Information on EC 1.1.5.3 - glycerol-3-phosphate dehydrogenase

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

EC NUMBER
COMMENTARY
1.1.5.3
-
RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
show the reaction diagram
ping-pong mechanism
-
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glycerol degradation I
-
glycerol-3-phosphate shuttle
-
glycerophosphodiester degradation
-
Glycerophospholipid metabolism
-
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol 3-phosphate:quinone oxidoreductase
This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [4]. The enzyme is activated by calcium [3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DsFAD-GPDH
Q06B39
-
FAD-dependent glycerol-3-phosphate dehydrogenase
-
-
FAD-dependent glycerol-3-phosphate dehydrogenase
Q06B39
-
FAD-glycerol phosphate dehydrogenase
P35571
-
FAD-GPDH
Q06B39
-
flavoprotein-dependent glycerol-3-phosphate dehydrogenase
-
-
flavoprotein-dependent glycerol-3-phosphate dehydrogenase
Rattus norvegicus Wistar
-
-
-
GlpO
Q3Y0N9
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase 2
Q64521
-
glycerol-3-phosphate oxidoreductase
-
-
glycerol-3-phosphate oxidoreductase
Rattus norvegicus Wistar
-
-
-
glycerophosphate dehydrogenase
P43304
mitochondrial, enzyme-bound FAD
GPD2
Q64521
-
GPDH
-
-
GPDH
Rattus norvegicus Wistar
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-49-4
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
in the absence of Gpd2, hyperactivation and acrosome reaction are significantly altered, and a few changes in protein tyrosine phosphorylation are observed during sperm capacitation. The testicular size of Gpd2-deficient animals is about 10% smaller than in wild type animals. Gpd2-null animals show a 4% reduction in tubular diameter and about 10% reduction in numbers of both spermatocytes and spermatids per seminiferous tubule
physiological function
-
GPD2 enables tyrosine phosphorylation during sperm capacitation. GPD2 activity is required for reactive oxygen species generation in mouse spermatozoa during capacitation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sn-glycerol 3-phosphate + 1-methyl-2-decyl-3,4-dimethoxybenzoquinone
glycerone phosphate + ?
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + 2,6-dichlorophenolindophenol
glycerone phosphate + reduced 2,6-dichlorophenylindophenol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + 2,6-dichlorophenolindophenol
glycerone phosphate + reduced 2,6-dichlorophenylindophenol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + 2,6-dichlorophenolindophenol
glycerone phosphate + reduced 2,6-dichlorophenylindophenol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + 2,6-dichlorophenolindophenol
glycerone phosphate + reduced 2,6-dichlorophenylindophenol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
-
key enzyme of the glycerol phosphate shuttle
-
-
?
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
-
enzyme is linked to the respiratory chain
-
-
?
sn-glycerol 3-phosphate + coenzyme Q
glycerone phosphate + red. coenzyme Q
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q0
glycerone phosphate + reduced coenzyme Q0
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q1
glycerone phosphate + reduced coenzyme Q1
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q1
glycerone phosphate + reduced coenzyme Q1
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q1
glycerone phosphate + reduced coenzyme Q1
show the reaction diagram
-
63% of the activity with 2,6-dichloroindophenol
-
-
?
sn-glycerol 3-phosphate + coenzyme Q10
glycerone phosphate + reduced coenzyme Q10
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q10
glycerone phosphate + reduced coenzyme Q10
show the reaction diagram
-
coenzyme Q10 is the only natural electron acceptor in insect flight muscles
-
-
?
sn-glycerol 3-phosphate + coenzyme Q2
glycerone phosphate + reduced coenzyme Q2
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q2
glycerone phosphate + reduced coenzyme Q2
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q5
glycerone phosphate + reduced coenzyme Q5
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q6
glycerone phosphate + reduced coenzyme Q6
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + decylubiquinone
glycerone phosphate + decylubiquinol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + duroquinone
glycerone phosphate + duroquinol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + ferricyanide
glycerone phosphate + ferrocyanide
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + ferricyanide
glycerone phosphate + ferrocyanide
show the reaction diagram
-
-
-
-
-
sn-glycerol 3-phosphate + ferricyanide
glycerone phosphate + ferrocyanide
show the reaction diagram
-
70% of the activity with 2,6-dichloroindophenol
-
-
?
sn-glycerol 3-phosphate + menadione
glycerone phosphate + reduced menadione
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + menadione
glycerone phosphate + reduced menadione
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + menadione
glycerone phosphate + reduced menadione
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + methylene blue
glycerone phosphate + reduced methylene blue
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
-
phenazine methosulfate-coupled reduction of thiazolyl blue tetrazolium
-
-
?
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
-
phenazine methosulfate coupled 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide reduction assay
-
-
?
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
-
specific for L-3-glycerophosphate
-
-
?
sn-glycerol 3-phosphate + quinone
glycerone phosphate + quinol
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + vitamin K3
glycerone phosphate + reduced vitamin K3
show the reaction diagram
-
-
-
-
?
glycerol 3-phosphate + a quinone
dihydroxyacetone phosphate + a quinol
show the reaction diagram
P43304
-
-
-
?
additional information
?
