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 hide
1.1.5.3
-
RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
degradation of sugar alcohols
-
-
glycerol degradation I
-
-
glycerol-3-phosphate shuttle
-
-
glycerol-3-phosphate to cytochrome bo oxidase electron transfer
-
-
glycerol-3-phosphate to fumarate electron transfer
-
-
glycerophosphodiester degradation
-
-
Glycerophospholipid metabolism
-
-
nitrate reduction IX (dissimilatory)
-
-
nitrate reduction X (periplasmic, dissimilatory)
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-49-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Q3Y0N9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerol 3-phosphate + a quinone
dihydroxyacetone phosphate + a quinol
show the reaction diagram
-
-
-
?
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 + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
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 Q10
glycerone phosphate + reduced coenzyme Q10
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 + 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 + oxidized coenzyme Q
glycerone phosphate + reduced coenzyme Q
show the reaction diagram
sn-glycerol 3-phosphate + phenazine methosulfate
glycerone phosphate + reduced phenazine methosulfate
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
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
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
sn-glycerol 3-phosphate + coenzyme Q10
glycerone phosphate + reduced coenzyme Q10
show the reaction diagram
sn-glycerol 3-phosphate + oxidized coenzyme Q
glycerone phosphate + reduced coenzyme Q
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme Q
-
-
flavin
FMN
-
contains 0.1 nmol of FMN /mg of protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2MoO4
-
-
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
deoxycholate
-
-
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
K3PO4
-
non-competitive
m-Chlorohydroxamate
-
-
phosphoenolpyruvate
-
-
Phosphoglycolic acid
-
-
Salicylhydroxamate
-
-
Thenoyltrifluoroacetone
-
-
Triton X100
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076 - 0.125
2,6-dichlorophenolindophenol
0.125
coenzyme Q0
-
-
0.013 - 0.052
coenzyme Q1
0.05
coenzyme Q10
-
-
0.023
coenzyme Q2
-
-
0.11
coenzyme Q6
-
-
5.17
DL-alpha-glycerophosphate
-
-
0.8 - 10.2
DL-glycerol 3-phosphate
0.55
ferricyanide
-
-
0.1 - 3.2
glycerol 3-phosphate
3.7 - 10
L-3-glycerophosphate
0.13
phenazine methosulfate
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3
glycerol 3-phosphate
Escherichia coli
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.9
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
-
-
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 7.1
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
flight muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
93500
-
equilibrium sedimentation
130000
-
gel filtration
300000
-
gel filtration
520000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
-
very low phospholipid content
phosphoprotein
-
GPD2 is tyrosine phosphorylated only in capacitated spermatozoa of wild type mice
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
unstable below
287806
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
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
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
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
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