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
1.1.1.43
-
RECOMMENDED NAME
GeneOntology No.
phosphogluconate 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glucose degradation (oxidative)
-
Glutathione metabolism
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-keto-6-phosphogluconate reductase
-
-
-
-
6-PGADHase
-
-
6-PGDase
-
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
Tripsacum dactyloides, Zea mays, Zea mays x Tripsacum dactyloides
-
-
6-phosphogluconate dehydrogenase (NAD)
-
-
-
-
6-phosphogluconate-dehydrogenase
-
-
6-phosphogluconate-dehydrogenase
-
-
-
6-phosphogluconic dehydrogenase
-
-
-
-
6-phosphoglucuronic acid dehydrogenase
-
-
6PGDH
-
-
6PGDH
-
-
gluconate 6-phosphate dehydrogenase
-
-
-
-
phosphogluconate dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-82-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Ankistrodesmus braunii
C.C.A.P 202/7C
-
-
Manually annotated by BRENDA team
Ankistrodesmus braunii C.C.A.P 202/7C
C.C.A.P 202/7C
-
-
Manually annotated by BRENDA team
ATCC 17616, synonymous with Pseudomonas cepacia
-
-
Manually annotated by BRENDA team
methanol utilizing yeast
-
-
Manually annotated by BRENDA team
yeast, strain pK 233
-
-
Manually annotated by BRENDA team
wild-type strain 2192, mutant strains nit A and nit B
-
-
Manually annotated by BRENDA team
pregnant and nonpregnant women
-
-
Manually annotated by BRENDA team
sea urchin
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
strain A 3.12
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens A 3.12
strain A 3.12
-
-
Manually annotated by BRENDA team
Pseudomonas sp. W5
W5
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
maize, L. Pioneer HiBred International line B73
-
-
Manually annotated by BRENDA team
Zea mays x Tripsacum dactyloides
hybrid, isozyme
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
6PGD enzymes functions to protect against cadmium toxicity
physiological function
-
the enzyme contributes to bacterial pathogenesis and functions as an adhesion and protective antigen in Haemophilus parasuis infection and immunity. The protein is capable of inhibiting the capacity of Haemophilus parasuis SH0165 cells of adhesion to swine alveolar epithelial cells by 69.5% and induces release of interleukin-6 and interleukin-8 by swine alveolar epithelial cells
physiological function
-
the enzyme contributes to bacterial pathogenesis and functions as an adhesion and protective antigen in Haemophilus parasuis infection and immunity. The protein is capable of inhibiting the capacity of Haemophilus parasuis SH0165 cells of adhesion to swine alveolar epithelial cells by 69.5% and induces release of interleukin-6 and interleukin-8 by swine alveolar epithelial cells
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-ketogluconate + NAD(P)H
D-gluconate + NAD(P)+
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens A 3.12
-
-
-
-
r
6-phospho-2-dehydro-D-gluconate + NAD(P)H
6-phospho-D-gluconate + NAD(P)+
show the reaction diagram
-
-
-
-
r
6-phospho-2-dehydro-D-gluconate + NAD(P)H
6-phospho-D-gluconate + NAD(P)+
show the reaction diagram
-
-
-
r
6-phospho-2-dehydro-D-gluconate + NAD(P)H
6-phospho-D-gluconate + NAD(P)+
show the reaction diagram
-
-
-
-
r
6-phospho-2-dehydro-D-gluconate + NAD(P)H
6-phospho-D-gluconate + NAD(P)+
show the reaction diagram
Pseudomonas fluorescens A 3.12
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
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
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
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
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Zea mays x Tripsacum dactyloides, Tripsacum dactyloides
-
-
-
-
?
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Ankistrodesmus braunii, 'Chlorella' fusca
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme involved in hexose monophosphate pathway, correlated to the rate of fatty acid synthesis
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Pseudomonas fluorescens A 3.12
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Ankistrodesmus braunii C.C.A.P 202/7C
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Pseudomonas sp. W5
-
-
-
-
r
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-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 + NAD+
2-dehydro-6-phospho-D-glucose + NADH
show the reaction diagram
-
enzyme active with NAD+, 2% of the activity compared to 6-phosphogluconate when NAD+ is cofactor, no activity detected with NADP+ as cofactor
-
-
?
D-glucose-6-phosphate + NAD+
2-dehydro-6-phospho-D-glucose + NADH
show the reaction diagram
Pseudomonas sp. C, Pseudomonas sp. W5
-
-
-
-
-
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
-
-
?
additional information
?
