Information on EC 1.1.5.3 - glycerol-3-phosphate dehydrogenase

for references in articles please use BRENDA:EC1.1.5.3
Word Map on EC 1.1.5.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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
glycerol degradation I
-
-
glycerol-3-phosphate shuttle
-
-
glycerol-3-phosphate to cytochrome bo oxidase electron transfer
-
-
glycerol-3-phosphate to fumarate electron transfer
-
-
glycerol-3-phosphate to hydrogen peroxide electron transport
-
-
glycerophosphodiester degradation
-
-
nitrate reduction IX (dissimilatory)
-
-
nitrate reduction X (dissimilatory, periplasmic)
-
-
degradation of sugar alcohols
-
-
Glycerophospholipid metabolism
-
-
Biosynthesis of secondary metabolites
-
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme is a very important enzyme of intermediary metabolism and as a component of glycerophosphate shuttle it functions at the crossroads of glycolysis, oxidative phosphorylation and fatty acid 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
DL-glycerol 3-phosphate + oxidized 2,6-dichlorophenolindophenol
dihydroxyacetone phosphate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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
?
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 + a quinone
glycerone phosphate + a quinol
show the reaction diagram
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
sn-glycerol 3-phosphate + coenzyme Q0
dihydroxyacetone phosphate + reduced coenzyme Q0
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
dihydroxyacetone 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 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
?
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 + ubiquinone
glycerone phosphate + ubiquinol
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 + a quinone
glycerone phosphate + a quinol
show the reaction diagram
sn-glycerol 3-phosphate + acceptor
glycerone phosphate + reduced acceptor
show the reaction diagram
sn-glycerol 3-phosphate + coenzyme Q0
dihydroxyacetone phosphate + reduced coenzyme Q0
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + coenzyme Q1
dihydroxyacetone 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 + oxidized coenzyme Q
glycerone phosphate + reduced coenzyme Q
show the reaction diagram
sn-glycerol 3-phosphate + ubiquinone
glycerone phosphate + ubiquinol
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
ubiquinone
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
activates
K+
-
20 mM NaCl or KCl required for maximal activity
Mg2+
-
activates
Mn2+
-
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
-
-
2,2-dimethyl-5-nitro-2H-benzimidazole
-
-
2-[(7-nitro-3-oxo-2,1,3l5-benzoxadiazol-4-yl)oxy]phenol
-
-
2-[(E)-(4-hydroxyphenyl)diazenyl]-1-benzothiophene-3-ol
-
-
4-(4-chloroanilino)-4-oxobutanoic acid
4-(4-methylanilino)-4-oxobutanoic acid
4-(hexylamino)-4-oxobutanoic acid
4-[3-(1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-(1,3-benzothiazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-(1,3-benzoxazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-(1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-(1H-naphtho[2,3-d]imidazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-(5-methyl-1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
4-[4-[5-(3-carboxypropanamido)-1H-benzimidazol-2-yl]anilino]-4-oxobutanoic acid
4-[4-[5-(cyclohexa-2,4-diene-1-carbonyl)-1H-benzimidazol-2-yl]anilino]-4-oxobutanoic acid
5-[(E)-(3-chlorophenyl)diazenyl]-2-hydroxybenzaldehyde
-
-
6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol
-
-
adriamycin
-
significant inhibition of reaction with hydrophobic electron acceptors, coenzyme Q or vitamin K3
alpha-tocopheryl succinate
bathophenanthroline
-
-
Cetylpyridinium bromide
-
-
Chloroquine
-
inhibits reaction with coenzyme Q1, no inhibition of the reaction with 2,6-dichloroindophenol
cisplatin
-
-
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-glyceraldehyde 3-phosphate
-
-
D-glycerol phosphate
-
-
-
D-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
-
-
ethyl 4-(3-oxo-1,2-thiazol-2(3H)-yl)benzoate
-
-
FMN
-
reaction with methylene blue
glyceraldehyde 3-phosphate
glycerone phosphate
K3PO4
-
non-competitive
L-Glyceraldehyde 3-phosphate
-
-
m-Chlorohydroxamate
-
-
methyl 4-(4-methylanilino)-4-oxobutanoate
metronidazole
-
-
N-(3,5-dibromo-4-hydroxyphenyl)-4-methylbenzene-1-sulfonamide
-
-
N-[4-(1H-naphtho[2,3-d]imidazol-2-yl)phenyl]butanamide
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]-2-oxopropanamide
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]-3-methylbutanamide
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]-4-ethoxybenzamide
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]cyclopropanecarboxamide
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]furan-2-carboxamide
palmitoyl-CoA
-
-
phosphoenolpyruvate
-
-
Phosphoglycolic acid
-
-
Salicylhydroxamate
-
-
Thenoyltrifluoroacetone
-
-
Triton X100
additional information
-
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
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0095
4-[4-(1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
-
pH not specified in the publication, 37C
0.0007
4-[4-(1H-naphtho[2,3-d]imidazol-2-yl)anilino]-4-oxobutanoic acid
-
pH not specified in the publication, 37C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
4-[3-(1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.015
4-[4-(1,3-benzothiazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.02
4-[4-(1,3-benzoxazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.0063 - 0.008
4-[4-(1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.0007 - 0.001
4-[4-(1H-naphtho[2,3-d]imidazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.005
4-[4-(5-methyl-1H-benzimidazol-2-yl)anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.003
4-[4-[5-(cyclohexa-2,4-diene-1-carbonyl)-1H-benzimidazol-2-yl]anilino]-4-oxobutanoic acid
Mus musculus
-
pH not specified in the publication, 37C
0.0006
6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol
Giardia intestinalis
-
at pH 7.5 and 25C
0.0019
metronidazole
Giardia intestinalis
-
at pH 7.5 and 25C
0.08
N-[4-(5,6-dihydro-1H-benzimidazol-2-yl)phenyl]furan-2-carboxamide
Mus musculus
-
pH not specified in the publication, 37C
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
35000
-
2 * 35000, SDS-PAGE
43000
-
1 * 43000 + 1 * 62000, SDS-PAGE
58000
-
2 * 58000, SDS-PAGE
62000
-
1 * 43000 + 1 * 62000, SDS-PAGE
68000
-
x * 68000, SDS-PAGE
75000
-
x * 75000, SDS-PAGE
93500
-
equilibrium sedimentation
120000
-
x * 120000, SDS-PAGE
130000
-
gel filtration
300000
-
gel filtration
520000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 74000, calculated from amino acid sequence
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
ubiquitination
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
-
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)
-
nickel resin column chromatography
-
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
-
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by ethanol
-
Show AA Sequence (15313 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.