-
-
distinct binding sites on the mitochondrial L-glycerol-3-phosphate dehydrogenase for hydrophobic and hydrophilic electron acceptors in vitro
-
-
-
additional information
?
-
-
enzyme forms part of a glycerol-3-phosphate shuttle and links cytosolic glycerol-3-phosphate metabolism to carbon source utilization and energy metabolism
-
-
-
additional information
?
-
-, Q06B39
expression of DsFAD-GPDH is enhanced at first by salt treatment, and repressed by oxygen deficiency and cold stress
-
-
-
additional information
?
-
-
high susceptibility to production of reactive oxygen species by mGPDH may reflect inefficient protection of its interaction with coenzyme Q and possibly also the low Fe-S content
-
-
-
additional information
?
-
-
SDP6 is essential for glycerol catabolism
-
-
-
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
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
-
key enzyme of the glycerol phosphate shuttle
-
-
?
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
-
enzyme is linked to the respiratory chain
-
-
?
sn-glycerol 3-phosphate + coenzyme Q
glycerone phosphate + red. coenzyme Q
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q10
glycerone phosphate + reduced coenzyme Q10
show the reaction diagram
-
coenzyme Q10 is the only natural electron acceptor in insect flight muscles
-
-
?
additional information
?
-
-
enzyme forms part of a glycerol-3-phosphate shuttle and links cytosolic glycerol-3-phosphate metabolism to carbon source utilization and energy metabolism
-
-
-
additional information
?
-
-, Q06B39
expression of DsFAD-GPDH is enhanced at first by salt treatment, and repressed by oxygen deficiency and cold stress
-
-
-
additional information
?
-
-
high susceptibility to production of reactive oxygen species by mGPDH may reflect inefficient protection of its interaction with coenzyme Q and possibly also the low Fe-S content
-
-
-
additional information
?
-
-
SDP6 is essential for glycerol catabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
contains 1 mol of acid-liberatable FAD per 5500000 g of protein
FAD
-
contains noncovalently bound FAD
FAD
-
contains up to 1 nmol of FAD/mg of protein
FAD
-
contains FAD as coenzyme
FAD
-
contains FAD as coenzyme
FAD
-
contains 1 mol of noncovalently bound FAD per dimer
FAD
-
contains 0.4 mol of FAD per protein monomer of 58000 Da
FAD
Q3Y0N9
dependent on
flavin
-
contains 3.5 flavins per 5200000 Da molecular weight
FMN
-
contains 0.1 nmol of FMN /mg of protein
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
0.7 mM required for half-maximal activation of activity with 2,6-dichlorophenolindophenol in euthyroid rats, 0.002 mM required for half-maximal activation of activity with vitamin K3 in euthyroid rats. Ca2+ causes an alteration in the conformation of the enzyme
Ca2+
-
activates; causes a conformational change of both the soluble and membrane-embedded enzyme
Ca2+
-
activates
Ca2+
-
activated by Ca2+
Ca2+
-
activated by Ca2+
Ca2+
P35571
lowers KM-value for glycerol phosphate
Iron
-
contains 1 gatom of acid liberatable iron per 310000 g of protein
Iron
-
contains 1 nmol non-heme iron per mg of protein
Iron
-
contains iron
Iron
-
contains 2 mol of non-heme iron per dimer
K+
-
20 mM NaCl or KCl required for maximal activity
Mg2+
-
activates
Na+
-
20 mM NaCl or KCl required for maximal activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,2-Dihydroxybenzene 3,5-disulfonic acid
-
-
1-(2-Thenoyl)-3,3,3-trifluoroacetone
-
-
adriamycin
-
significant inhibition of reaction with hydrophobic electron acceptors, coenzyme Q or vitamin K3
bathophenanthroline
-
-
Cetylpyridinium bromide
-
-
Chloroquine
-
inhibits reaction with coenzyme Q1, no inhibition of the reaction with 2,6-dichloroindophenol
Cu2+
-
specifically inhibits phenazine methosulfate coupled 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide reduction assay
D-2-Phosphoglyceric acid
-
-
D-3-glycerophosphate
-
-
D-3-Phosphoglyceric acid
-
-
D-3-Phosphoglyceric acid
-
competitive with respect to glycerophosphate
D-3-Phosphoglyceric acid
-
-
Digitonin
-
strong inhibition, the activity is recovered to 148% of control values by the addition of exogenous synthetic analog of CoQ idebenone, i.e. hydroxydecylubiquinone, and cytochrome c. The compound also strongly activates glycerol-3-phosphate oxidation inhibited by endogenous or added free fatty acids
dihydroxyacetone phosphate
-
-
Ethacrynic acid
-
-
FMN
-
reaction with methylene blue
glyceraldehyde 3-phosphate
-
D-3-glyceraldehyde phosphate; L-3-glyceraldehyde phosphate
glyceraldehyde 3-phosphate
-
-
K3PO4
-
non-competitive
m-Chlorohydroxamate
-
-
phosphoenolpyruvate
-
-
Phosphoglycolic acid
-
-
Salicylhydroxamate
-
-
Thenoyltrifluoroacetone
-
-
Triton X100
-
in presence of phospholipids
Zn2+
-
specifically inhibits ferricyanide reduction assay
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bathocuproine
