarbamate
Q9Y8D9
complete inhibition, Cu,Zn-SOD
diethyldithiocarbamate
-
copper-chelator, wild-type and mutant Cu,Zn-SOD
diethyldithiocarbamate
-
inhibits recombinant Cu,Zn-SOD, at 0.05-0.1 mM inactivation occurs gradually within 1 h
diethyldithiocarbamate
-
causes decline of the enzyme in various tissues after intraperitoneal injection, alpha-tocopherol feeding prior to application of diethyldithiocarbamate leads to reduced inhibition of the enzyme
diethyldithiocarbamate
-
Cu,Zn-SOD
DTPA
-
i.e. diethylenetriamine-N,N,N,N,N-pentaacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
EDTA
-
Mn-SOD; slightly
EDTA
-
no inhibition
EDTA
Q9Y8D9
no inhibition
EDTA
Radix lethospermi
-
2 mM, 18% inhibition
EDTA
-
i.e. diethylenediamine-N,N,N,N-tetraacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
EDTA
Marinomonas sp.
-
slight inhibition
EDTA
-
66% inhibition at 1 mM
EDTA
-
inhibition is reversible by Cu and Zn
EGTA
Marinomonas sp.
-
slight inhibition
Fe2+
-
inhibits by 44% at 10 mM
-
fluoride
-
Fe-SOD
fluoride
P80857
recombinant Fe-reconstituted SOD
formate
-
-
Guanidinium chloride
-
Mn-SOD, 70% inhibition at 1 mM
guanidinium hydrochloride
-
up to 50% inhibition
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
Fe-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
extracellular enzyme, rapidly
H2O2
-
no inhibition: Mn-SOD
H2O2
-
SOD-2 and SOD-4 inhibited, SOD-3 not
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
Q96UT6
no inhibition: Mn-SOD
H2O2
Q9Y8D9
complete inhibition; Cu,Zn-SOD
H2O2
-
Cu,Zn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Fe-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
50 mM, 100% inhibition
H2O2
-
partial sensitivity
H2O2
Radix lethospermi
-
-
H2O2
-
60% inhibition
H2O2
-
71% inhibition
H2O2
P84612
half-life of 22 min both in absence or presence of 2-mercaptoethanol
H2O2
Marinomonas sp.
-
10 mM, complete inhibition
H2O2
Q8J0N2
2.5 mM, 20% residual activity
H2O2
Q8MUI5, -
5 mM, partial inhibition
H2O2
P80857
distinguishes Fe-SOD from Mn-SOD, since it inactivates only Fe-SOD
H2O2
Rhodothermus sp.
-
inhibition at 10 mM, the Fe-SOD is less sensitive
H2O2
-
H2O2 does not show significant inhibition of the SOD activity in cell-free extracts prepared from cells grown in Mn-rich medium, but inhibits 30% of the enzyme activity in cell extracts from cells grown in Fe-rich medium
H2O2
B0L421, B2KYC6, B2KYC9, -
inactivation of FeSOD; inactivation of FeSOD; inactivation of FeSOD
H2O2
-
inactivation kinetics of rSmSOD by hydrogen peroxide, overview
Hg2+
-
inhibits by 35% at 10 mM
HgCl2
-
1 mM, inhibition of isozyme SODI
HS-
P0AGD3
substrate analogue, formation of a green complex upon binding
hydrogen peroxide
-
up to 80% inhibition
hydrogen peroxide
-
-
imidazole
Q2UZU7, -
above 1.6 mM
iodoacetamide
-
Mn-SOD
iodoacetamide
-
Cu,Zn-SOD
iodoacetic acid
-
23.5% inhibition at 1 mM
K+
-
inhibits by 14% at 10 mM
KCN
Q33DP1
3 mM, 65% loss of activity
KCN
Q8J0N2
5 mM, 40% residual activity
KCN
Q8MUI5, -
2 mM, complete inhibition
KCN
Rhodothermus sp.
