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Information on EC 1.1.1.44 - phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38720

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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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Saccharomyces cerevisiae
UNIPROT: P38720
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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-phosphogluconate dehydrogenase Gnd1
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6-phospho-D-gluconate dehydrogenase
-
-
-
-
6-phosphogluconate dehydrogenase
6-phosphogluconate dehydrogenase (decarboxylating)
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-
-
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6-phosphogluconic carboxylase
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-
-
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6-phosphogluconic dehydrogenase
-
-
-
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GNTZII
-
-
-
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phosphogluconic acid dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
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-
-
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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
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0509
6-phospho-D-gluconate
pH 7.5
0.068 - 3.13
6-phosphogluconate
0.025 - 0.033
NADP+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
disruption of glucose-6-phosphate dehydrogenase (ZWF1), 6-phosphogluconate dehydrogenase GND1 and 6-phosphogluconate dehydrogenase GND2 genes can decrease the ability of yeast cells to reproduction in the exponential phase of culture
physiological function
the enzyme is responsible for NADPH formation in the pentose phosphate pathway
physiological function
the enzyme is responsible for NADPH formation in the pentose phosphate pathway
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method at 15°C, crystal structure of 6-phosphogluconate dehydrogenase determined at 2.37 Å resolution by molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
both of the soluble and immobilized enzyme have the maximum thermal stability at 30°C
40
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1 h, immobilized enzyme loses 84% of its initial activity, soluble enzyme loses 89% of its initial activity
50
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1 h, immobilized enzyme loses 92% of its initial activity, soluble enzyme loses 97% of its initial activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme immobilized on 2-aminoethyl-3-aminopropyltriethoxysilane modified core-shell Fe3O4SiO2 magnetic nanoparticles maintains 62% of its initial activity after five cycles
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thermal, and storage stability of the enzyme (6PGDH) are improved with covalent immobilization of the enzyme (6PGDH) on 2-aminoethyl-3-aminopropyltriethoxysilane modified core-shell Fe3O4SiO2 magnetic nanoparticles
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, enzyme immobilized on 2-aminoethyl-3-aminopropyltriethoxysilane modified core-shell Fe3O4SiO2 magnetic nanoparticles maintains 35% of its initial activity after 22 days of storage
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4°C, the soluble enzyme completely loses its initial activity after 15 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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immobilization of 6PDGH on ASMNPs can be an effective way for its biotechnological and biosensor applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rippa, M.; Signorini, M.; Dallocchio, F.
A multiple role for the coenzyme in the mechanism of action of 6-phosphogluconate dehydrogenase
J. Biol. Chem.
248
4920-4925
1973
Saccharomyces cerevisiae, Cyberlindnera jadinii, Sus scrofa
Manually annotated by BRENDA team
King, J.
6-Phosphogluconat-dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
668-672
1974
Saccharomyces cerevisiae, Homo sapiens
-
Manually annotated by BRENDA team
Scott, W.A.; Abramsky, T.
6-Phosphogluconate dehydrogenase from Neurospora crassa
Methods Enzymol.
41
227-231
1975
Saccharomyces cerevisiae, Neurospora crassa
Manually annotated by BRENDA team
Beitner, R.; Nordenberg, J.
Inhibition of 6-phosphogluconate dehydrogenase(decarboxylating) by glucose 1,6-bisphosphate
Biochim. Biophys. Acta
583
266-269
1979
Saccharomyces cerevisiae, Rattus norvegicus
Manually annotated by BRENDA team
Graefe, U.; Bormann, E.J.; Truckenbrodt, G.
Control by phospho-adenosinediphospho-ribose of NADP-dependent isocitrate dehydrogenase and 6-phosphogluconate dehydrogenase in Streptomyces griseus
Z. Allg. Mikrobiol.
20
607-611
1980
Saccharomyces cerevisiae, Streptomyces griseus
Manually annotated by BRENDA team
Adams, M.J.; Gover, S.; Pickersgill, R.W.; Helliwell, J.R.
Structure-function relationships of NAD+ and NADP+-dependent dehydrogenases with particular reference to the three-dimensional structure of 6-phosphogluconate dehydrogenase
Biochem. Soc. Trans.
11
429-435
1983
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Miernyk, J.A.; MacDougall, P.S.; Dennis, D.T.
In vitro inhibition of the plastid and cytosolic isozymes of 6-phosphogluconate dehydrogenase from developing endosperm of Ricinus communis by fructose 2,6-bisphosphate
Plant Physiol.
76
1093-1094
1984
Saccharomyces cerevisiae, Ricinus communis, Nicotiana tabacum, Rattus norvegicus
Manually annotated by BRENDA team
Rendina, A.R.; Hermes, J.D.; Cleland, W.W.
Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase
Biochemistry
23
6257-6262
1984
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Veronese, F.M.; Boccu, E.; Schiavon, O.; Grandi, C.; Fontana, A.
General stability of thermophilic enzymes: Studies on 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus and yeast
J. Appl. Biochem.
6
39-47
1984
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503, Saccharomyces cerevisiae
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
Kato, N.; Sahm, H.; Schutte, H.; Wagner, F.
Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii
Biochim. Biophys. Acta
566
1-11
1979
Saccharomyces cerevisiae, [Candida] boidinii, Ovis aries
Manually annotated by BRENDA team
He, W.; Wang, Y.; Liu, W.; Zhou, C.
Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1
BMC Struct. Biol.
7
38
2007
Saccharomyces cerevisiae (P38720), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kwolek-Mirek, M.; Maslanka, R.; Molon, M.
Disorders in NADPH generation via pentose phosphate pathway influence the reproductive potential of the Saccharomyces cerevisiae yeast due to changes in redox status
J. Cell. Biochem.
120
8521-8533
2019
Saccharomyces cerevisiae (P38720), Saccharomyces cerevisiae (P53319), Saccharomyces cerevisiae BY4742 (P38720), Saccharomyces cerevisiae BY4742 (P53319)
Manually annotated by BRENDA team
Sahin, S.
Stability evaluation of 6-phosphogluconate dehydrogenase immobilized on amino-functionalized magnetic nanoparticles
Prep. Biochem. Biotechnol.
49
590-596
2019
Saccharomyces cerevisiae
Manually annotated by BRENDA team