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Literature summary for 1.15.1.1 extracted from

  • Kumar, A.; Sharma, M.; Bhardwaj, P.; Vats, S.; Singh, D.; Kumar, S.
    Copper, zinc superoxide dismutase from Caragana jubata a thermostable enzyme that functions under a broad pH and temperature window (2016), Process Biochem., 51, 1434-1444 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain M15 Caragana jubata

Inhibitors

Inhibitors Comment Organism Structure
H2O2
-
Caragana jubata
KCN
-
Caragana jubata
additional information the enzyme is resistant to denaturation by sodium dodecyl sulfate (SDS) and urea Caragana jubata

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble Cj-Cu,Zn SOD is a hydrophilic protein with no transmembrane domains Caragana jubata
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a Cu,Zn SOD Caragana jubata
Zn2+ a Cu,Zn SOD Caragana jubata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 superoxide + 2 H+ Caragana jubata
-
O2 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Caragana jubata A5HIG4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography, dialysis, and ultrafiltration Caragana jubata

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1547
-
purified recombinant enzyme, 0°C, pH 7.8 Caragana jubata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 superoxide + 2 H+
-
Caragana jubata O2 + H2O2
-
?
additional information enzyme activity assay method using riboflavin and nitroblue tetrazolium (NBT) reduction Caragana jubata ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 17500, His-tagged enzyme, SDS-PAGE, 2 * 15160, sequence calculation Caragana jubata
monomer 1 * 17500, His-tagged enzyme, SDS-PAGE, 1 * 15160, sequence calculation Caragana jubata
More the enzyme exists in both monomeric and dimeric forms, the latter being more active. Circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD, secondary structure analysis, overview Caragana jubata

Synonyms

Synonyms Comment Organism
Cj-Cu, Zn SOD
-
Caragana jubata
Cu, Zn superoxide dismutase
-
Caragana jubata
SOD
-
Caragana jubata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
-
4
-
Caragana jubata

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
80 activity range between -10-80°C Caragana jubata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD. Thermal inactivation first-order kinetics Caragana jubata
80
-
recombinant enzyme SOD Cj-Cu,Zn SOD shows a residual SOD activity of 26.07% after being heated for 160 min Caragana jubata
121
-
Cj-Cu,Zn SOD retains 50% of the maximum activity after autoclaving, autoclaved Ca-Cu,Zn SOD exhibits 40% of maximum activity of unautoclaved enzyme at 20°C and 30°C. Thermal inactivation kinetics of Ca-Cu,Zn SOD, overview Caragana jubata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Caragana jubata

pH Range

pH Minimum pH Maximum Comment Organism
6 9 activity range Caragana jubata

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 10 purified recombinant His-tagged enzyme, stable for 2 and 24 h of incubation,after which it retains over 80% activity, 20–30% decrease in activity is observed at pH 10.0 Caragana jubata

pI Value

Organism Comment pI Value Maximum pI Value
Caragana jubata sequence calculation
-
5.82