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Information on EC 1.1.1.351 - phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]
for references in articles please use BRENDA:EC1.1.1.351
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.351 phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]
IUBMB Comments
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions. Unlike EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), it is not specific for NADP+ and can accept both cofactors with similar efficiency. cf. EC 1.1.1.343, phosphogluconate dehydrogenase [NAD+-dependent, decarboxylating].
The enzyme appears in viruses and cellular organisms
showSynonyms
6-phospho-d-gluconate dehydrogenase (decarboxylating), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phospho-D-gluconate:NADP+ 2-oxidoreductase
6-phosphogluconate dehydrogenase
6-phosphogluconate dehydrogenase (NADP+/NAD+)
gnd
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-gluconate + NAD(P)+ = D-ribulose 5-phosphate + CO2 + NAD(P)H + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase (decarboxylating)
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions. Unlike EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), it is not specific for NADP+ and can accept both cofactors with similar efficiency. cf. EC 1.1.1.343, phosphogluconate dehydrogenase [NAD+-dependent, decarboxylating].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
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6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
the enzyme is active with both NAD+ and NADP+. The rate of reaction with NADP+ is 20%, of the rate with NAD+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
30-40% residual activity at 0.2 mM, the enzyme is inhibited by NADH and NADPH to a similar extend
NADPH
-
25-35% residual activity at 0.2 mM, the enzyme is inhibited by NADH and NADPH to a similar extend
ATP
-
with NAD+ as the coenzyme ATP inhibits 6-phosphogluconate dehydrogeanse activity, while with NADP+ as the coenzyme, activity is less affected
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
6-phospho-D-gluconate
-
with NADP+ as cosubstrate, in 50 mM HEPES buffer (pH 7.5), at 80°C
0.1
6-phospho-D-gluconate
-
using NADP+ as cosubstrate, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
325
6-phospho-D-gluconate
-
with NADP+ as cosubstrate, in 50 mM HEPES buffer (pH 7.5), at 80°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.023
-
using NAD+ as cosubstrate, in 50 mM Tris/HCl buffer pH 8.2, at 20°C
0.121
-
using NADP+ as cosubstrate, in 50 mM Tris/HCl buffer pH 8.2, at 20°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
the enzyme retains about 2 and 20% of its maximum activity at 30 and 60°C, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 90
-
the enzyme has half-life times of 48 and 140 h at 90 and 80°C, respectively. The enzyme retains more than 90% activity for 48 h at 60 and 80°C and retains about 50% enzymatic activity after 48 h at 90°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ben-Bassat, A.; Goldberg, I.
Purification and properties of glucose-6-phosphate dehydrogenase (NADP+/NAD+) and 6-phosphogluconate dehydrogenase (NADP+/NAD+) from methanol-grown Pseudomonas C
Biochim. Biophys. Acta
611
1-10
1980
Pseudomonas sp., Pseudomonas sp. C
brenda
Wang, Y.; Zhang, Y.H.
Overexpression and simple purification of the Thermotoga maritima 6-phosphogluconate dehydrogenase in Escherichia coli and its application for NADPH regeneration
Microb. Cell Fact.
8
30
2009
Thermotoga maritima
brenda
Stournaras, C.; Maurer, P.; Kurz, G.
6-Phospho-D-gluconate dehydrogenase from Pseudomonas fluorescens. Properties and subunit structure
Eur. J. Biochem.
130
391-396
1983
Pseudomonas fluorescens
brenda
Kiriuchin, M.; Kletsova, L.; Chistoserdov, A.; Tsygankov, Y.
Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT
FEMS Microbiol. Lett.
52
199-204
1988
Methylobacillus flagellatus
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.351)
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Release 2023.1 (January 2023)
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