Information on EC 1.1.3.B4 - glycerol oxidase

for references in articles please use BRENDA:EC1.1.3.B4
Word Map on EC 1.1.3.B4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.1.3.B4
preliminary BRENDA-supplied EC number
top print hide
RECOMMENDED NAME
GeneOntology No.
glycerol oxidase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycerol + O2 = glyceraldehyde + H2O2
show the reaction diagram
-
-
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
glycerol:oxygen 1-oxidoreductase
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-butanediol + O2
?
show the reaction diagram
1,3-propanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,4-butanediol + O2
?
show the reaction diagram
D-fructose + O2
?
show the reaction diagram
D-galactose + O2
?
show the reaction diagram
dihydroxyacetone + O2
3-hydroxy-2-oxopropanal + H2O2
show the reaction diagram
glycerol + O2
glyceraldehyde + H2O2
show the reaction diagram
additional information
?
-
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerol + O2
glyceraldehyde + H2O2
show the reaction diagram
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protoheme IX
-
the enzyme contains 0.94 mol of heme per mol of enzyme
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
contains 2 atoms of copper per mol of enzyme
Cu2+
-
15% increase of activity in the presence of 1 mM Cu2+
Fe3+
-
10% increase of activity in the presence of 1 mM Fe3+
Mg2+
-
activates
Mn2+
-
activates
Ni2+
-
activates
additional information
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
25% inhibition at 0.01 mM
8-hydroxyquinoline
-
7.9% inhibition at 1 mM
Chloramine T
-
60% inhibition at 1 mM
diethyldithiocarbamate
-
40.1% inhibition at 1 mM
dimercapto-1-propanol
-
56.3% inhibition at 0.01 mM
dithiothreitol
-
26.5% inhibition at 0.01 mM
ethyl xanthate
-
27.1% inhibition at 0.1 mM
Hg2+
-
60% inhibition at 1 mM
hydroxylamine
-
87% inhibition at 1 mM
KCN
-
complete inhibition at 1 mM
L-ascorbic acid
-
31.2% inhibition at 0.1 mM
L-cysteine
-
12.2% inhibition at 0.1 mM
NaN3
-
complete inhibition at 1 mM
reduced glutathione
-
40.8% inhibition at 0.1 mM
Salicylaldoxime
-
11.2% inhibition at 1 mM
sodium sulfite
-
46.2% inhibition at 0.1 mM
Tetranitromethane
-
46% inhibition at 1 mM
additional information
-
EDTA, phenylglycoxyl, iodoacetic acid, and o-phenanthroline do not show significant inhibitory effects on the enzyme activity
-
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Borate
-
exposure of the enzyme to borate buffer of pH 10.0 results in activation of the enzyme
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9
glycerol
at pH 9.0 and 50°C
top print hide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
dimercapto-1-propanol
-
at pH 7.0 and 37°C
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7
-
crude extract, at pH 7.0 and 30°C
66.7
-
after 39.2fold purification, at pH 7.0 and 30°C
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
-
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
more than 60% activity between pH 7.0 and 10.0
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
isoelectric focusing
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75000
2 * 75000, SDS-PAGE
400000
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 75000, SDS-PAGE
top print hide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
the enzyme is stable in the pH range from 5.5 to 6.5
738126
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
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
-
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
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5°C, activated enzyme at pH 8.0-10.0, 1 week, no loss of activity
-
top print hide
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
-
DEAE-Sephadex A-25 column chromatography, hydroxylapatite column chromatography, and Sephadex G-200 gel filtration
-
Superdex 75 gel filtration
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.1.3.B4)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)