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Literature summary for 1.1.3.13 extracted from

  • Jadhav, U.; Dawkar, V.; Tamboli, D.; Govindwar, S.
    Purification and characterization of veratryl alcohol oxidase from Comamonas sp. UVS and its role in decolorization of textile dyes (2009), Biotechnol. Bioprocess Eng., 14, 369-376.
No PubMed abstract available

Application

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
SDS-PAGE Comamonas sp.

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Comamonas sp.
-
-
-
Comamonas sp. UVS
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-cellulose column chromatography and Biogel P-100 gel filtration Comamonas sp.

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
VAO
-
Comamonas sp.
veratryl alcohol oxidase
-
Comamonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
at pH 3.0 Comamonas sp.

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
-
Comamonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
Comamonas sp.