Information on EC 1.1.1.43 - phosphogluconate 2-dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.43
-
RECOMMENDED NAME
GeneOntology No.
phosphogluconate 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucose degradation (oxidative)
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Glutathione metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Pentose phosphate pathway
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SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-82-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
Ankistrodesmus braunii
C.C.A.P 202/7C
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-
Manually annotated by BRENDA team
Ankistrodesmus braunii C.C.A.P 202/7C
C.C.A.P 202/7C
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-
Manually annotated by BRENDA team
methanol utilizing yeast
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-
Manually annotated by BRENDA team
yeast, strain pK 233
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-
Manually annotated by BRENDA team
wild-type strain 2192, mutant strains nit A and nit B
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-
Manually annotated by BRENDA team
sea urchin
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
tobacco
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-
Manually annotated by BRENDA team
strain A 3.12
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-
Manually annotated by BRENDA team
strain A 3.12
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-
Manually annotated by BRENDA team
C; W5
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-
Manually annotated by BRENDA team
C
-
-
Manually annotated by BRENDA team
W5
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-
Manually annotated by BRENDA team
castor bean
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-
Manually annotated by BRENDA team
yeast
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-
Manually annotated by BRENDA team
spinach
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-
Manually annotated by BRENDA team
sea urchin
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Zea mays x Tripsacum dactyloides
hybrid, isozyme
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
2-ketogluconate + NAD(P)H
D-gluconate + NAD(P)+
show the reaction diagram
6-phospho-2-dehydro-D-gluconate + NAD(P)H
6-phospho-D-gluconate + NAD(P)+
show the reaction diagram
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
6-phospho-D-gluconate + NADP+
6-phospho-2-dehydro-D-gluconate + NADPH + H+
show the reaction diagram
6-phosphono-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
second step of hexose monophosphate shunt, i.e. HMS
-
-
?
D-glucose-6-phosphate + NAD+
2-dehydro-6-phospho-D-glucose + NADH
show the reaction diagram
D-glucose-6-phosphate + NADP+
2-dehydro-6-phospho-D-glucose + NADPH
show the reaction diagram
-
NADP-specific enzyme, 4% of the activity with 6-phosphogluconate
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-
?
additional information
?
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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
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
6-phosphono-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
second step of hexose monophosphate shunt, i.e. HMS
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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the activity of 6PGD is stimulated after three days in the liver at a dose of 1 mg/l Cd and on the first day in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished
Mn2+
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activity increases slightly with 7.5 mM MnCl2
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30 kDa glycoprotein GF-AS
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significant decrease in enzyme activity in chronic alcohol-treated rats
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4-[(1R,2S)-1-hydroxy-2-{[2-(4-hydroxyphenyl)ethyl]amino}propyl]phenol
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non-competitive inhibition
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
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-
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
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Adenosine 5'-triphosphate
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ATP inhibits the enzyme which is active with NAD+, not the NADP+ dependent activity
dacarbazine
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non-competitive inhibition
dorzolamide
-
-
fructose 1,6-bisphosphate
Furosemide
-
non-competitive inhibition
gadopentetic acid
-
non-competitive inhibition
guanosine 5'-triphosphate
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GTP inhibits the NADP+ specific enzyme
ketotifen
-
non-competitive inhibition
meloxicam
-
non-competitive inhibition
methotrexate
-
non-competitive inhibition
metochloropramide
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non-competitive inhibition
additional information
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not inhibited by 5-(3alpha-hydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide, 5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide, 5-(3alpha,acetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide, 5-(3,7,12-trioxo-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide, and acetazolamide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose 6-phosphate
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phosphoenolpyruvate
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additional information
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nicotine activates the muscle, lungs, and testicular 6PGD enzyme activity but has no effect on heart and liver 6PGD activity, when nicotine is administered with vitamin E the increase in 6PGD enzyme activity in muscle and testicles are lower, vitamin E may favourably increase 6PGD enzyme activity in liver in nicotine treated rats, while it has negligible effects on this enzyme activity in other tissues