-
inhibition at 10 mM, the Fe-SOD is less sensitive
KCN
-
30% inhibition at 2 mM
KCN
D0UXW7, D0UXW8
inhibits Cu,Zn-SOD
Ketoconazole
-
-
Mg2+
-
inhibits by 64% at 10 mM
Mn(Me-Phimp)2(ClO4)
-
i.e. Mn(2-(1-(2-phenyl-2-(pyridine-2-yl)hydrazono)ethyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2
-
i.e. Mn-(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)napthalen-1-ol), active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)napthalen-1-ol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(Phimp)2
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol), active as cofactor in superoxide dismutation reaction
Mn(Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
Mn2+
-
64% inhibition
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
i.e. Woodwards reagent, Kat 50 mM
N3-
-
Fe-SOD, slightly
N3-
-
no inhibition, Fe-SOD
N3-
-
extracellular enzyme
N3-
-
binds to Fe3+, but has no effect on activity
N3-
-
SOD-2 and SOD-4 inhibited, SOD-3 not inhibited
N3-
-
no inhibition: Zn,Cu-SOD
N3-
-
Fe-SOD, slightly
N3-
-
Mn-SOD is inhibited by 50%, enzyme reconstituted by Fe3+ shows increased inhibition
N3-
-
extracellular enzyme; Mn-SOD
NaCl
-
slight inhibition at 1 mM
NaN3
-
13.5 mM, inhibition
NaN3
P84612
50% inhibition at 6.9 mM in absence, at 9.0 mM in presence of 2-mercaptoethanol
NaN3
-
inhibits the enzyme mutants Y41F and H155Q, but not the wild-type enzyme
NaN3
Rhodothermus sp.
-
inhibition at 5 mM, the Fe-SOD is less sensitive
NaN3
-
inactivates 15% and 24% of the SODs present in cell extracts prepared from cells grown in the Mn- and Fe-rich media, respectively
Ni2+
-
inhibits by 57% at 10 mM
nitroprusside
-
Mn-SOD
o-phenanthroline
-
slightly
o-phenanthroline
-
depending on assay method; Fe-SOD
o-phenanthroline
-
Mn-SOD
O2
P81527
repressed expression
O2-
-
substrate inhibition for mutant C140S/Q143A
OH-
-
Cu,Zn-SOD, competitively
p-hydroxymercuribenzoate
-
completely inhibited at 1 mM; Mn-SOD
p-hydroxymercuribenzoate
-
completely inhibited at 1 mM; Mn-SOD
Penicillamine
-
copper-chelator, wild-type and mutant Cu,Zn-SOD
perchlorate
-
competitive
peroxynitrite
P84612
50% inhibition at 0.032 mM in absence, at 0.153 mM in presence of 2-mercaptoethanol
peroxynitrite
P04179
almost complete inhibition via nitration of active-site residue Y34, no significant change in conformation upon nitration. Inhibition occurs either through a steric effect of 3-nitrotyrosine 34 that impedes substrate binding or through an electrostatic effect of the nitro group
Phenyl mercuric acetate
-
Cu,Zn-SOD
Phenylglyoxal
-
25% activity remaining after 3 h for native and recombinant wild-type and recombinant mutant H30A, complete inactivation of recombinant mutant K179R after 7 min
phenylmethanesulfonyl fluoride
-
irreversible inactivation by attachment of a molecule phenylmethanesulfonyl fluoride to the active site Tyr41 reinforcing the heat stability of the enzyme, overview
PMSF
-
irreversible inhibition by binding to active site Tyr41
potassium cyanide
-
up to 90% inhibition
potassium cyanide
-
2 mM, complete inhibition
rho-diazobenzene sulfonic acid
-
-
-
SDS
-
1 mM, inhibition of isozyme SODI
SDS
-
recombinant Cp-icCuZnSOD is active and retains more than 80% activity under treatment with 1-6% SDS. It retains 70% activity after treatment with 8% SDS but activity is rapidly lowered to 52% after treatment with 10% SDS
Sodium azide
-
32% inhibition
Sodium azide
-
33% inhibition
Sodium cyanide
-
-
Sodium cyanide
-
36% inhibition
Sodium diethyldithiocarbamate
-
complete inhibition above 0.1 mM
Sodium dodecyl sulfate
-
2% w/v, Cu,Zn-SOD and EC-SOD
Sodium dodecyl sulfate
-
1%, complete inhibition
sodium dodecylsulfate
Radix lethospermi
-
2 mM, 34% inhibition
sodium dodecylsulfate
-
up to 67% inhibition
sulfate
-
-
tetrathiomolybdate
-
i.e. ATN-224, choline salt, inhibition leads to antiangiogenic and antitumour effects
-
Thiocyanate
-
-
trichloromethane-ethanol
-
-
-
Urea
-
Mn-SOD, 90% inhibition at 6 M
ZnCl2
-
slight inhibition at 1 mM
Mn2+
-
55% inhibition
additional information
-
insensitive to fluoride
-
additional information
-
no inhibition by N-ethylmaleide
-
additional information
-
no inhibition by dithiothreitol and beta-mercaptoethanol
-
additional information
-
not inhibitiory: cyanide
-
additional information
-
not inhibitory: cyanide
-
additional information
-
not inhibitory: potassium cyanide, H2O2
-
additional information
-, Q5JCT2
not inhibitory: sodium dodecylsulfate up to 2.5%
-
additional information
Q2UZU7, -
not inhibitory: sodium dodecylsulfate
-
additional information
-, Q7X4G4
not inhibitory H2O2 up to 80 mM
-
additional information
Radix lethospermi
-
not inhibitory: dithiothreitol, sodium azide, 2-mercaptoethanol
-
additional information
-
no effect: Cu2+, Ca2+
-
additional information
-
not inhibitory: sodium azide, potassium cyanide
-
additional information
-
not inhibitory: sodium dodecyl sulfate up to 4%
-
additional information
-
not inhibitory: cyanide
-
additional information
-
no effect: Cu2+, Co2+, Ca2+, sodium dodecylsulfate, 2-mercaptoethanol
-
additional information
-
not inhibitory: EDTA
-
additional information
-
not inhibitory: KCN
-
additional information
Marinomonas sp.
-
not inhibitory: cyanide
-
additional information
-
enzyme is not inhibited by H2O2 and unusually resistant to KCN; SodC is resistant to inhibition by H2O2 and is unusually resistant to KCN for a Cu,Zn-SOD
-
additional information
Q5K650, -
imidazole up to 0.8 M and sodium dodecylsulfate up to 4% are not inhibitory
-
additional information
Q9S8P4
not inhibitory: sodium dodecylsulfate
-
additional information
-, Q6TKF7
not inhibitory: NaN3
-
additional information
-
the enzyme is insensitive to cyanide inhibition
-
additional information
-
no inhibition of the purified enzyme by 6 M guanidinium chloride or by proteases trypsin and Staphylococcus aureus V8 protease
-
additional information
P80857
recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
-
additional information
-
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
isoyzme SODI is insensitive to H2O2 and KCN
-
additional information
-
no inhibition of Cu,Zn-SOD by sodium azide and O-phenanthroline
-
additional information
-, Q52JH6
tributyltin chloride does not affect enzyme expression
-
additional information
B0L421, B2KYC6, B2KYC9, -
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
-
no inhibition of Cu/ZnSOD by 10 mM H2O2, 1 mM CaCl2, and 1 mM NaN3
-
additional information
-
ligand complex synthesis, electrochemical properties, and structure determination, overview
-
additional information
A3RLW7, -
no inhibition by KCN and H2O2
-
additional information
-
no inhiibtion by CN-
-
additional information
-
no inhibition by KCN and H2O2
-
additional information
-, Q5UVY7
no inhibition by NaN3 and KCN
-
additional information
-
the native enzyme is degraded by pepsin and trypsin, while the polysialylated SOD is resistant to pepsin and trypsin
-
additional information
-, Q1HEQ0
no inhibition by NaN3
-
additional information
-
melatonin, testosterone, dihydrotestosterone, estradiol, and vitamin D induce activation of SOD1 in mitochondria. Enzyme activation is not affected by furafylline, a selective inhibitor of the P450 1A2 isoform, but is inhibited by omeprazole and ketoconazole, and by tiron, a superoxide radical specific scavenger
-
additional information
Q6B7T0, -
no inhibition by NaN3
-
additional information
D0UXW7, D0UXW8
no inhibition by KCN of MnSOD
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM
2-mercaptoethanol
Marinomonas sp.
-
slight activation
8-Hydroxyquinoline-5-sulfonate
-
Fe-SOD, slightly stimulating, depending on the assay method
corticotrophin
-
enzyme activity in the inner zone mitochondria of adrenal gland is enhaced by corticotrophin and by a low-sodium diet
-
dihydrotestosterone
-
-
dithiothreitol
Marinomonas sp.
