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
1.1.3.21
-
RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alpha-glycerol-3-phosphate oxidase
Q70GP9
-
alpha-glycerol-3-phosphate oxidase
Mycoplasma mycoides subsp. mycoides SC strain Afade
Q70GP9
-
-
alpha-glycerophosphate oxidase
-
-
-
-
alpha-glycerophosphate oxidase
-
-
GlpO
Mycoplasma mycoides subsp. mycoides SC strain Afade
Q70GP9
-
-
GlpO protein
-
-
glycerol phosphate oxidase
-
-
-
-
glycerol-1-phosphate oxidase
-
-
-
-
glycerol-3-P oxidase
Q833L7
-
Glycerol-3-phosphate oxidase
-
-
-
-
Glycerol-3-phosphate oxidase
-
-
GPO
Enterococcus faecium M74-LC
-
-
-
L-alpha-glycerol-3-phosphate oxidase
-
-
-
-
L-alpha-glycerophosphate oxidase
-
-
-
-
L-alpha-glycerophosphate oxidase
-
-
L-alpha-glycerophosphate oxidase
Q70GP9
-
L-alpha-glycerophosphate oxidase
Mycoplasma mycoides subsp. mycoides SC strain Afade
Q70GP9
-
-
oxidase, glycerol phosphate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9046-28-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CETC 978
-
-
Manually annotated by BRENDA team
strain DBM 1509
-
-
Manually annotated by BRENDA team
Aerococcus viridans CETC 978
strain CETC 978
-
-
Manually annotated by BRENDA team
Aerococcus viridans DBM 1509
strain DBM 1509
-
-
Manually annotated by BRENDA team
Enterococcus faecalis 10C1
10C1
-
-
Manually annotated by BRENDA team
Enterococcus faecium F24
F24
-
-
Manually annotated by BRENDA team
Enterococcus faecium M74-LC
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
Mycoplasma mycoides T1
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
LITERATURE
malfunction
-
the glpD mutant strain GPM52 (glpD gene disrupted between nucleotides 555 and 556, resulting in a truncated protein of 185 amino acids) does not grow at all in glycerol-containing medium
malfunction
-
the glpD mutant strain GPM52 (glpD gene disrupted between nucleotides 555 and 556, resulting in a truncated protein of 185 amino acids) does not grow at all in glycerol-containing medium
-
metabolism
-
glycerol is one of the few carbon sources that can be utilized by Mycoplasma pneumoniae. Glycerol metabolism involves uptake by facilitated diffusion, phosphorylation, and the oxidation of glycerol 3-phosphate to dihydroxyacetone phosphate, a glycolytic intermediate. Glycerol metabolism is important for cytotoxicity of Mycoplasma pneumoniae with the enzyme being important but not essential, overview
metabolism
-
glycerol is one of the few carbon sources that can be utilized by Mycoplasma pneumoniae. Glycerol metabolism involves uptake by facilitated diffusion, phosphorylation, and the oxidation of glycerol 3-phosphate to dihydroxyacetone phosphate, a glycolytic intermediate. Glycerol metabolism is important for cytotoxicity of Mycoplasma pneumoniae with the enzyme being important but not essential, overview
-
physiological function
Q70GP9
GlpO is involved in production and translocation of toxic H2O2 into the host cell, causing inflammation and cell death
physiological function
-
the formation of hydrogen peroxide by GlpD is crucial for cytotoxic effects of Mycoplasma pneumoniae. The glycerol 3-phosphate oxidase encoded by glpD is essential for glycerol utilization
physiological function
-
the formation of hydrogen peroxide by GlpD is crucial for cytotoxic effects of Mycoplasma pneumoniae. The glycerol 3-phosphate oxidase encoded by glpD is essential for glycerol utilization
-
physiological function
Mycoplasma mycoides subsp. mycoides SC strain Afade
-
GlpO is involved in production and translocation of toxic H2O2 into the host cell, causing inflammation and cell death
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
r
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
Q833L7
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
Q70GP9
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
involved in the glycerate metabolism
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
from triolein, coupled assay method by use of co-immobilized lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase, overview
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
involved in the glycerate metabolism
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
Mycoplasma mycoides subsp. mycoides SC strain Afade
Q70GP9
-
-
-
?
glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
-
-
r
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Pediococcus sp.