-
slight activation
cardiolipin
-
when functioning with hydrophobic electron acceptor essential in both leaflets of the membrane
Chloroform
-
slight activation
cytochrome c
-
role of cyt c in activation of glycerol-3-phosphate and succinate oxidation in frozenthawed mitochondria
Detergent
-
required for maximal activity
-
Detergent
-
detergent-depleted enzyme requires exogenous phospholipid or nondenaturing detergent for activity
-
FAD
-
stimulates the reaction with phenazine methosulfate and methylene blue. 20% increase in activity of the reaction with phenazine methosulfate with a half-maximal concentration of 200 nM
FMN
-
stimulates the reaction with phenazine methosulfate. 6fold increase in activity with a half-maximal concentration of 0.13 mM
Phospholipid
-
detergent-depleted enzyme requires exogenous phospholipid or nondenaturing detergent for activity
sodium oleate
-
activates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.076
-
2,6-dichlorophenolindophenol
-
-
0.125
-
2,6-dichlorophenolindophenol
-
-
0.125
-
coenzyme Q0
-
-
0.013
-
coenzyme Q1
-
-
0.052
-
coenzyme Q1
-
-
0.05
-
coenzyme Q10
-
-
0.023
-
Coenzyme Q2
-
-
0.11
-
coenzyme Q6
-
-
5.17
-
DL-alpha-glycerophosphate
-
-
-
0.8
-
DL-glycerol 3-phosphate
-
-
1.9
-
DL-glycerol 3-phosphate
-
with phenazine methosulfate coupled with 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide as electron acceptor
10.2
-
DL-glycerol 3-phosphate
-
with ferricyanide as electron acceptor
0.55
-
ferricyanide
-
-
0.1
-
glycerol 3-phosphate
-
in absence of exogenous FMN
0.339
-
glycerol 3-phosphate
-
in presence of exogenous FMN
0.4
-
glycerol 3-phosphate
-
enzyme from testis and pancreatic islets, in presence of saturating concentrations of free Ca2+
2.5
-
glycerol 3-phosphate
-
enzyme from pancreatic islets, in absence of free calcium
3.2
-
glycerol 3-phosphate
-
enzyme from testis in absence of free calcium
3.7
-
L-3-glycerophosphate
-
with ferricyanide as electron acceptor
4.02
-
L-3-glycerophosphate
-
with phenazine methosulfate as electron acceptor
6.2
-
L-3-glycerophosphate
-
with coenzyme Q10 as electron acceptor
0.13
-
phenazine methosulfate
-
-
10
-
L-3-glycerophosphate
-
with 2,6-dichloroindophenol, phenazine methosulfate, coenzyme Q0, coenzyme Q1, coenzyme Q2 or coenzyme Q6 as electron acceptor
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
33.3
-
glycerol 3-phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.15
-
-
-
2.9
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
7.1
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
glycerol-3-phosphate dehydrogenase protein levels and enzyme activity are highest in brown adipose tissue
Manually annotated by BRENDA team
-
very low activity
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
very low activity
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with membrane
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
inner mitochondrial membrane. The mature protein has three transmembrane helices. The first membrane-spanning region coincides with the FAD site and thus this site is placed within the membrane. The calcium-binding region lies outside the membrane exposed to the cytosolic environment
Manually annotated by BRENDA team
-
nuclear-encoded enzyme associated with the inner mitochondrial membrane
Manually annotated by BRENDA team
-
tightly bound to the outer surface of the inner mitochondrial membrane
Manually annotated by BRENDA team
-
located on the inner mitochondrial membrane
Manually annotated by BRENDA team
-
the enzyme is localized to the outer membrane of the mitochondria facing the cytoplasm
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
gel filtration
80000
-
-
SDS-PAGE
93500
-
-
equilibrium sedimentation
130000
-
-
gel filtration
300000
-
-
gel filtration
520000
-
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 75000, SDS-PAGE
?
-
x * 68000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
1 * 43000 + 1 * 62000, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
GPD2 is tyrosine phosphorylated only in capacitated spermatozoa of wild type mice
lipoprotein
-
very low phospholipid content
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
structure of a deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) is determined using multiwavelength anomalous dispersion data and refined at 2.3 A resolution
Q3Y0N9
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
unstable below
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C or 4C, concentrated to 4-10 mg/ml, stable
-
-70C, 30% ethylene glycol, stable for at least 1 month
-
3C, 30% ethylene glycol, stable for at least 4 days
-
4C, pH 6.0-8.5, 20% ethylene glycol v/v, 10% loss of activity after 60 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region)
Q3Y0N9
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) is expressed in Escherichia coli
Q3Y0N9