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S5639

Sigma-Aldrich

Superoxide Dismutase from Escherichia coli

lyophilized powder, ≥1,000 units/mg protein

Synonym(s):

SOD, Superoxide: superoxide oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥1,000 units/mg protein

mol wt

39.5 kDa

composition

Protein, ≥70% biuret

storage temp.

−20°C

Gene Information

Escherichia coli CFT073 ... sodA(1040208) , sodB(1036179) , sodC(1036143)

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General description

Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide. The direct electron transfer of superoxide dismutases can be efficiently promoted by a self-assembled monolayer of 3-mercaptopropionic acid confined on a gold electrode.

Application

Superoxide dismutase from Escherichia coli has been used in a study to determine that anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34. Superoxide dismutase from Escherichia coli has also been used in a study to demonstrate that molecular dynamics simulation and limited proteolysis are complementary and specific tools to identify flexible sites in proteins.

Biochem/physiol Actions

Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.

Other Notes

Manganese-containing enzyme

Unit Definition

One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 mL reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.

Physical form

Contains Tris buffer salts

Analysis Note

For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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U Wendling et al.
Journal of immunology (Baltimore, Md. : 1950), 164(5), 2711-2717 (2000-02-29)
Immunization with Mycobacterium tuberculosis heat shock protein (hsp) 60 has been shown to protect rats from experimental arthritis. Previously, the protection-inducing capacity was shown to reside in the evolutionary conserved parts of the molecule. Now we have studied the nature
M Falconi et al.
Proteins, 47(4), 513-520 (2002-05-10)
Limited proteolysis by trypsin of monomeric Cu,Zn superoxide dismutase from Escherichia coli induces a specific cleavage of the polypeptide chain at the level of Lys60 located in the S-S subloop of loop 6,5 where, when compared to the eukaryotic enzyme
Yoshikazu Kawai et al.
Nature communications, 14(1), 4123-4123 (2023-07-12)
Inhibition of bacterial cell wall synthesis by antibiotics such as β-lactams is thought to cause explosive lysis through loss of cell wall integrity. However, recent studies on a wide range of bacteria have suggested that these antibiotics also perturb central
Anne-Frances Miller et al.
Biochemistry, 44(16), 5969-5981 (2005-04-20)
We report the first spectroscopic observation of substrate analogue binding to the reduced state of iron superoxide dismutase from Escherichia coli (Fe(2+)SOD) and demonstrate that the pH dependence reflects inhibition of anion binding by ionized Tyr34, not loss of a
Yang Tian et al.
Analytical chemistry, 76(14), 4162-4168 (2004-07-16)
In this article, the electrochemical properties and electrocatalytic activity of three kinds of superoxide dismutases (SODs), that is, bovine erythrocyte copper-zinc superoxide dismutase (Cu/Zn-SOD), iron superoxide dismutase from Escherichia coli (Fe-SOD), and manganese superoxide dismutase from E. coli (Mn-SOD), in

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