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Literature summary for 1.15.1.1 extracted from

  • Yamamoto, K.; Kimura, M.; Aso, Y.; Banno, Y.; Koga, K.
    Characterization of superoxide dismutase from the fall webworm, Hyphantria cunea: comparison of its properties to superoxide dismutase from the silkworm Bombyx mori (2007), Appl. Entomol. Zool., 42, 465-472.
No PubMed abstract available
Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene sod, DNA and amino acid sequence determination and analysis Bombyx mori
gene sod, DNA and amino acid sequence determination and analysis, functional overexpression of the soluble enzyme in Escherichia coli Hyphantria cunea

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a Cu,Zn-SOD Bombyx mori
Cu2+ a Cu,Zn-SOD Hyphantria cunea
additional information the enzyme contains 6 metal binding sites Hyphantria cunea
additional information the enzyme contains 7 metal binding sites Bombyx mori
Zn2+ a Cu,Zn-SOD Bombyx mori
Zn2+ a Cu,Zn-SOD Hyphantria cunea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15832
-
 x * 15832, sequence calculation Hyphantria cunea
15841
-
 x * 15841, sequence calculation Bombyx mori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O2.- + H+ Bombyx mori SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms O2 + H2O2
-
 ?
O2.- + H+ Hyphantria cunea SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms O2 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Bombyx mori
-
 silkworm
-
Hyphantria cunea A7BI63 fall webworm, gene sod
-

Purification (Commentary)

Purification (Comment) Organism
soluble recombinant enzyme from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography to homogeneity Hyphantria cunea

Source Tissue

Source Tissue Comment Organism Textmining
fat body larval tissue Hyphantria cunea
-
hemocyte larval tissue Hyphantria cunea
-
larva fourth-instar larva Hyphantria cunea
-
midgut larval tissue Hyphantria cunea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5780
-
 purified recombinant enzyme Hyphantria cunea
7980
-
 purified recombinant enzyme Bombyx mori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate i.e. WST-1, activity assay detection method Hyphantria cunea ?
-
 ?
O2.- + H+
-
 Bombyx mori O2 + H2O2
-
 ?
O2.- + H+
-
 Hyphantria cunea O2 + H2O2
-
 ?
O2.- + H+ SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms Bombyx mori O2 + H2O2
-
 ?
O2.- + H+ SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms Hyphantria cunea O2 + H2O2
-
 ?

Subunits

Subunits Comment Organism
? x * 15832, sequence calculation Hyphantria cunea
? x * 15841, sequence calculation Bombyx mori

Synonyms

Synonyms Comment Organism
Cu,Zn-SOD
-
 Bombyx mori
Cu,Zn-SOD
-
 Hyphantria cunea
SOD
-
 Bombyx mori
SOD
-
 Hyphantria cunea

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 and below, 30 min, purified recombinant enzyme, completely stable Hyphantria cunea
40
-
 and below, completely stable Bombyx mori

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 11 stable Bombyx mori
5 11 purified recombinant enzyme, stable Hyphantria cunea

pI Value

Organism Comment pI Value Maximum pI Value
Hyphantria cunea sequence calculation
-
 5.65
Bombyx mori sequence calculation
-
 5.78