-
-
appears to lack 6PGAD except during growth on glucose or gluconate
-
-
-
additional information
?
-
-
fructose-6-phosphate and 2-keto-3-deoxy-6-phosphogluconate are not reduced
-
-
-
additional information
?
-
-
glucose, 2-deoxyglucose, gluconate, fructose-6-phosphate, glucose-1-phosphate, fructose-1,6-diphosphate, ribulose-5-phosphate and 1,3-diphosphoglycerate are no substrates
-
-
-
additional information
?
-
-
glucose does not serve as substrate
-
-
-
additional information
?
-
Pseudomonas fluorescens A 3.12
-
fructose-6-phosphate and 2-keto-3-deoxy-6-phosphogluconate are not reduced
-
-
-
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
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Ankistrodesmus braunii, 'Chlorella' fusca
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
enzyme involved in hexose monophosphate pathway, correlated to the rate of fatty acid synthesis
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Pseudomonas fluorescens A 3.12
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
-
-
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Ankistrodesmus braunii C.C.A.P 202/7C
-
enzyme belongs to the oxidative pentose phosphate pathway
-
-
r
6-phospho-D-gluconate + NAD(P)+
6-phospho-2-dehydro-D-gluconate + NAD(P)H
show the reaction diagram
Pseudomonas sp. W5
-
-
-
-
r
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
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
dual specificity for both NAD+ and NADP+
NADP+
-
NAD+ does not substitute NADP+
NADP+
-
dual specificity for both NAD+ and NADP+
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
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
Mg2+
-
20 mM required for maximum activity
Mg2+
-
2 mM required for maximum activity
Mg2+
-
stimulated by MgCl2
Mg2+
-
activity increases slightly with 7.5 mM MgCl2
Mn2+
-
activity increases slightly with 7.5 mM MnCl2
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
30 kDa glycoprotein GF-AS
-
significant decrease in enzyme activity in chronic alcohol-treated rats
-
4-[(1R,2S)-1-hydroxy-2-{[2-(4-hydroxyphenyl)ethyl]amino}propyl]phenol
-
non-competitive inhibition
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
Adenosine 5'-triphosphate
-
ATP inhibits the enzyme which is active with NAD+, not the NADP+ dependent activity
ATP
-
NAD+-specific enzyme
ATP
-
with NAD+ as coenzyme, with NADP+ as coenzyme activity is less affected
dacarbazine
-
non-competitive inhibition
dorzolamide
-
-
fructose 1,6-bisphosphate
-
NADP+-specific enzyme
fructose 1,6-bisphosphate
-
-
Furosemide
-
non-competitive inhibition
gadopentetic acid
-
non-competitive inhibition
guanosine 5'-triphosphate
-
GTP inhibits the NADP+ specific enzyme
ketotifen
-
non-competitive inhibition
meloxicam
-
non-competitive inhibition
methotrexate
-
non-competitive inhibition
NADPH
-
inhibition is competitive with respect to NADP+
metochloropramide
-
non-competitive inhibition
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
phosphoenolpyruvate
-
-
D-glucose 6-phosphate
-
-
additional information
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.38
-
2-keto-6-phospho-D-gluconate
-
with NADPH as coenzyme
0.66
-
2-keto-6-phospho-D-gluconate
-
with NADH as coenzyme
0.014
-
6-phospho-D-gluconate
-
homogenates
0.02
-
6-phospho-D-gluconate
-
isoform specific for NADP+ and isoform active with NAD+, with NADP+ as cofactor
0.02
-
6-phospho-D-gluconate
-
-
0.04
-
6-phospho-D-gluconate
-
isoform specific for NADP+, with NADP+ as cofactor, 5 mM ATP, glucose grown bacteria; isoform specific for NADP+, with NADP+ as cofactor, glucose grown bacteria
0.094
-
6-phospho-D-gluconate
-
-
0.1
-
6-phospho-D-gluconate
-
-
0.107
-
6-phospho-D-gluconate
-
permeabilized cells
0.14
-
6-phospho-D-gluconate
-
7.5 mM MgCl2
0.15
-
6-phospho-D-gluconate
-
1 mM MnCl2
0.2
-
6-phospho-D-gluconate
-
isoform active with NAD+, NADP+ as cofactor, glucose grown bacteria
0.2
-
6-phospho-D-gluconate
-
-
0.3
-
6-phospho-D-gluconate
-
enzyme active with NAD+ or NADP+
0.32
-
6-phospho-D-gluconate
-
-
0.39
-
6-phospho-D-gluconate
-
0.01 mM NADPH
0.7
-
6-phospho-D-gluconate
-
isoform active with NAD as cofactor and isoform specific for NADP as cofactor, glucose grown bacteria