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
other electron acceptors: ferricyanide
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
2,6-dichloroindophenol, at lower rate than O2
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
ferricyanide, in absence of O2
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
methylene blue and cytochrome c, at very low rate, high specificity for L-alpha-glycerophosphate
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
high specificity for L-alpha-glycerophosphate
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
structural characterization, substrate binding site
-
-
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Enterococcus faecalis 10C1
-
2,6-dichloroindophenol, at lower rate than O2, methylene blue and cytochrome c, at very low rate, high specificity for L-alpha-glycerophosphate
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Aerococcus viridans DBM 1509
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Aerococcus viridans CETC 978
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Mycoplasma mycoides T1
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Enterococcus faecium F24
-
-
i.e. dihydroxyacetone phosphate
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
Q833L7
-
-
-
?
glycerol 3-phosphate + O2
dihydroxyacetone phosphate + H2O2
show the reaction diagram
-
involved in the glycerate metabolism
-
-
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Pediococcus sp.
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
-
structural characterization, substrate binding site
-
-
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Enterococcus faecalis 10C1
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Aerococcus viridans DBM 1509
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Aerococcus viridans CETC 978
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Mycoplasma mycoides T1
-
-
i.e. dihydroxyacetone phosphate
?
sn-glycerol-3-phosphate + O2
glycerone phosphate + H2O2
show the reaction diagram
Enterococcus faecium F24
-
-
i.e. dihydroxyacetone phosphate
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
prosthetic group
FAD
-
2 mol bound per mol of enzyme; prosthetic group
FAD
-
prosthetic group
FAD
Pediococcus sp.
-
-
FAD
-
the first two domains of the GlpO protein fold involved in FAD binding, linkage of substrate-binding domain to a beta-beta-alpha element of the FAD-binding domain
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
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
-
not inhibited by KCN, azide, iodoacetate or p-chloromercurobenzoate
-
additional information
-
strain CETC 978, not inhibited by 20-80 mM fructose-1-phosphate or fructose-6-phosphate
-
additional information
-
absence of carbon catabolite repression in the expression of the enzymes of glycerol metabolism
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-aminoantipirine
-
0.009%, ranging from 0.006 to 0.074%
Phenol
-
activity positively affected by the presence of 0.018% phenol, ranging from 0.006 to 0.123%
Triton X-100
-
strain DBM 1509, 1%
Triton X-100
-
0.1% of Triton X-100 slightly stimulates enzyme activity
glycerol
-
strain DBM 1509, 50%
additional information
-
increasing the buffer concentration from 10 mM to 100 mM leads to an 2.6-10fold increase in activity, this effect is observed with potassium phosphate, sodium acetate, sodium maleate or other anionic buffers
-
additional information
-
absence of substrate induction in the expression of the enzymes of glycerol metabolism
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
L-alpha-glycerophosphate
-
pH 7.0, 5C, wild-type enzyme, intact
2.3
L-alpha-glycerophosphate
-
strain CETC 978
4
L-alpha-glycerophosphate
-
-
6.6
L-alpha-glycerophosphate
-
pH 7.0, 5C, recombinant deletion mutant
0.052
O2
-
pH 7.0, 5C, wild-type enzyme, intact
0.069
O2
-
pH 7.0, 5C, wild-type enzyme, nicked
0.46
O2
-
pH 7.0, 5C, recombinant deletion mutant
6
sn-glycerol-3-phosphate
-
-
26
sn-glycerol-3-phosphate
-
-
36.2
L-alpha-glycerophosphate
-
pH 7.0, 5C, wild-type enzyme, nicked
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.2
L-alpha-glycerophosphate
-
10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5C, recombinant deletion mutant
14.1
L-alpha-glycerophosphate
-
10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5C, wild-type enzyme, nicked
17.9
L-alpha-glycerophosphate
-
10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5C, wild-type enzyme, intact
23.8
L-glycerophosphate
-
strain ATCC 12755
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.025
-
enzyme activity in cell extracts
15.6
-
strain F-24
62
-
strain ATCC 12755
85 - 95
-
strain ATCC 12755
433.2
-
strain CETC 978
additional information
-
0.118 ml O2/min/mg
additional information
-
structural characterization, wild-type and deletion mutant, FAD- and substrate binding sites identified, active-site overlays, residues interacting with the amino acid substrate or with inhibitor carboxylate identified, structural and functional divergence between alpha-glycerophosphate oxidase (GlpO) and the bacterial and mitochondrial alpha-glycerophosphate dehydrogenases (GlpDs) discussed
