Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Glycine max |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Glycine max | - |
soybean | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
root | nodules | Glycine max | - |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ascorbate + H2O2 | - |
Glycine max | dehydroascorbate + H2O | - |
? |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Glycine max |
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 |