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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession Q08713

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IUBMB 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.
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Sulfolobus acidocaldarius
UNIPROT: Q08713
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
2
+
2
=
+
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe-superoxide dismutase
-
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-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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 hide
9054-89-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
Fe/Mn-type SOD, the Fe-type enzyme contains Gln85
Iron
contains one iron atom per dimer, the protein contains a mononuclear iron center
Mn2+
Fe/Mn-type SOD, the Mn-type enzyme contains Gly85
Fe2+
-
bound by His33, His84, His174, and Asp170, coordination in the active site, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3000
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
stable, the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the organism has a very high enzyme content
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22400
24270
2 * 24270, calculated from sequence
45000
dimeric form, gel filtration
87000
tetrameric form, gel filtration
24270
2 * 24270, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
tetramer
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
dimer
2 * 24270, sequence calculation
additional information
-
secondary, quarternary and three-dimensional structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, hanging drop vapor diffusion method, 20°C, mixing of 0.003 ml of the concentrated protein solution with 0.003 ml of the reservoir solution containing 16.25% PEG 4000, 0.2 M ammonium sulfate, 5% w/v 2-propanole, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
purified enzyme, half-life is 48 h or above
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
incubation with proteases (e.g. trypsin, V8 Staphylococcus aureus protease) has no effect on this enzyme
treatment with the proteases V8 shows no effect on the enzyme
treatment with trypsin shows little effect on the enzyme
the purified enzyme is stable in 6 M guanidinium chloride for 72 h loosing only 33% activity
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
SDS
incubation with 0.1% SDS shows no effect on the enzyme. Simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a second form of the enzyme with a molecular mass of 87000 Da. It is most likely a tetramer. The specific activity of the tetrameric form is about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sod, DNA and amino acid sequence determination and analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klenk, H.P.; Schleper, C.; Schwass, V.; Brudler, R.
Nucleotide sequence, transcription and phylogeny of the gene encoding the superoxide dismutase of Sulfolobus acidocaldarius
Biochim. Biophys. Acta
1174
95-98
1993
Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q08713)
Manually annotated by BRENDA team
Schaefer, T.; Boenisch, H.; Kardinahl, S.; Schmidt, C.; Schaefer, G.
Three extremely thermostable proteins from Sulfolobuc and a reappraisal of the 'traffic rules'
Biol. Chem.
377
505-512
1996
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius DSM 639 (Q08713)
Manually annotated by BRENDA team
Knapp, S.; Kardinahl, S.; Hellgren, N.; Tibbelin, G.; Schfer, G.; Ladenstein, R.
Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution.
J. Mol. Biol.
285
689-702
1999
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
Manually annotated by BRENDA team
Kardinahl, S.; Schmidt, C.L.; Petersen, A.; Schaefer, G.
Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius
FEMS Microbiol. Lett.
138
65-70
1996
Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q08713)
Manually annotated by BRENDA team