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Enzyme Nomenclature
Information on EC 1.1.3.B4 - glycerol oxidase
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1.1.3.B4 glycerol oxidaseSpecify your search results
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The enzyme appears in viruses and cellular organisms
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
glycerol + O2 = glyceraldehyde + H2O2
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SYSTEMATIC NAME
IUBMB Comments
glycerol:oxygen 1-oxidoreductase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerol + O2
glyceraldehyde + H2O2
17% activity compared to methanol
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
400000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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)
brenda
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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