We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
The taxonomic range for the selected organisms is: Escherichia coli 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
copper-zinc superoxide dismutase
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
dismutase, superoxide
-
-
-
-
ferrisuperoxide dismutase
-
-
-
-
manganese superoxide dismutase
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 superoxide + 2 H+ = O2 + H2O2
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
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
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
a liganding water molecule is evident
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Iron
-
-
Iron
-
each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzymes active site
Mn2+
-
-
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
overview: metal content
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
HS-
substrate analogue, formation of a green complex upon binding
perchlorate
-
competitive
H2O2
-
no inhibition: Mn-SOD
N3-
-
-
N3-
-
binds to Fe3+, but has no effect on activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
additional information
additional information
pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34
-
additional information
additional information
-
pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34
-
additional information
additional information
-
thermodynamics, dissociation constants, and kinetics of RNA binding by enzyme MnSOD at pH 6.0-7.5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
pH-dependence, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
manganese superoxide dismutase
Uniprot
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
additional information
-
the bacterial manganese superoxide dismutase (MnSOD) localizes to the chromosomal portion of the cell
-
brenda
-
-
-
brenda
-
Cu,Zn-SOD in mammalian extracellular fluids
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
21000
-
2 * 21000, Fe-SOD
22900
-
2 * 22900, Mn-SOD
40000
-
Fe-SOD
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
-
dimer
-
2 * 22900, Mn-SOD
dimer
-
2 * 21000, Fe-SOD
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glycoprotein
-
Cu,Zn-SOD in mammalian extracellular fluids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
additional information
-
naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
-
brenda
Munkres, K.D.
Purification of exocellular superoxide dismutases
Methods Enzymol.
186
249-260
1990
Bacillus subtilis, Bos taurus, Escherichia coli, Saccharomyces cerevisiae, Triticum aestivum
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda