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Literature summary for 1.11.1.11 extracted from

  • Mathews, M.C.; Summers, C.B.; Felton, G.W.
    Ascorbate peroxidase: a novel antioxidant enzyme in insects (1997), Arch. Insect Biochem. Physiol., 34, 57-68.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Hydroxyurea 26% inhibition at 1 mM Helicoverpa zea
KCN 10% inhibition at 5 mM Helicoverpa zea
p-Aminophenol not inhibitory Helicoverpa zea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
H2O2
-
Helicoverpa zea
0.14
-
ascorbate
-
Helicoverpa zea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
10000
-
partially purified enzyme, molecular weight cut-off centrifugation Helicoverpa zea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ascorbate + H2O2 Helicoverpa zea the enzyme may be important in removing H2O2 and lipid peroxides in insects dehydroascorbate + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Helicoverpa zea
-
larvae
-

Purification (Commentary)

Purification (Comment) Organism
partial, from whole body homogenate, using ammonium sulfate fractionation, column chromatography on Sephadex G-75 and isoelectric focusing. Second isolation of the enzyme: from regurgitant of actively feeding fifth instar organism, using centrifugation, a concentrator and isoelectric focusing Helicoverpa zea

Source Tissue

Source Tissue Comment Organism Textmining
fat body 55.6% relative activity to salivary gland Helicoverpa zea
-
malpighian tubule 31.1% relative activity to salivary gland Helicoverpa zea
-
midgut 20% relative activity to salivary gland Helicoverpa zea
-
salivary gland highest activity Helicoverpa zea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.1
-
substrate: cumene hydroperoxide Helicoverpa zea
19.2
-
substrate: tert-butyl hydroperoxide Helicoverpa zea
20.9
-
substrate: H2O2 Helicoverpa zea
46.7
-
partially purified enzyme Helicoverpa zea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cysteine + H2O2 enzyme partially purified from whole body homogenate, 40% of the activity with L-ascorbate Helicoverpa zea ? + H2O
-
?
cytochrome c + H2O2 enzyme partially purified from whole body homogenate, 44% of the activity with L-ascorbate Helicoverpa zea ? + H2O
-
?
glutathione + H2O2 enzyme partially purified from whole body homogenate: 22% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 0% relative activity to L-ascorbate, when assayed at the same concentration Helicoverpa zea ? + H2O
-
?
guaiacol + H2O2 no activity Helicoverpa zea ?
-
?
L-ascorbate + H2O2 tert-butyl hydroperoxide and cumene hydroperoxide also serve as electron acceptor Helicoverpa zea dehydroascorbate + H2O
-
?
L-ascorbate + H2O2 L-ascorbate is the most effective natural electron donor Helicoverpa zea dehydroascorbate + H2O
-
?
L-ascorbate + H2O2 the enzyme may be important in removing H2O2 and lipid peroxides in insects Helicoverpa zea dehydroascorbate + 2 H2O
-
?
L-ascorbic acid + cumene hydroperoxide 34% of the activity with H2O2 Helicoverpa zea dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
-
?
L-ascorbic acid + tert-butylhydroperoxide 92% of the activity with H2O2 Helicoverpa zea dehydroascorbate + tert-butylalcohol
-
?
additional information no activity with guaiacol Helicoverpa zea ?
-
?
NADPH + H2O2 enzyme partially purified from whole body homogenate: 93% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 36% of the activity with L-ascorbate, when assayed at the same concentration Helicoverpa zea ? + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 10000, SDS-PAGE, partially purified enzyme Helicoverpa zea

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
complete loss of activity Helicoverpa zea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Helicoverpa zea

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme may not be a heme-peroxidase Helicoverpa zea