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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Caenorhabditis elegans

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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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This record set is specific for:
Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
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
copper-zinc superoxide dismutase
-
-
-
-
Cu,Zn-SOD
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
cuprein
-
-
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
-
-
-
-
erythrocuprein
-
-
-
-
Fe-SOD
-
-
-
-
ferrisuperoxide dismutase
-
-
-
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
manganese superoxide dismutase
-
-
Mn-SOD
-
-
-
-
SOD
-
-
-
-
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
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-
-
-
superoxide dismutase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
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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
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
MnSOD-2 and MnSOD-3
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SODC_CAEEL
180
0
18700
Swiss-Prot
other Location (Reliability: 4)
SODE_CAEEL
221
0
23326
Swiss-Prot
Secretory Pathway (Reliability: 1)
SODM1_CAEEL
221
0
24537
Swiss-Prot
Mitochondrion (Reliability: 4)
SODM2_CAEEL
218
0
24661
Swiss-Prot
Mitochondrion (Reliability: 3)
G5ECR5_CAEEL
221
0
23338
TrEMBL
Secretory Pathway (Reliability: 1)
Q27538_CAEEL
178
0
18507
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MnSOD-2 and MnSOD-3, at 3 and 8 mg/ml respectively, in 10 mM Tris-HCl, pH 7.8, mixing of 0.001 ml protein and reservoir solution, the latter containing 0.1 M bicine pH 9.2 and 3.0 M ammonium sulfate for MnSOD-2, and 0.1 M bicine, pH 9.2, and 2.7 M ammonium sulfate for MnSOD-3, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged MnSOD-2 and MnSOD-3 by nickel affinity and anion exchange chromatography, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged MnSOD-2 and MnSOD-3
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Trinh, C.H.; Hunter, T.; Stewart, E.E.; Phillips, S.E.; Hunter, G.J.
Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans
Acta Crystallogr. Sect. F
64
1110-1114
2008
Caenorhabditis elegans
Manually annotated by BRENDA team