-
slight activation
malathion
-
subchronic exposure to malathion increases the enzyme activity in liver by 11%
o-phenanthroline
-
depending on assay method; Fe-SOD, slightly stimulating
sodium dodecylsulfate
-
1 mM
sulfhydryl compounds
-
e.g. reduced glutathione, cysteine, 2-mercaptopropionylglycine activate
testosterone
-
-
Thiourea
Marinomonas sp.
-
slight activation
Urea
Marinomonas sp.
-
slight activation
additional information
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in DKO mice with combined leptin and LDL-receptor deficiency, leading to less oxLDL accumulation within atherosclerotic plaques and inhibition of plaque progression, and restores enzyme expression in THP-1 macrophages and foam cells, overview
-
additional information
-
teneurin carboxy-terminal associated peptide-1, i.e. TCAP-1, upregulates the enzyme expression, shows neuroprotective activity, and is implicated in the regulation of neuron growth and differentiation, the TCAP-teneurin system may be part of a mechanism to protect neurons during trauma, such as hypoxia and ischemia, overview
-
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
the enzyme is 5fold induced by iron starvation
-
additional information
-, Q52JH6
tributyltin chloride does not affect enzyme expression
-
additional information
-
activation of intermembrane space SOD1 upon oxidation of critical thiols. Melatonin, testosterone, dihydrotestosterone, estradiol, and vitamin D induce activation of SOD1 in mitochondria. Enzyme activation is not affected by furafylline, a selective inhibitor of the P450 1A2 isoform, but is inhibited by omeprazole and ketoconazole
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
Nitro blue tetrazolium
-
-
15
-
Nitro blue tetrazolium
-
-
0.355
-
O2-
-
-
0.0016
-
riboflavin
-
-
2.3
-
riboflavin
-
-
additional information
-
additional information
-
evaluation of catalytic rate constant as a function of ionic strength and copper and zinc content. rate constant increases with ionic strength up to 1500000000 per M and s at an ionic strength of 15 mM, and decreases thereafter
-
additional information
-
additional information
P0AGD3
pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34
-
additional information
-
additional information
-
ratio kcat/Km per microM and s: wild-type, 800, mutant C140S, 800, mutant N73S, 470, mutant Q143A, 3.1, mutant N73S/Q143A, 13, mutant N73S/C140S/Q143A, 15
-
additional information
-
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
-
additional information
-
rate constants and kinetic mechanism
-
additional information
-
additional information
-
rate constants and kinetics compared to other SODs from other species, overview
-
additional information
-
additional information
-
steady-state kinetics with artificial substrates, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1100
-
O2-
-
pH 7.5, 25C, mutant Y34F with fluorinated Tyr-residues
3300
-
O2-
-
pH 7.5, 25C, mutant Y34F
4600
-
O2-
-
pH 7.5, 25C, wild-type with fluorinated Tyr-residues
40000
-
O2-
-
pH 7.5, 25C, wild-type
100000
-
O2.-
-
-
additional information
-
additional information
-
determination of catalytic rate constant by pulse irradiation and cytochrome c assay after addition of EDTA to eliminate excess copper. kcat Value is 2820000000 per M and s at low ionic strength and 1300000000 per M and s in presence of 50 mM phosphate, pH 7.8
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
O2-
-
mutant C140S/Q143A, pH 9.0, 25C
20
-
perchlorate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00076
-
Mn(Me-Phimp)2(ClO4)
-
-
0.00112
-
Mn(N-Phimp)2(ClO4)
-
-
0.00029
-
Mn(Phimp)2
-
-
0.00039
-
Mn(Phimp)2(ClO4)
-
-
0.04
-
Sodium diethyldithiocarbamate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.2
-
P80857
reconstituted Mn-SOD
1.41
-
-
purified Cu,Zn-SOD
4.3
-
P80857
reconstituted Mn-SOD mutant Y88F
7.4
-
A6MHS2, -, Q6QHT3
-
11
-
-, Q7X4G4
pH 8.0, apoprotein
17.3
-
-
purified extracellular enzyme, pyrogallol autoxidation inhibition assay method
18.6
-
A6MHS2, -, Q6QHT3
-
20
40
-
pH 7.8
20.1
-
C7DRQ4, -
purified recombinant enzyme, in absence of Mn2+
27.5
-
Q9Y8H8
apoenzyme, pH not specified in the publication, 37C
31.24
-
-
mitochondrial Mn-SOD
39.64
-
-
cytosolic Cu/Zn-SOD
40.21
-
-
mitochondrial Cu/Zn-SOD
63
-
-, Q7X4G4
pH 8.0, apoprotein reconstitued in presence of iron
66
-
-
wild-type strain
89
-
-
purified enzyme
113.8
-
-
purified isozyme SODII
115.8
-
-
purified native enzyme
127.4
-
-, Q1HEQ0
purified recombinant enzyme, pH 6.5, 60C
150
-
Q1HDV5, -
purified native enzyme
160
-
Q9Y8H8
