Application | Comment | Organism |
---|---|---|
degradation | the purified enzyme is able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 0.04 nm/ml concentration | Comamonas sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cd2+ | 65% residual activity at 0.5 mM | Comamonas sp. | |
Cu2+ | 15% residual activity at 0.5 mM | Comamonas sp. | |
dithiothreitol | 85% residual activity at 0.5 mM | Comamonas sp. | |
EDTA | 75% residual activity at 0.5 mM | Comamonas sp. | |
Hg2+ | 52% residual activity at 0.5 mM | Comamonas sp. | |
K+ | 75% residual activity at 0.5 mM | Comamonas sp. | |
L-cysteine | 70% residual activity at 0.5 mM | Comamonas sp. | |
Mg2+ | 90% residual activity at 0.5 mM | Comamonas sp. | |
Mn2+ | 62% residual activity at 0.5 mM | Comamonas sp. | |
additional information | not inhibited by Ba2+, Ca2+, and Na+ | Comamonas sp. | |
Sodium azide | the enzyme is completely inhibited by 0.5 mM sodium azide | Comamonas sp. | |
Zn2+ | 35% residual activity at 0.5 mM | Comamonas sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
66000 | - |
SDS-PAGE | Comamonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
isopropanol + O2 | Comamonas sp. | - |
2-propanone + H2O2 | - |
? | |
isopropanol + O2 | Comamonas sp. UVS | - |
2-propanone + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas sp. | - |
- |
- |
Comamonas sp. UVS | - |
- |
- |
Purification (Comment) | Organism |
---|---|
DEAE-cellulose column chromatography and Biogel P-100 gel filtration | Comamonas sp. |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
the specific activity of the crude enzyme and after 13.9fold purification is 0.064 and 0.89 units/mg, respectively, using veratryl alcohol as substrate at pH 3.0 and 65°C. The substrate specificity of the VAO enzyme is 1.64 units/mg for n-propanol, 1.43 units/mg for veratryl alcohol, 0.48 units/mg for ethanol, 0.36 units/mg for L-dopa, 0.34 units/mg for indole and hydroxyquinone, 0.28 units/mg for L-tryptophan, and 0.03 units/mg for xylidine. One unit of an enzyme activity is defined as a change in absorbance unit/min/mg protein | Comamonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + O2 | - |
Comamonas sp. | acetaldehyde + H2O2 | - |
? | |
ethanol + O2 | - |
Comamonas sp. UVS | acetaldehyde + H2O2 | - |
? | |
hydroxyquinone + O2 | - |
Comamonas sp. | ? | - |
? | |
indole + O2 | - |
Comamonas sp. | ? | - |
? | |
indole + O2 | - |
Comamonas sp. UVS | ? | - |
? | |
isopropanol + O2 | - |
Comamonas sp. | 2-propanone + H2O2 | - |
? | |
isopropanol + O2 | - |
Comamonas sp. UVS | 2-propanone + H2O2 | - |
? | |
L-DOPA + O2 | - |
Comamonas sp. | ? | - |
? | |
L-DOPA + O2 | - |
Comamonas sp. UVS | ? | - |
? | |
L-tryptophan + O2 | - |
Comamonas sp. | ? | - |
? | |
n-propanol + O2 | maximum specific activity with n-propanol | Comamonas sp. | n-propanal + H2O2 | - |
? | |
n-propanol + O2 | maximum specific activity with n-propanol | Comamonas sp. UVS | n-propanal + H2O2 | - |
? | |
veratryl alcohol + O2 | - |
Comamonas sp. | ? | - |
? | |
xylidine + O2 | lowest specific activity with xylidine | Comamonas sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
VAO | - |
Comamonas sp. |
veratryl alcohol oxidase | - |
Comamonas sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
at pH 3.0 | Comamonas sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
the enzyme loses its activity after 5 h and 15 h at pH 3.0 and pH 7.0, respectively | Comamonas sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3 | - |
- |
Comamonas sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Comamonas sp. |