Information on EC 1.1.3.21 - glycerol-3-phosphate oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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 ACCESSION NO.
LITERATURE
sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
show the reaction diagram
mechanism
-
sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
-
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
A flavoprotein (FAD).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
SEQUENCE CODE
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 ACCESSION NO.
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
-
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
Q70GP9
GlpO is involved in production and translocation of toxic H2O2 into the host cell, causing inflammation and cell death
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
-
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
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
a minor fraction of GlpD is associated with the membrane; membrane-spanning protein
Manually annotated by BRENDA team
-
a minor fraction of GlpD is associated with the membrane; membrane-spanning protein
-
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
Streptococcus sp
Streptococcus sp
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
Q70GP9
two bands at 45000 and 90000 Da, SDS-PAGE
90000
-
Q70GP9
two bands at 45000 and 90000 Da, SDS-PAGE
123000
-
-
strain ATCC 12755, sedimentation equilibrium
131000
-
-
strain ATCC 12755, gel filtration, sucrose density centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
LITERATURE
Ers protein acts as a positive regulator of the glpKOF operon encoding glycerol-3-phosphate oxidase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
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
-
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
-
deletion mutant, 50-residue insert lacked consisting of residues Asp356-Ala405 including a flexible surface region
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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