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Literature summary for 1.11.1.11 extracted from

  • Jones, D.K.; Dalton, D.A.; Rosell, F.I.; Raven, E.L.
    Class I heme peroxidases: characterization of soybean ascorbate peroxidase (1998), Arch. Biochem. Biophys., 360, 173-178.
    View publication on PubMed
Search for more literature for 1.11.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
-
 soybean
-

Source Tissue

Source Tissue Comment Organism Textmining
root nodules Glycine max
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32
-
 recombinant enzyme Glycine max
34
-
 wild-type enzyme Glycine max

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ascorbate + H2O2
-
 Glycine max dehydroascorbate + H2O
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
49
-
 melting temperature of the ferric derivative, monitored by circular dichroism spectroscopy Glycine max
57
-
 melting temperature of the ferric-cyanide derivative, monitored by circular dichroism spectroscopy Glycine max

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Glycine max

Cofactor

Cofactor Comment Organism Structure
heme
-
 Glycine max
additional information electronic, EPR, and NMR spectra are consistent with a high-spin ferric resting state for the enzyme at 298K, low temperature EPR and electronic absorption experiments indicate formation of a low-spin heme derivative at these temperatures, the midpoint reduction potential for the Fe(III)/Fe(II) redox couple, determined by spectroelectrochemistry is -159 mV vs SHE, sodium phosphate: pH 7, 25°C, 0.10 M Glycine max