Any feedback?
Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Aeropyrum pernix and UniProt Accession Q9Y8H8
for references in articles please use BRENDA:EC1.15.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.15.1.1 superoxide dismutaseIUBMB Comments
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.
Specify your search results
Word Map
- 1.15.1.1
- catalase
- malondialdehyde
- gsh
- necrosis
- endothelial
- tnf
- wistar
- artery
- ascorbate
- gsh-px
- caspase-3
- cholesterol
- cardiac
-
reperfusion
-
neuroprotective
- sclerosis
-
tbars
-
anti-oxidant
- ischemia
-
thiobarbituric
- myocardial
- triglyceride
-
alt
-
amyotrophic
-
mime
-
sacrificed
- chlorophyll
-
neurotoxicity
- hippocampus
- myeloperoxidase
- infarct
- cerebral
- xanthine
-
hepatotoxicity
- streptozotocin
-
albino
-
sham
- creatinine
-
ischemia-reperfusion
- bcl-2
- s-transferase
- glutathione-s-transferase
-
hepatoprotective
- diagnostics
-
chemiluminescence
- synthesis
-
gavage
-
cardioprotective
- ceruloplasmin
- drug development
- oxygenase-1
-
endothelium-dependent
- peroxynitrite
- environmental protection
- analysis
- biotechnology
- medicine
- agriculture
The taxonomic range for the selected organisms is: Aeropyrum pernix
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
copper-zinc superoxide dismutase
-
-
-
-
Cu,Zn-SOD
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
cuprein
-
-
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
-
-
-
-
erythrocuprein
-
-
-
-
Fe-SOD
-
-
-
-
ferrisuperoxide dismutase
-
-
-
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
Mn-SOD
-
-
-
-
SOD
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
SOD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9054-89-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
SOD enzyme activity is determined by measuring enzyme ability to inhibit the photochemical reduction of nitrobluetetrazolium
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+ +
O2 + H2O2
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mn2+
Fe2+
Mn2+
additional information
-
the native forms of SODAp and NTD-fused N-terminal domain ntdSODAp prefer binding Fe2+ over Mn2+ (about 10fold) but contain low ion amounts in each monomer, respectively
Fe2+
the SOD is active with Fe2+ and Mn2+, Fe2+ activates 6fold, binding structure, overview
Fe2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Mn2+
the SOD is active with Fe2+ and Mn2+, Mn2+ activates 20fold, binding structure, overview
Mn2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Fe2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Fe-reconstituted enzyme contains 0.79 atom of iron per subunit
Mn2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Mn-reconstituted enzyme contains 0.82 atom of manganese per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
inactivates the Fe-reconstituted SOD in a time-dependent manner, but not the Mn-reconstituted enzyme. The incubation time for 50% inactivation of the Fe-reconstituted enzyme in the presence of 0.24 mM H2O2 is 50 min
Sodium azide
50% inhibition of the Fe-reconstituted enzyme at 41 mM. Sodium azide does not inhibit the Mn-reconstituted superoxide dismutase even at concentrations up to 400 mM
Sodium fluoride
inhibits both the Mn- and Fe-reconstituted enzyme. The concentrations of sodium fluoride causing 50% inhibition of the Mn- and Fe reconstituted enzymes are 89 and 13 mM, respectively
2-mercaptoethanol
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM
EDTA
-
60% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, 20% at 1 mM
guanidinium hydrochloride
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM
SDS
-
60% inhibition of Mn-reconstituted wild-type enzyme at 1%, and 40% inhibition of the Mn-reconstituted N-terminal domain
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.155
-
purified recombinant Mn-reconstituted N-terminal domain mutant SOD, pH 7.8, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
recombinant fusion enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
superoxide dismutases play a protective role against oxidative stress by catalyzing disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen
physiological function
-
superoxide dismutases protect against oxidative stress by disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen through a redox cycle of metal ions
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24577
24577
in crystals, 4 * 24577, sequence calculation and gel filtration
24577
in solution, 2 * 24577, sequence calculation and gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
in crystals, 4 * 24577, sequence calculation and gel filtration
homodimer
in solution, 2 * 24577, sequence calculation and gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo, Mn-bound and Fe-bound enzyme, in presence of PEG, 2-3 days, X-ray diffraction structure determination and analysis at 1.56 A, 1.35 A, and 1.48 A, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
generation of a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation engineering. Recombinant wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp are incorporated with metal cofactors by two ways: the Fe2+- and Mn2+-contained SODs are obtained by in vivo modification (Mn-med SODAp and ntdSODAp) and in vitro reconstitution (Mn-rec SODAp and ntdSODAp), respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10
744564
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
the enzyme is stable in aqueous solution at temperatures up to 85°C
100
-
recombinant wild-type enzyme SODAp retains 44&% of maximal activity, while recombinant Mn-rec ntdSODAp N-termina domain retains 58% activity
70 - 110
-
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits higher tolerance for denaturants and organic media than recombinant wild-type Mn-rec SODAp
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpressed as a GST fusion protein at a high level in Escherichia coli
recombinant expression of His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamura, T.; Torikai, K.; Uegaki, K.; Morita, J.; Machida, K.; Suzuki, A.; Kawata, Y.
Crystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1 - insights into the enzyme mechanism and stability
FEBS J.
278
598-609
2011
Aeropyrum pernix (Q9Y8H8), Aeropyrum pernix
Yamano, S.; Sako, Y.; Nomura, N.; Maruyama, T.
A cambialistic SOD in a strictly aerobic hyperthermophilic archaeon, Aeropyrum pernix
J. Biochem.
126
218-225
1999
Aeropyrum pernix (Q9Y8H8), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9Y8H8)
Lee, H.J.; Kwon, H.W.; Koh, J.U.; Lee, D.K.; Moon, J.Y.; Kong, K.H.
An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1
J. Microbiol. Biotechnol.
20
727-731
2011
Aeropyrum pernix (Q9YE27), Aeropyrum pernix DSM 11879 (Q9YE27)
Li, M.; Guo, S.; Li, X.; Wang, Q.; Zhu, L.; Yin, C.; Wang, W.
Engineering a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation
Biotechnol. Bioprocess Eng.
22
725-733
2017
Aeropyrum pernix
-
EXTERNAL LINKS (specific for EC-Number 1.15.1.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