0.7
-
6-phospho-D-gluconate
-
-
1
-
6-phospho-D-gluconate
-
0.005 M GTP
2
-
6-phospho-D-gluconate
-
isoform active with NAD+ as cofactor, 5 mM ATP, glucose grown bacteria
0.04
-
NAD+
-
-
0.013
-
NADP+
-
-
0.02
-
NADP+
-
enzyme active with NAD+ and NADP+-specific enzyme
0.02
-
NADP+
-
-
0.023
-
NADP+
-
7.5 mM MgCl2
0.028
-
NADP+
-
-
0.0422
-
NADP+
-
-
0.25
-
NADP+
-
0.01 mM NADPH
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
0.0878
-
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.01
-
dacarbazine
-
25C, pH 8.0, non-competitive inhibition
3.145
-
dorzolamide
-
-
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.66
-
4-[(1R,2S)-1-hydroxy-2-{[2-(4-hydroxyphenyl)ethyl]amino}propyl]phenol
-
25C, pH 8.0, non-competitive inhibition
0.00253
-
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.0601
-
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.01
-
dacarbazine
-
25C, pH 8.0, non-competitive inhibition
1.41
-
dorzolamide
-
-
0.125
-
Furosemide
-
25C, pH 8.0, non-competitive inhibition
209
-
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
0.142
-
methotrexate
-
25C, pH 8.0, non-competitive inhibition
3.27
-
metochloropramide
-
25C, pH 8.0, non-competitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20.8
-
-
-
34
-
-
NADP+ as cofactor
42.3
-
-
NAD+ as cofactor
56.4
-
-
-
102
-
-
coenzyme NAD+
141
-
-
coenzyme NADP+
additional information
-
-
the homogenate has a specific activity of 0.05 EU/mg, after 484fold purification the specific activity is 25 EU/mg
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
8
-
coenzyme NADH
7.4
-
-
coenzyme NADPH
8
-
-
assay at
8.5
9.5
-
enzyme active with NAD+
8.5
-
-
NADP-specific enzyme
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
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
-
fertilized and unfertilized eggs
Manually annotated by BRENDA team
Zea mays x Tripsacum dactyloides
-
-
Manually annotated by BRENDA team
-
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
-
from seedlings
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55000
-
-
SDS-PAGE
82000
-
-
enzyme active with NAD+, sucrose density gradient sedimentation
84000
-
-
enzyme active with NAD+, gel filtration
92000
-
-
PAGE
94000
-
-
sedimention-equilibrium measurement by the meniscus-depletion method, initial protein concentration 0.2 mg/ml
95000
-
-
gel filtration
98000
-
-
sedimention-equilibrium measurement by the meniscus-depletion method, initial protein concentration 0.4 mg/ml
102000
-
-
-
110000
120000
-
NADP+-specific enzyme
110000
-
-
-
110000
-
-
gel filtration
120000
-
-
NADP+-specific enzyme, gel filtration
123000
-
-
NADP+-specific enzyme, sucrose density gradient sedimentation
129000
-
-
short-column equilibrium sedimentation
220000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 58000, SDS-PAGE
?
-
x * 58000, SDS-PAGE
-
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 40000, enzyme active with NAD+; 2 * 60000, enzyme specific for NADP+
dimer
-
2 * 57000
dimer
-
-
homodimer
-
2 * 56000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
Pseudomonas sp. C, Pseudomonas sp. W5
-
4 * 55000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
20% glycerol stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C both 6-phosphogluconate dehydrogenase species obtained by treatment with ammonium sulfate retain 100% of their activity when stored for several months
-
0C freezing preserves activity for several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NiNTA column chromatography
-
ammonium sulfate precipitation, 2',5'-ADP Sepharose 4B affinity chromatography, and Sephadex G-200 gel filtration
-
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
-
ammonium sulfate precipitation, 2,5-ADP Sepharose 4B column chromatography, and Sephadex G-25 gel filtration
-
partial, electrophoretic isozyme pattern
-
partial, electrophoretic isozyme pattern
Zea mays, Zea mays x Tripsacum dactyloides
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Tripsacum dactyloides, Zea mays, Zea mays x Tripsacum dactyloides
-
usage of isozymes as marker for chromosome identification and evaluation of introgression of genes in apomictic mode of reproduction of Tripsacum dactyloides into Zea mays