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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Escherichia coli and UniProt Accession P00448

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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:
Escherichia coli
UNIPROT: P00448
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
-
-
-
-
superoxide dismutase II
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 superoxide + 2 H+ = O2 + H2O2
show the reaction diagram
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 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
additional information
?
-
-
equilibrium binding of Escherichia coli MnSOD to poly(U), poly(A), poly(C), poly(dU) and double-stranded (ds) DNA, overview. The polynucleotides bind to MnSOD in the following affinity hierarchy, poly(dU) N poly(U) N dsDNA N poly(A) N poly(C). The differences in the hierarchy are not large in magnitude as the poly(dU) bound with less than a 100fold higher affinity than poly(C). For each polynucleotide, Kobs decreases only slightly with increasing [K+], surprising for a relatively non-specific nucleic acid protein. There is either only one binding site shared by these polynucleotides or the larger site size occluded by poly(C) overlaps that of poly(U) and poly(A), but extends further on the protein
-
-
?
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
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
?
O2- + H+
O2 + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
a liganding water molecule is evident
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Manganese
analysis of manganese(II) high-field electron paramagnetic resonance spectrum. In the -248°C to -73°C range, the zero-field interaction steadily decreases with increasing temperature. Above -33°C, 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
-
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
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fluoride
-
Fe-SOD
HS-
substrate analogue, formation of a green complex upon binding
perchlorate
-
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
perchlorate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
assay at
additional information
-
pH-dependence, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
manganese superoxide dismutase
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the bacterial manganese superoxide dismutase (MnSOD) localizes to the chromosomal portion of the cell
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the bacterial manganese superoxide dismutase (MnSOD) localizes to the chromosomal portion of the cell and impart protection from ionizing radiation to DNA. MnSOD can bind to RNA leads to the possibility that MnSOD may confer protection to RNA, as well
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
2 * 21000, Fe-SOD
22900
-
2 * 22900, Mn-SOD
40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
Cu,Zn-SOD in mammalian extracellular fluids
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y34F
unlike wild-type, F- binding is retained at high pH-values. N3- inhibitis Y34F with a 20fold lower KI-value than for wild-type
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
extracellular enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beyer, W.; Imlay, J.; Fridovich, I.
SODs: varieties and distributions. X-ray crystallography of Mn-SODs and Fe-SODs
Prog. Nucleic Acid Res. Mol. Biol.
40
221-253
1991
Synechococcus elongatus PCC 7942 = FACHB-805, Geobacillus stearothermophilus, Bacteroides thetaiotaomicron, Bacteroides fragilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Thermus thermophilus, Ginkgo biloba, Halobacterium salinarum, Homo sapiens, Methanobacterium bryantii, Paracoccus denitrificans, Mus musculus, Mycolicibacterium phlei, Nocardia asteroides, Photobacterium leiognathi, Leptolyngbya boryana, Propionibacterium freudenreichii subsp. shermanii, Pseudomonas putida, Rattus norvegicus, Gordonia bronchialis, Streptococcus mutans, Thermoplasma acidophilum, Zea mays, Thermus thermophilus Mn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Pseudomonas putida Fe-SOD, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Paracoccus denitrificans CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Thermoplasma acidophilum Fe-SOD
Manually annotated by BRENDA team
Cass, A.E.G.
Superoxide dismutases
Top. Mol. Struct. Biol.
6
121-156
1985
Geobacillus stearothermophilus, Bos taurus, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Photobacterium leiognathi, Propionibacterium freudenreichii subsp. shermanii, Bos taurus CuZn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Caulobacter vibrioides CB15, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Saccharomyces cerevisiae CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Saccharomyces cerevisiae Mn-SOD
-
Manually annotated by BRENDA team
Munkres, K.D.
Purification of exocellular superoxide dismutases
Methods Enzymol.
186
249-260
1990
Bacillus subtilis, Bos taurus, Escherichia coli, Saccharomyces cerevisiae, Triticum aestivum
Manually annotated by BRENDA team
Slykhouse, T.O.; Fee, J.A.
Physical and chemical studies on bacterial superoxide dismutases. Purification and some anion binding properties of the iron-containing protein of Escherichia coli B
J. Biol. Chem.
251
5472-5477
1976
Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli Fe-SOD
Manually annotated by BRENDA team
Miller, A.F.; Sorkin, D.L.; Padmakumar, K.
Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34
Biochemistry
44
5969-5981
2005
Escherichia coli (P0AGD3), Escherichia coli
Manually annotated by BRENDA team
Whittaker, M.M.; Mizuno, K.; Baechinger, H.P.; Whittaker, J.W.
Kinetic analysis of the metal binding mechanism of Escherichia coli manganese superoxide dismutase
Biophys. J.
90
598-607
2006
Escherichia coli
Manually annotated by BRENDA team
Tabares, L.C.; Cortez, N.; Agalidis, I.; Un, S.
Temperature-dependent coordination in E. coli manganese superoxide dismutase
J. Am. Chem. Soc.
127
6039-6047
2005
Escherichia coli (P00448), Escherichia coli
Manually annotated by BRENDA team
Smolik, A.C.; Bengez-Pudja, L.; Cheng, I.; Mascotti, D.P.
Characterization of E. coli manganese superoxide dismutase binding to RNA and DNA
Biochim. Biophys. Acta
1844
2251-2256
2014
Escherichia coli
Manually annotated by BRENDA team