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38 - 0.66
2-keto-6-phospho-D-gluconate
0.014 - 2
6-phospho-D-gluconate
0.04 - 0.5
NAD+
0.013 - 0.25
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
4-[(1R,2S)-1-hydroxy-2-{[2-(4-hydroxyphenyl)ethyl]amino}propyl]phenol
-
25C, pH 8.0, non-competitive inhibition
0.0042
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
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-
0.0878
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
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-
0.01
dacarbazine
-
25C, pH 8.0, non-competitive inhibition
3.145
dorzolamide
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-
0.127
Furosemide
-
25C, pH 8.0, non-competitive inhibition
0.0734
gadopentetic acid
-
25C, pH 8.0, non-competitive inhibition
0.008
ketotifen
-
25C, pH 8.0, non-competitive inhibition
0.05
meloxicam
-
25C, pH 8.0, non-competitive inhibition
0.136
methotrexate
-
25C, pH 8.0, non-competitive inhibition
0.002
metochloropramide
-
25C, pH 8.0, non-competitive inhibition
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.66
4-[(1R,2S)-1-hydroxy-2-{[2-(4-hydroxyphenyl)ethyl]amino}propyl]phenol
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
0.00253
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
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-
0.0601
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
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-
0.01
dacarbazine
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
1.41
dorzolamide
Homo sapiens
-
-
0.125
Furosemide
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
209
gadopentetic acid
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
0.008
ketotifen
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
0.05
meloxicam
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
0.142
methotrexate
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
3.27
metochloropramide
Homo sapiens
-
25C, pH 8.0, non-competitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20.8
-
-
34
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NADP+ as cofactor
42.3
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NAD+ as cofactor
102
-
coenzyme NAD+
141
-
coenzyme NADP+
additional information
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the homogenate has a specific activity of 0.05 EU/mg, after 484fold purification the specific activity is 25 EU/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8
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coenzyme NADH
7.4
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coenzyme NADPH
7.8 - 8
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8 - 8.5
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8.5 - 9.5
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enzyme active with NAD+
8.5
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NADP-specific enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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a 6PGD gene expression pattern in ovines differing in weight is not followed by analogous changes of its enzymatic activity suggesting that other post transcription or post translation regulation is involved
Manually annotated by BRENDA team
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of pregnant and nonpregnant women, enzyme undergoes retrograde transport to the microtubule-organizing centers in neutrophils from pregnant women, can be blocked by colchicine, anterograde distribution in cells from nonpregnant women
Manually annotated by BRENDA team
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from seedlings
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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SDS-PAGE
82000
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enzyme active with NAD+, sucrose density gradient sedimentation
84000
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enzyme active with NAD+, gel filtration
92000
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PAGE
94000
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sedimention-equilibrium measurement by the meniscus-depletion method, initial protein concentration 0.2 mg/ml
95000
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gel filtration
98000
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sedimention-equilibrium measurement by the meniscus-depletion method, initial protein concentration 0.4 mg/ml
110000 - 120000
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NADP+-specific enzyme
110000
120000
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NADP+-specific enzyme, gel filtration
123000
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NADP+-specific enzyme, sucrose density gradient sedimentation
129000
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short-column equilibrium sedimentation
220000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 56000, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% glycerol stabilizes the enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C both 6-phosphogluconate dehydrogenase species obtained by treatment with ammonium sulfate retain 100% of their activity when stored for several months
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0C freezing preserves activity for several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, 2',5'-ADP Sepharose 4B affinity chromatography, and Sephadex G-200 gel filtration
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ammonium sulfate precipitation, 2,5-ADP Sepharose 4B column chromatography, and Sephadex G-25 gel filtration
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NiNTA column chromatography
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partial, electrophoretic isozyme pattern
purified 2256times in a yield of 44.22% by using ammonium sulfate precipitation and 2', 5'-ADP Sepharose 4B affinity gel. Temperature of +4C is maintained during the purification process
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information