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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Deinococcus radiodurans and UniProt Accession Q9RUV2

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EC Tree
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:
Deinococcus radiodurans
UNIPROT: Q9RUV2
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Word Map
The taxonomic range for the selected organisms is: Deinococcus radiodurans
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-containing superoxide dismutase
-
-
Mn-SOD
-
-
-
-
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
O2.- + H+
O2 + H2O2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Manganese
-
when the Deinococcus radiodurans Mn2+SOD reacts with a substoichiometric amount of superoxide, Deinococcus radiodurans Mn3+SOD is produced
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
rate constants and kinetic mechanism
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
x * 22000, recombinant Mn-SOD, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 22000, recombinant Mn-SOD, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
two different monoclinic crystal forms, both with space group P21. Form 1 contains a homodimer in the asymetric unit, form II contains two homodimers per asymmetric unit. Comparison with isostructural MnSOD of Escherichia coli
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y34F
-
the mutant shows metalcofactor kinetics similar to the human not the Deinococcus radiodurans Mn-SOD, formation of human-like Mn3+SOD and human-like Mn3+SOD-O2 - adduct, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Mn-SOD from Escherichia coli strain QC774 by anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from genomic DNA, expression in Escherichia coli strain QC774
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dennis, R.J.; Micossi, E.; McCarthy, J.; Moe, E.; Gordon, E.J.; Kozielski-Stuhrmann, S.; Leonard, G.A.; McSweeney, S.
Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms
Acta Crystallogr. Sect. F
62
325-329
2006
Deinococcus radiodurans (Q9RUV2), Deinococcus radiodurans
Manually annotated by BRENDA team
Abreu, I.A.; Hearn, A.; An, H.; Nick, H.S.; Silverman, D.N.; Cabelli, D.E.
The kinetic mechanism of manganese-containing superoxide dismutase from Deinococcus radiodurans: a specialized enzyme for the elimination of high superoxide concentrations
Biochemistry
47
2350-2356
2008
Deinococcus radiodurans
Manually annotated by BRENDA team