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EC Tree
The enzyme appears in viruses and cellular organisms
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glycerol + O2 = glyceraldehyde + H2O2
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glycerol:oxygen 1-oxidoreductase
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1,3-propanediol + O2
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dihydroxyacetone + O2
3-hydroxy-2-oxopropanal + H2O2
glycerol + O2
glyceraldehyde + H2O2
additional information
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1,3-butanediol + O2
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1,3-butanediol + O2
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1,4-butanediol + O2
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1,4-butanediol + O2
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D-fructose + O2
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slight oxidation activity
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D-fructose + O2
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slight oxidation activity
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D-galactose + O2
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slight oxidation activity
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D-galactose + O2
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slight oxidation activity
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dihydroxyacetone + O2
3-hydroxy-2-oxopropanal + H2O2
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58.8% activity compared to glycerol
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dihydroxyacetone + O2
3-hydroxy-2-oxopropanal + H2O2
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132% activity compared to glycerol
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dihydroxyacetone + O2
3-hydroxy-2-oxopropanal + H2O2
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132% activity compared to glycerol
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glycerol + O2
glyceraldehyde + H2O2
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glycerol + O2
glyceraldehyde + H2O2
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100% activity
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glycerol + O2
glyceraldehyde + H2O2
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100% activity
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glycerol + O2
glyceraldehyde + H2O2
17% activity compared to methanol
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additional information
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no activity with glycerol 3-phosphate, methanol, ethanol, and polyvinyl alcohol
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additional information
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no activity with glycerol 3-phosphate, methanol, ethanol, and polyvinyl alcohol
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?
additional information
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the enzyme does not oxidize 1,2-propanediol, 1,3-butanediol, glyceraldehyde, glycero-3-phosphate, 3-phosphoglyceric acid, methanol, ethanol, n-propanol, iso-propanol, n-butanol, ethylene glycol, D-glucose, D-galactose, and phenol
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?
additional information
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the enzyme does not oxidize 1,2-propanediol, 1,3-butanediol, glyceraldehyde, glycero-3-phosphate, 3-phosphoglyceric acid, methanol, ethanol, n-propanol, iso-propanol, n-butanol, ethylene glycol, D-glucose, D-galactose, and phenol
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glycerol + O2
glyceraldehyde + H2O2
glycerol + O2
glyceraldehyde + H2O2
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?
glycerol + O2
glyceraldehyde + H2O2
17% activity compared to methanol
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?
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protoheme IX
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the enzyme contains 0.94 mol of heme per mol of enzyme
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Co2+
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contains 2 atoms of copper per mol of enzyme
Cu2+
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15% increase of activity in the presence of 1 mM Cu2+
Fe3+
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10% increase of activity in the presence of 1 mM Fe3+
Zn2+
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contains 0.76 atoms of zinc per mol of enzyme. Zn2+ is the most effective cation with activation being 2.3fold at a concentration of 1.0 mM
Zn2+
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15% increase of activity in the presence of 1 mM Zn2+
additional information
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the enzyme does not contain molybdenum and manganese
additional information
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not influenced by Co2+, Mn2+, Mg2+, Pb2+, Ca2+, and Cd2+
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2-mercaptoethanol
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25% inhibition at 0.01 mM
8-hydroxyquinoline
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7.9% inhibition at 1 mM
Chloramine T
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60% inhibition at 1 mM
diethyldithiocarbamate
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40.1% inhibition at 1 mM
dimercapto-1-propanol
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56.3% inhibition at 0.01 mM
dithiothreitol
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26.5% inhibition at 0.01 mM
ethyl xanthate
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27.1% inhibition at 0.1 mM
Hg2+
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60% inhibition at 1 mM
hydroxylamine
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87% inhibition at 1 mM
KCN
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complete inhibition at 1 mM
L-ascorbic acid
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31.2% inhibition at 0.1 mM
L-cysteine
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12.2% inhibition at 0.1 mM
NaN3
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complete inhibition at 1 mM
reduced glutathione
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40.8% inhibition at 0.1 mM
Salicylaldoxime
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11.2% inhibition at 1 mM
sodium sulfite
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46.2% inhibition at 0.1 mM
Tetranitromethane
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46% inhibition at 1 mM
additional information
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EDTA, phenylglycoxyl, iodoacetic acid, and o-phenanthroline do not show significant inhibitory effects on the enzyme activity
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Borate
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exposure of the enzyme to borate buffer of pH 10.0 results in activation of the enzyme
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1.9
glycerol
at pH 9.0 and 50°C
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0.012
dimercapto-1-propanol
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at pH 7.0 and 37°C
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1.7
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crude extract, at pH 7.0 and 30°C
66.7
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after 39.2fold purification, at pH 7.0 and 30°C
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7 - 10
more than 60% activity between pH 7.0 and 10.0
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brenda
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brenda
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UniProt
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brenda
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T2M2J4_PHACH
651
0
72537
TrEMBL
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75000
2 * 75000, SDS-PAGE
400000
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gel filtration
400000
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sedimentation equilibrium method
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homodimer
2 * 75000, SDS-PAGE
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5.5 - 6.5
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the enzyme is stable in the pH range from 5.5 to 6.5
738126
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20 - 60
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after 1 h of incubation, the enzyme is relatively stable from 20 to 40°C and loses most of its activity over 50°C
45 - 50
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the enzyme is stable up to 45°C and loses about 40% of activity at 50°C in 50 mM TES buffer, pH 7.0
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5°C, activated enzyme at pH 8.0-10.0, 1 week, no loss of activity
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ammonium sulfate fractionation, Sephadex G-100 gel filtration, Fractogel DEAE-650M column chromatography, Toyopearl phenyl-650M column chromatography, and Ultrogel hydroxyapatite column chromatography
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DEAE-Sephadex A-25 column chromatography, hydroxylapatite column chromatography, and Sephadex G-200 gel filtration
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Superdex 75 gel filtration
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Lin, S.F.; Chiou, C.M.; Tsai, Y.C.
Purification and characterization of a glycerol oxidase from Penicillium sp. TS-622
Enzyme Microb. Technol.
18
383-387
1996
Penicillium sp., Penicillium sp. TS-622
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Linke, D.; Lehnert, N.; Nimtz, M.; Berger, R.G.
An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity
Enzyme Microb. Technol.
61-62
7-12
2014
Phanerochaete chrysosporium (T2M2J4), Phanerochaete chrysosporium
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Uwajima, T.; Shimizu, Y.; Terada, O.
Glycerol oxidase, a novel copper hemoprotein from Aspergillus japonicus. Molecular and catalytic properties of the enzyme and its application to the analysis of serum triglycerides
J. Biol. Chem.
259
2748-2753
1984
Aspergillus japonicus, Aspergillus japonicus AT 008
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Enzyme Nomenclature
1.1.3.B4 glycerol oxidase
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