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1.15.1.1: superoxide dismutase

This is an abbreviated version!
For detailed information about superoxide dismutase, go to the full flat file.

Word Map on EC 1.15.1.1

Reaction

2 superoxide + 2 H+ =

O2
+
H2O2

Synonyms

AhSOD, alr2938, AmSOD, APE0743, ApMn-SOD1, ApMn-SOD2, ASAC_0498, Ca-Cu,Zn SOD, cambialistic superoxide dismutase, Cg-EcSOD, chloroplastic Fe-SOD, Cj-Cu, Zn SOD, cMn-SOD, cMnSOD, cold-active superoxide dismutase, copper, zinc superoxide dismutase, copper-zinc superoxide dismutase, copper/zinc superoxide dismutase, copper/zinc-superoxide dismutase, CpSOD, CSD1, CSD2, CtSOD, Cu, Zn SOD, Cu, Zn superoxide dismutase, Cu, Zn-superoxide dismutase, Cu, ZnSOD, Cu,Zn superoxide dismutase, Cu,Zn-SOD, Cu,Zn-superoxide dismutase, Cu,ZnSOD, Cu-Zn SOD, Cu-Zn superoxide dismutase, Cu-Zn-SOD, Cu/Zn SOD, Cu/Zn superoxide dismutase, Cu/Zn superoxide dismutase 1, Cu/Zn-SOD, Cu/Zn-SODI, Cu/Zn-SODII, Cu/Zn-superoxide dismutase, Cu/ZnSOD, cuprein, CuZn superoxide dismutase, CuZn superoxide dismutase 1, CuZn-SOD, CuZn-superoxide dismutase, CuZnSOD, cytMnSOD, cytocuprein, cytoplasmic manganese SOD, cytosolic Cu/Zn superoxide dismutase, cytosolic Cu/Zn-SOD, cytosolic manganese superoxide dismutase, DaSOD, dhsod-1, dismutase, superoxide, EC-SOD, ecCuZnSOD, ECSOD, ElFe-SOD, ElSOD, erythrocuprein, erythrocyte superoxide dismutase, eSOD, extracellular copper-zinc superoxide dismutase, extracellular CuZnSOD, extracellular SOD, extracellular superoxide dismutase, Fe-SOD, Fe-SODe, Fe-SOD_ASAC, Fe-superoxide dismutase, Fe-type SOD, Fe/Mn-SOD, Fe/Mn-type SOD, Fe/MnSOD, ferrisuperoxide dismutase, FeSOD, GTNG_2884, hEC-SOD, hemocuprein, hepatocuprein, high isoelectric point superoxide dismutase, intracellular Cu-Zn superoxide dismutase, iron SOD, iron SOD type, iron superoxide dismutase, iron-containing superoxide dismutase, iron-dependent superoxide dismutase, iron-superoxide dismutase, KmSod1p, LSOD, manganese superoxide dismutase, manganese-containing SOD, manganese-containing superoxide dismutase, MgMnSOD1, MgMnSOD2, mitMn-SOD, mitochondrial manganese superoxide dismutase, mMnSOD, Mn-containing superoxide dismutase, Mn-SOD, Mn-type SOD, Mn/Fe superoxide dismutase, MnSOD, MnSOD-2, MnSOD-3, MnSOD1, MnSOD47, More, mtMnSOD, mtSOD, nectarin I, neelaredoxin, Nlr, Of-cCu/ZnSOD, PASOD, perMn-SOD, pfSOD, PschSOD, PsSOD, PthipI-SODC, PthipI-SODC1, PthipI-SODC2, RmFeSOD, RsrSOD, SaCSD1, SaFe-SOD, sdB, SOD, SOD 1, SOD I, SOD-1, SOD-2, SOD-3, SOD-4, SOD1, SOD2, SOD3, SODA, SodB, SODB1, SODB2, SodC, SODF, SODI, SODII, SODIII, SODIV, SODS, SSO0316, superoxide dismutase, superoxide dismutase 1, superoxide dismutase I, superoxide dismutase II, superoxide dismutase [Cu-Zn]

ECTree

     1 Oxidoreductases
         1.15 Acting on superoxide as acceptor
             1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)
                1.15.1.1 superoxide dismutase

Renatured

Renatured on EC 1.15.1.1 - superoxide dismutase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
activity cannot be restored by Fe2+, Cu2+, Zn2+, and Cu2+/Zn2+, but by Mn2+
-
after reconstitution with Fe3+ instead of Mn2+, the enzyme shows properties similar to Fe-SODs
-
apoprotein expressed in insect cells can be restored by addition of Cu2+, fully active
-
enzyme folding and unfolding kinetic mechanism of wild-type and mutant enzymes at pH 7.8 and 25°C, role of metal ions, overview
-
incubation of purified apoprotein with metal salts at ambient temperatures, no restauration of activity. Reactivation by heating apoprotein with manganese salts at elevated temperatures, both manganese and iron bind to protein, but only manganese restores activity. Mechanism of metallation
-
recombinant EC-SOD refolds from inclusion bodies in E. coli after denaturing
-
reconstitution of active enzyme after withdrawal of metal by either Mn or Fe yielding an active enzyme irrespective of the metal ion initially present
reconstitution of active enzyme after withdrawal of metal either with the native metal or with cadmium, chromium or iron
-
reconstitution of active enzyme after withdrawal of Mn2+ by addition of Mn2+ to apoprotein in 8 M urea at acid pH
-
reconstitution of active protein after withdrawal of metal, higher activity with Mn2+, lower activity with Fe3+
reconstitution of enzyme demetalled with EDTA by addition of zinc and copper
-
reconstitution of Fe-SOD from purified recombinant apo-enzyme, apo-enzyme preparation: purified recombinant enzyme is denatured in buffer containing 50 mM acetate buffer, pH 3.8, 6 M guanidine hydrochloride, and 10 mM EDTA for 16 h at 50°C, followed by dialysis against the same buffer containing MnSO4 instead of EDTA, and removal of guanidine hydrochloride in a second dialysis step, followed by gel filtration, overview
reconstructed Fe-/Mn-SOD is almost equal to native Fe-SOD
Zn2+ inhibits reconstitution with Mn2+ or Fe3+
-