Fe2+-bound enzyme, pH not specified in the publication, 37C
178.7
-
C7EXL1
recombinant wild-type SOD1, pH not specified in the publication, temperature not specified in the publication
179
-
-
purified isozyme SODI
230
-
Q9Y8H8
Fe2+-bound enzyme, pH not specified in the publication, 70C
289
-
-, Q7X4G4
pH 8.0, apoprotein reconstitued in presence of manganese and iron
387
-
-
purified mutant Y41F
421
-
-, Q7X4G4
pH 8.0, recombinant enzyme
480
-
Q6QGY4
purified Mn-SOD from peroxisomal membrane
481
-
P80857
reconstituted Fe-SOD
500
-
E9RHW0
purified native enzyme, pH not specified in the publication, temperature not specified in the publication
550
-
Q9Y8H8
Mn2+-bound enzyme, pH not specified in the publication, 37C
572
-
-, Q7X4G4
pH 8.0, apoprotein reconstitued in presence of manganese
574
-
Q65Y02
-
755
-
P80857
reconstituted Fe-SOD mutant Y88F
996.2
-
-
purified native enzyme
1331
-
C7EXL1
recombinant SOD1-Lys7 chimera, pH not specified in the publication, temperature not specified in the publication
1418
-
-
purified recombinant enzyme, one unit of SOD activity is defined as the amount of enzyme required to inhibit the autooxidation of pyrogallol to 50%. pH 8.2, 37C
1853
-
C7DRQ4, -
purified recombinant enzyme, in presence of Mn2+
1890
-
-
25C, pH 8.2
2000
-
-
pH 10.2, 25C
2170
-
-, Q1HEQ0
purified recombinant enzyme, pH 6.5, 60C
2324
-
A3RLW7, -
purified recombinant enzyme
2700
-
Q9Y8H8
Mn2+-bound enzyme, pH not specified in the publication, 70C
2781
-
Q0PKG3
pH 10.5, 25C
2940
-
-
purified Cu,Zn-SOD
3000
-
-
purified enzyme
3788
-
C7EXL1
recombinant SOD1 mutant P143S/P145L, pH not specified in the publication, temperature not specified in the publication
3839
-
-
pH 7.8
3980
-
-
purified mutant H155Q
4843
-
Radix lethospermi
-
-
5672
-
Marinomonas sp.
-
pH 7.8
5780
-
A7BI63
purified recombinant enzyme
6540
-
Q71S33, -
pH 10.2, 25C
6720
-
-
purified wild-type enzyme
7381
-
-
purified SODIII
7980
-
-
purified recombinant enzyme
9446
-
-
purified SODI
9480
-
-
purified enzyme, pH 8.2, 20C
10750
-
-
purified SODIV
11960
-
Q8J0N2
-
13960
-
-
purified SODII
17060
-
Q8J0N2
pH 7.8, native protein
27270
-
Q8J0N2
pH 7.8, recombinant protein
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
overview: superoxide dismutase assays
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
modeling of kinetics
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q96UT6
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
recombinant EC-SOD
additional information
-
-
-
additional information
-
O82519
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
native and recombinant, wild-type and restored enzyme, with Fe2+ and Mn2+
additional information
-
Q71S31
dimeric form shows 65% higher activity than monomeric form
additional information
-
-
Mn-SOD, native and recombinant wild-type and mutants
additional information
-
-
-
additional information
-
-
development of a 96-well-plate mircoassay for enzyme activity
additional information
-
P84612
specific activity is 14000 U per mg protein and mol Fe, and 10000 U per mg protein and mol Fe in presence of 2-mercaptoethanol. Specific activity shows little variation between 5C and 25C
additional information
-
-
-
additional information
-
-
activities of the native metalloenzyme and isotopically enriched metalloenzyme containing two different metal isotopes, measurement of SOD inhibition of the autoxidation of pyrogallol, method development, overview
additional information
-
B0B552
Cu/Zn-SOD activity in overexpressing cells from different culture conditions, overview
additional information
-
-
SOD activity profile after intravenous administration of Cu,Zn-SOD covalently linked to lecithin, measurement of serum and urinary PC-Cu,Zn-SOD concentrations after application of exogenous recombinant human isozyme to male and female humans, overview
additional information
-
-
enzyme activity in dogs with unilateral testicular tumor or unilateral cryptorchid testis, and with or without Sertoli cell tumor, seminoma and/or Leydig cell tumor, overview
additional information
-
-
purified native enzyme
additional information
-
-
activity of native enzyme and modified, fatty acid-conjugated enzyme, overview, coupled assay method using inhibition of the autooxidation of pyrogallol
additional information
-
-
activity in egg white and yolk during storage, overveiw
additional information
-
-
yeast Mn-SOD shows high activity compared to other species' enzymes
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
6.5
Q0PKG3
100% activity within this range
5
-
Rhodothermus sp.
-
recombinant enzyme
5.5
7.4
-
assay at
6.5
-
-, Q1HEQ0
recombinant enzyme
6.5
-
-, Q1HEQ0
recombinant enzyme
7
11
Q9Y8D9
native and recombinant Cu,Zn-SOD, activity is pH-independent
7
8
-
assay at
7
-
-
isoenzyme I
7
-
-
assay at
7.4
-
P81527
assay at
7.4
-
-
assay at
7.5
-
Q0PKG3
20% residual activity
7.5
-
A3RLW7, -
recombinant enzyme
7.8
-
-
assay at
7.8
-
-
Mn-SOD
7.8
-
-
assay at
7.8
-
-
Fe-SOD
7.8
-
-
assay at
7.8
-
P80857
assay at
7.8
-
B0B552
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
8
-
-
isozyme SODI
8
-
Q6B7T0, -
broad pH optimum
8.2
8.8
Q8J0N2
-
8.2
-
-
assay at
8.2
-
-
assay at
8.2
-
-
assay at
8.5
-
-
Mn-SOD
8.5
-
-
assay at
8.6
-
-
Mn-SOD
8.9
-
-
Cu,Zn-SOD
9
-
C7DRQ4, -
-
9.5
-
-
Mn-SOD
10.1
-
-
Mn-SOD
10.2
-
-
Cu,Zn-SOD I and II
10.2
-
-
assay at
additional information
-
-
pH-dependence, overview
additional information
-
-
the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
9
-
activity range, the enzyme shows 30% of maximal activity at pH 10.0 and is inactive at pH 11.0
2.2
11.2
Q2TV65
high enzyme activity
3
11
-
pH-profile, overview. Outside the range of 5.0-7.0, activity is rapidly lost
4
12
Rhodothermus sp.
-
inactivation at pH 2.0, shrap drop of activity below pH 4.0, high activity at pH 4.0-pH 5.0, about 70% of maximal activity at pH 6.0-12.0
4
12
-
90% of maximal activity at pH 5.6-pH 7.5, 15% at pH 4.0, 60% at pH 12.0, 25C, pH profile, overview
5
10
-, Q1HEQ0
activity profile, overview
6
10.6
-
Mn-SOD
6
10.6
-
Mn-SOD
6.4
10.9
-
-
6.5
10.2
-
activity decreases as pH increases
6.5
9
A3RLW7, -
activity range
7
11
Q9Y8D9
native and recombinant Cu,Zn-SOD, activity is pH-independent
7
9.5
-, Q5UVY7
optimum pH-range
7.6
10.5
-
-
8
10
Marinomonas sp.
-
-
8
10.5
C7DRQ4, -
50% of maximal activity at pH 8.0 and pH 10.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
Marinomonas sp.
-
about 35% of maximum activity
5
25
P84612
no data available above or below
20
-
-
assay at
22
-
-
assay at room temperature
24
-
-
assay at
25
30
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
P81527
assay at
25
-
P80857
assay at
25
-
B0B552
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
37
-
Q9Y8D9
native and recombinant Cu,Zn-SOD
37
-
Q0PKG3
-
37
-
-
assay at
40
-
Marinomonas sp.
-
-
50
70
Rhodothermus sp.
