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Information on EC 1.1.1.44 - phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) and Organism(s) Escherichia coli and UniProt Accession P00350

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IUBMB Comments
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
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This record set is specific for:
Escherichia coli
UNIPROT: P00350
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
6pgd, 6-pgd, 6-p-gluconate dehydrogenase, os6pgdh1, 6-phospho-d-gluconate dehydrogenase, 6-phosphogluconate dehydrogenase (decarboxylating), llpdh, 6-gpd, p6pgdh, tm0438, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phosphogluconate dehydrogenase
-
6-phospho-D-gluconate dehydrogenase
-
-
-
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase (decarboxylating)
-
-
-
-
6-phosphogluconic carboxylase
-
-
-
-
6-phosphogluconic dehydrogenase
-
-
-
-
GNTZII
-
-
-
-
phosphogluconic acid dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating)
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
CAS REGISTRY NUMBER
COMMENTARY hide
9073-95-4
-
SUBSTRATE
PRODUCT                       
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 + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
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 + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
D-fructose 1,6-diphosphate
-
-
p-chloromercuribenzoate
-
-
Rose bengal
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
menadione
-
the enzyme shows more than 4fold increased activity at 2.5 mM menadione
tellurite
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the enzyme shows more than 4fold increased activity at 0.005 mg/ml tellurite
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093
6-phospho-D-gluconate
in 50 mM Tris-HCl buffer (pH 8.0), 20 mM MgCl2, at 25°C
0.049
NADP+
in 50 mM Tris-HCl buffer (pH 8.0), 20 mM MgCl2, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is involved in tellurite detoxification and resistance in Escherichia coli
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
?
-
x * 50000, His6-tagged enzyme, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with substrate, substrate/NADPH and glucose, sitting drop vapour diffusion method, using 0.1 M sodium citrate dihydrate buffer (pH5.4), 0.5 M ammonium acetate, 6-7% (w/v) PEG 3350, and 17-18% (w/v) PEG 4000 as a reservoir, at 18°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
stable below
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
denaturation by urea
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, in phosphate buffer pH 6.8 in presence of the reducing agent beta-mercaptoethanol enzyme remains fully active for 24 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the Y378C mutant is expressed in Escherichia coli BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fontana, A.; Grandi, C.; Boccu, E.; Veronese, F.M.
Comparative thermostability of thermophilic and mesophilic 6-phosphogluconate dehydrogenase
Hoppe-Seyler's Z. Physiol. Chem.
356
1191-1193
1975
Geobacillus stearothermophilus, Escherichia coli, Geobacillus stearothermophilus NCA 1503
Manually annotated by BRENDA team
Veronese, F.M.; Boccu, E.; Fontana, A.
Denaturation of thermophilic and mesophilic 6-phosphogluconate dehydrogenase by 8 M urea
Int. J. Pept. Protein Res.
7
341-343
1975
Escherichia coli, Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
Manually annotated by BRENDA team
Betts, S.A.; Mayer, R.J.
Purification and properties of 6-phosphogluconate dehydrogenase from rabbit mammary gland
Biochem. J.
151
263-270
1975
Cyberlindnera jadinii, Oryctolagus cuniculus, Escherichia coli, Ovis aries, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Veronese, F.M.; Boccu, E.; Fontana, A.
Isolation and properties of 6-phosphogluconate dehydrogenase from Escherichia coli. Some Comparisons with the thermophilic enzyme from Bacillus stearothermophilus
Biochemistry
15
4026-4033
1976
Cyberlindnera jadinii, Enterococcus faecalis, Escherichia coli, Escherichia coli MRE 600, Geobacillus stearothermophilus, Neurospora crassa
Manually annotated by BRENDA team
Orozco de Silva, A.; Fraenkel, D.G.
The 6-phosphogluconate dehydrogenase reaction in Escherichia coli
J. Biol. Chem.
254
10237-10242
1979
Escherichia coli, Escherichia coli RW226/pLC33-5
Manually annotated by BRENDA team
Veronese, F.M.; Boccu, E.; Fontana, A.
6-Phosphogluconate dehydrogenase from Bacillus stearothermophilus
Methods Enzymol.
89
282-291
1982
Geobacillus stearothermophilus, Cyberlindnera jadinii, Escherichia coli, Geobacillus stearothermophilus NCA 1503
Manually annotated by BRENDA team
Sawa, Y.; Suzuki, K.; Ochiai, H.
Purification and characterization of 6-phosphogluconate dehydrogenase from Phormidium sp.
Agric. Biol. Chem.
49
2543-2549
1985
Geobacillus stearothermophilus, Cyberlindnera jadinii, Escherichia coli, Enterococcus faecalis, Neurospora crassa, Phormidium sp., Rattus norvegicus, Synechococcus sp., Synechococcus sp. PCC 6307, Synechococcus sp. PCC 6716
-
Manually annotated by BRENDA team
Chooback, L.; Price, N.E.; Karsten, W.E.; Nelson, J.; Sundstrom, P.; Cook, P.F.
Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liver
Protein Expr. Purif.
13
251-258
1998
Cyberlindnera jadinii, Escherichia coli, Ovis aries, Escherichia coli JM109 M15
Manually annotated by BRENDA team
Moritz, B.; Striegel, K.; de Graaf, A.A.; Sahm, H.
Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo
Eur. J. Biochem.
267
3442-3452
2000
Acer pseudoplatanus, Gluconobacter oxydans, Corynebacterium glutamicum, [Brevibacterium] flavum, Saccharomyces cerevisiae, [Candida] boidinii, Corynebacterium glutamicum ssp. flavum, Escherichia coli, Ovis aries, Pseudomonas sp., Pseudomonas sp. C
Manually annotated by BRENDA team
Chen, Y.Y.; Ko, T.P.; Chen, W.H.; Lo, L.P.; Lin, C.H.; Wang, A.H.
Conformational changes associated with cofactor/substrate binding of 6-phosphogluconate dehydrogenase from Escherichia coli and Klebsiella pneumoniae: Implications for enzyme mechanism
J. Struct. Biol.
169
25-35
2010
Escherichia coli (P00350), Klebsiella pneumoniae (Q762L5), Klebsiella pneumoniae NTUH-K2044 (Q762L5)
Manually annotated by BRENDA team
Sandoval, J.M.; Arenas, F.A.; Garcia, J.A.; Diaz-Vasquez, W.A.; Valdivia-Gonzalez, M.; Sabotier, M.; Vasquez, C.C.
Escherichia coli 6-phosphogluconate dehydrogenase aids in tellurite resistance by reducing the toxicant in a NADPH-dependent manner
Microbiol. Res.
177
22-27
2015
Escherichia coli, Escherichia coli BW25113
Manually annotated by BRENDA team