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Literature summary extracted from
- Class I heme peroxidases: characterization of soybean ascorbate peroxidase (1998), Arch. Biochem. Biophys., 360, 173-178.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.11.1.11 | expression in Escherichia coli | Glycine max |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.11 | Glycine max | - |
soybean | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.11.1.11 | root | nodules | Glycine max | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.11 | 32 | - |
recombinant enzyme | Glycine max |
| 1.11.1.11 | 34 | - |
wild-type enzyme | Glycine max |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.11 | L-ascorbate + H2O2 | - |
Glycine max | dehydroascorbate + H2O | - |
? |  |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.11 | 49 | - |
melting temperature of the ferric derivative, monitored by circular dichroism spectroscopy | Glycine max |
| 1.11.1.11 | 57 | - |
melting temperature of the ferric-cyanide derivative, monitored by circular dichroism spectroscopy | Glycine max |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.11 | 7 | - |
assay at | Glycine max |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.11 | heme | - |
Glycine max | |
| 1.11.1.11 | 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 |
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Release 2023.1 (January 2023)
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