-
recombinant enzyme
55
-
A3RLW7, -
recombinant enzyme
60
-
-, Q1HEQ0
recombinant enzyme
60
-
-, Q1HEQ0
recombinant enzyme
70
-
Q0PKG3
about 50% residual activity
70
-
Q9Y8H8
-
95
-
-
stable, the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
additional information
-
-
the enzyme is cold-active
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
80
-
temprature profile, overview
25
85
-
at pH 7.8, temperature profile, overview
50
90
A3RLW7, -
-
60
115
-
activity range, profile, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.6
-
-
isoelectric focusing, isozyme SODII
3.8
-
-
isoelectric focusing
3.8
-
-
SODIV, isoelectric focussing
4
-
-
isozyme SODI, isoelectric focusing
4.4
-
-
isoelectric focusing
4.55
-
-
isoform with molecular weight of 130 kDa, CuZn-type, induction by exposure of mussels to copper
4.6
-
-
isoform with molecular weight of 155 kDa, CuZn-type
4.7
-
-
isoform with molecular weight of 205 kDa, CuZn-type
5.14
-
-
calculated
5.2
-
-
SODIII, isoelectric focussing
5.31
-
Q9M7R2
calculated
5.31
-
B0L421, B2KYC6, B2KYC9, -
SOD1, sequence calculation; SOD1, sequence calculation; SOD1, sequence calculation
5.54
-
Rhodothermus sp.
-
sequence calcualtion
5.6
-
-
Fe-SOD, i.e. SodB, isoelectric focusing
5.65
-
A7BI63
sequence calculation
5.66
-
Q6QGY4
mitochondrial Mn-SOD, isoelectric focusing
5.75
-
Q6QGY4
peroxisomal Mn-SOD, isoelectric focusing
5.78
-
-
sequence calculation
5.9
-
-
isoelectric focusing, recombinant enzyme
5.9
-
-
Mn-SOD, i.e. SodA, isoelectric focusing
6
-
-
isoelectric focusing
6.15
-
-
sequence calculation
6.2
-
-
recombinant enzyme, isoelectric focusing
6.3
-
-, Q52JH6
cytoplasmic CuZn-SOD, sequence calculation
6.39
-
B0B552
Cu/Zn-SOD sequence calculation
6.5
-
Q0PKG3
calculated
6.71
-
-
calculated from sequence
6.75
-
C7DRQ4, -
sequence calculation
6.8
-
-
isoelectric focusing, isozyme SODI
6.8
-
-
SODII, isoelectric focussing
6.86
-
Q2KN28, Q2KN29, Q2KN30, Q381J5
calculated
6.9
-
-
SODI, isoelectric focussing
7
-
Q8J0N2
isoelectric focusing
8.29
-
Q2TV65
sequence calculation, MnSOD
8.4
-
-
isoelectric focusing
8.65
-
Q2KN28, Q2KN29, Q2KN30, Q381J5
calculated
9.2
-
Q65Y02
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
an ovarian carcinoma cell line
Manually annotated by BRENDA team
-
enzyme mRNA is only found in the inner zones of adrenal cortex, not the glomerulosa. Enzyme activity in the inner zone mitochondria is enhaced by corticotrophin and by a low-sodium diet, but suppressed by betamethasone
Manually annotated by BRENDA team
-
internal mammary arteries
Manually annotated by BRENDA team
-
developmental stage of organism
Manually annotated by BRENDA team
-
harbors MnSOD with the ala16val polymorphism
Manually annotated by BRENDA team
-
isozyme profile, 4 constitutive isozymes, 3 cold-inducible isozymes, overview. The enzyme activity declines in the beginning of storage, that with cold treatment at 4C rapidly increases. After 7 days, two Fe-Sod isozymes are still active, while the Mn-SOD are inactivated
Manually annotated by BRENDA team
-
the organism has a very high enzyme content
Manually annotated by BRENDA team
Penicillium marneffei
B6QEB3
propagation of the fungus in the Mus musculus macrophage cell line derived from a reticulum sarcoma, J774.1, ATCC TIB-67, the enzyme expression is upregulated during macrophage infection
Manually annotated by BRENDA team
Marchantia paleacea CuZn-SOD
-
-
-
Manually annotated by BRENDA team
Penicillium marneffei
B6QEB3
accumulation of sodA mRNA in conidia, semi-quantitative expression analysis
Manually annotated by BRENDA team