Information on EC 1.1.3.21 - glycerol-3-phosphate oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.3.21
-
RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Glycerophospholipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9046-28-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CETC 978
-
-
Manually annotated by BRENDA team
strain DBM 1509
-
-
Manually annotated by BRENDA team
10C1
-
-
Manually annotated by BRENDA team
F24
-
-
Manually annotated by BRENDA team
M74-LC
-
-
Manually annotated by BRENDA team
strain T1
-
-
Manually annotated by BRENDA team
Mycoplasma mycoides subsp. mycoides SC strain Afade
-
UniProt
Manually annotated by BRENDA team
strain T1
-
-
Manually annotated by BRENDA team
; gene glpD
-
-
Manually annotated by BRENDA team
no activity in Mycoplasma mycoides
mutant strain
-
-
Manually annotated by BRENDA team
no activity in Mycoplasma mycoides G1
mutant strain
-
-
Manually annotated by BRENDA team
Pediococcus sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
-
-
r
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
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 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
10 mM, 7.7fold activation
CoCl2
-
10 mM, 10.2fold activation
KCl
-
100 mM, 5.8fold activation
MgCl2
-
10 mM, 6.8fold activation
MnCl2
-
10 mM, 7.6 fold activation
NaCl
-
100 mM, 3.8fold activation
ZnCl2
-
1 mM, 6.3fold activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acriflavine
-
8 mM, 50% inhibition
Atebrin
-
25 mM, 50% inhibition
azide
-
5 mM, 50% inhibition
benzoylformic acid
-
strain CETC 978, competitive inhibition
carboxylate
-
structural characterization of enzyme-inhibitor interaction
fructose-1-phosphate
-
-
fructose-6-phosphate
-
-
glyoxylic acid
-
strain CETC 978, competitive inhibition
iodoacetate
-
1 mM, less than 20% inhibition
methylglyoxal
-
strain CETC 978, 277 mM, complete inactivation after 50 min, in the presence of 30 mM benzoylformic acid complete inactivation after 20 min
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminoantipirine
-
0.009%, ranging from 0.006 to 0.074%
glycerol
-
strain DBM 1509, 50%
Phenol
-
activity positively affected by the presence of 0.018% phenol, ranging from 0.006 to 0.123%
Triton X-100
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 36.2
L-alpha-glycerophosphate
0.052 - 0.46
O2
6 - 26
sn-glycerol-3-phosphate
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.2 - 17.9
L-alpha-glycerophosphate
23.8
L-glycerophosphate
Enterococcus faecium
-
strain ATCC 12755
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.025
-
enzyme activity in cell extracts
15.6
-
strain F-24
62
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strain ATCC 12755
85 - 95
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strain ATCC 12755
433.2
-
strain CETC 978
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
strain CETC 978
8.5
-
assayed between pH 5.0 and pH 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.7
-
pH 5.0: about 50% of activity maximum, pH 6.7: about 30% of activity maximum
5 - 10
-
activity within, optimum at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
immobilized enzyme
60
-
at pH 8.0, tested at temperatures of 25, 30, 37, 45, 50, 55, 60, 65, 70C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
-
activity measured after incubating the enzyme in Tris/HCl buffer at various temperatures for 1 h
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
two bands at 45000 and 90000 Da, SDS-PAGE
90000
two bands at 45000 and 90000 Da, SDS-PAGE
123000
-
strain ATCC 12755, sedimentation equilibrium
131000
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strain ATCC 12755, gel filtration, sucrose density centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
intact GlpO structure, refined at 2.4 A resolution and structure of a deletion mutant lacking 50-residue insert, refined at 2.3 A resolution, multiwavelength anomalous dispersion data
-
microseeding and hanging-drop vapor-equilibrium method, best condition for the growth of large crystals are 18-20% PEG 1000, 0.1 M Tris, pH 8.0, 0.2 M MgCl2*6H2O
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
lower activity above pH 9.0, tested in a range between pH 6-10
688443
9
-
strain DBM 1509
287569
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
-
activity measured after incubating the enzyme solution for 1 h at various temperatures of 0, 30, 50, 60, 70, 80C in Tris/HCl buffer, activity of 0.222 U/ml at 0C and of 0.238 U/ml at 80C
70
-
15 min,immobilized enzyme, 50% remaining activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme coimmobilized with lipase, glycerol kinase and peroxidase onto glutaraldehyde onto glutaraldehyde activated alkylamine glass beads is active even after regulate use for 6 months when stored at 4C in distilled water. Immobilized enzyme possess higher pH and thermal and storage stability than soluble enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 40 d, 13% loss of activity, 4C, 14 d, 92% loss of activity, 30, 24 h, 90% loss of activity, 40C, 80 min, 80% loss of activity, 4C, 0.2% dithiothreitol, 20 d, 32% loss of activity, 4C, 0.2% mercaptoethanol, 20 d, 34% loss of activity, 4C, 50% glycerol, 20 d, 36% loss of activity, 4C, 100 mM EDTA, 20 d, 24% loss of activity, 4C, 2.5% polyethylenglycol, 20 d, 63% loss of activity, 4C, lyophilization, 2% dextrin II 14 d, 35% loss of activity, 20C, lyophilization, 2% dextrin II, 14 d, 60% loss of activity, 37C, lyophilization, 2% dextrin II, 14 d, 85% loss of activity
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2C, several weeks, slow decline of activity
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40C, during storage for 21 days 20% of activity lost, sodium azide as stabilizer in a concentration of 0.05% maintains activity of the enzyme in 98.4%, addition of sucrose maintains only 74% of activity
-
immobilized enzyme, 50% loss of activity after 150 uses in analysis for triglycerides, within 33 days at 4C in 0.1 M sodium phosphate buffer, pH 7.0
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant protein
-
Ni-NTA column chromatography
strain CETC 978, Triton X-114, ammonium sulfate, ion-exchange chromatography, hydrophobic chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli, strain B834, pQE30 and pREP4 vectors
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gene glpD, DNA sequence determination of wild-type and transposon insertion mutant enzymes, expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Ers protein acts as a positive regulator of the glpKOF operon encoding glycerol-3-phosphate oxidase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase on to aryl amine glass beads affixed on plastic strip for determination of triglycerides in serum
synthesis
Pediococcus sp.
-
synthesis of dihydroxyacetone phosphate, enzyme coimmobilized with catalase on oxirane activated acrylic polymer beads, Eupergit C 250
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