additional information
-
consumption of oxygen determined by oxygraphy, activity measured by peroxidase chromogen method, a 120 min reaction time and a concentration of 0.5 M of glycerol phosphate considered as best conditions for determination of enzyme activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
strain DBM 1509
7.5
-
immobilized enzyme
7.5
-
assay at
8
-
strain CETC 978
8.5
-
assayed between pH 5.0 and pH 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
activity within, optimum at pH 8.5
5 - 6.7
-
pH 5.0: about 50% of activity maximum, pH 6.7: about 30% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
strain DBM 1509
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
LITERATURE
30 - 80
-
activity measured after incubating the enzyme in Tris/HCl buffer at various temperatures for 1 h
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the major fraction of GlpD is present in the cytoplasm
Manually annotated by BRENDA team
-
the major fraction of GlpD is present in the cytoplasm
-
Manually annotated by BRENDA team
-
membrane-spanning protein, a minor fraction of GlpD is associated with the membrane
Manually annotated by BRENDA team
-
membrane-spanning protein, a minor fraction of GlpD is associated with the membrane
-
Manually annotated by BRENDA team
additional information
-
subcellular localization analysis, overview
-
Manually annotated by BRENDA team
additional information
-
subcellular localization analysis, overview
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
Q70GP9
two bands at 45000 and 90000 Da, SDS-PAGE
713579
90000
Q70GP9
two bands at 45000 and 90000 Da, SDS-PAGE
713579
123000
-
strain ATCC 12755, sedimentation equilibrium
287565
131000
-
strain ATCC 12755, gel filtration, sucrose density centrifugation
287564
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
strain CETC 978, x * 63000, SDS-PAGE
?
Aerococcus viridans CETC 978
-
strain CETC 978, x * 63000, SDS-PAGE
-
dimer
-
2 * 72000, SDS-PAGE
dimer
-
2 * 65000, SDS-PAGE
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
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
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
688443
70
-
15 min,immobilized enzyme, 50% remaining activity
698226
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
-
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
-
2C, several weeks, slow decline of activity
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
strain CETC 978, Triton X-114, ammonium sulfate, ion-exchange chromatography, hydrophobic chromatography
-
Ni-NTA column chromatography
Q70GP9
gel filtration, recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
Q70GP9
gene glpD, DNA sequence determination of wild-type and transposon insertion mutant enzymes, expression analysis
-
expressed in Escherichia coli, strain B834, pQE30 and pREP4 vectors
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Ers protein acts as a positive regulator of the glpKOF operon encoding glycerol-3-phosphate oxidase
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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, reusability of the strip-bound enzyme, overview
additional information
Q70GP9
recombinant GlpO lacking the six amino acids Gly12-Gly13-Gly14-Ile15-Ile16-Gly17 (GlpODELTAFAD) is unable to bind FAD and is also devoid of glycerophosphate oxidase activity
additional information
Mycoplasma mycoides subsp. mycoides SC strain Afade
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recombinant GlpO lacking the six amino acids Gly12-Gly13-Gly14-Ile15-Ile16-Gly17 (GlpODELTAFAD) is unable to bind FAD and is also devoid of glycerophosphate oxidase activity
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additional information
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random transposon insertion mutations, construction of the glpD mutant strain GPM52, the glpD mutant exhibits a significantly reduced formation of hydrogen peroxide and a severely reduced cytotoxicity. GlpD disruption does not prevent synthesis of the essential protein GlpK
additional information
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random transposon insertion mutations, construction of the glpD mutant strain GPM52, the glpD mutant exhibits a significantly reduced formation of hydrogen peroxide and a severely reduced cytotoxicity. GlpD disruption does not prevent synthesis of the essential protein GlpK
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additional information
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deletion mutant, 50-residue insert lacked consisting of residues Asp356-Ala405 including a flexible surface region
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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.
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synthesis of dihydroxyacetone phosphate, enzyme coimmobilized with catalase on oxirane activated acrylic polymer beads, Eupergit C 250