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Information on EC 1.1.1.343 - phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
for references in articles please use BRENDA:EC1.1.1.343
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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
1.1.1.343 phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
IUBMB Comments
Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway . cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 1.1.1.343
-
1.1.1.44
- glucose-6-phosphate
-
4.1.3.8
-
5.3.1.9
-
3.1.3.11
- industry
showSynonyms
6-phospho-gluconate dehydrogenase, 6-phospho-d-gluconate:nad+ 2-oxidoreductase (decarboxylating), nad-specific 6-phosphogluconate dehydrogenase, nad+-dependent 6-p-gluconate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-PGDH
6-phosphogluconate dehydrogenase
6PGDH
EC 1.1.1.44
GND1
gndA
GNDl
gntZ
HVO_1830
NAD+-dependent 6-P gluconate dehydrogenase
NAD+-dependent 6-P-gluconate dehydrogenase
NAD+-dependent 6-phosphogluconate dehydrogenase
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
NAD-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
NAD-dependent PGDH
NAD-specific 6-PGDH
NAD-specific 6-phosphogluconate dehydrogenase
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
formaldehyde oxidation I
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SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NAD+ 2-oxidoreductase (decarboxylating)
Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway [4]. cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-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: -
?
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 + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
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: the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
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: the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
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 + 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 + 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 + 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+
Levilactobacillus brevis SHO-82
-
Substrates: -
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: highest activity
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: the enzyme is specific for NAD+
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
Substrates: the enzyme is specific for NAD+
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the wild type enzyme shows very low activity with NAD+, mutations at A30, R31, and T32 increase the catalytic activity with NAD+
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 + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Weissella paramesenteroides SHO-89
-
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: the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
Substrates: the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
Products: -
Products: -
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
Substrates: lowest activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no NADP-dependent activity is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: no NADP-dependent activity is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: no NADP-dependent activity is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: no NADP-dependent activity is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADP+
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: the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
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: the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: the wild type enzyme shows very low activity with NAD+, mutations at A30, R31, and T32 increase the catalytic activity with NAD+
Products: -
Products: -
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
NAD+
the catalytic efficiency (kcat/Km) of the enzyme for NAD+ (174/s*mM) is about 2000fold higher than for NADP+ (0.082/s*mM) defining the enzyme as NAD+ specific
NAD+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Slow-binding inhibition of 6-phosphogluconate dehydrogenase by zinc ion.
Chemical and Drug Induced Liver Injury
[Catalytic properties of 6-phosphogluconate dehydrogenase from rat liver in normal state and during toxic hepatitis]
Hypothyroidism
Changes of activity and kinetics of certain liver and heart enzymes of hypothyroid and T(3)-treated rats.
Neoplasms
Tissue glycolytic enzymes in primary breast cancer patients receiving adjuvant chemotherapy.
Seizures
The calculation of the cytoplasmic free [NADP+]/[NADPH] ratio in brain: effect of electroconvulsive seizure.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0334
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
0.44
6-phospho-D-gluconate
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
0.934
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
0.01187
NAD+
mutant enzyme A30D/R31I/T32I, in 100 mM HEPES (pH 7.5), at 50°C
0.0404
NAD+
mutant enzyme A30C/R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
0.0529
NAD+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
0.064
NAD+
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
0.103
NAD+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
0.127
NAD+
mutant enzyme A30E/R31I/T32D, in 100 mM HEPES (pH 7.5), at 50°C
0.354
NAD+
mutant enzyme R31I, in 100 mM HEPES (pH 7.5), at 50°C
0.362
NAD+
mutant enzyme R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
0.605
NAD+
mutant enzyme R31T, in 100 mM HEPES (pH 7.5), at 50°C
1.397
NAD+
wild type enzyme, in 100 mM HEPES (pH 7.5), at 50°C
2.5
NAD+
mutant enzyme N32E/R33I7T34I, in 100 mM HEPES (pH 7.5), at 70°C
3.9
NAD+
mutant enzyme N32D/R33I/T34I, in 100 mM HEPES (pH 7.5), at 70°C
7.5
NAD+
mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C
0.869
NADP+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
2.393
NADP+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
3.63
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
23
6-phospho-D-gluconate
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
2.62
NAD+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
5.75
NAD+
mutant enzyme A30D/R31I/T32I, in 100 mM HEPES (pH 7.5), at 50°C
6
NAD+
mutant enzyme A30C/R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
6.06
NAD+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
9.12
NAD+
mutant enzyme R31T, in 100 mM HEPES (pH 7.5), at 50°C
10.8
NAD+
mutant enzyme A30E/R31I/T32D, in 100 mM HEPES (pH 7.5), at 50°C
12.6
NAD+
wild type enzyme, in 100 mM HEPES (pH 7.5), at 50°C
12.94
NAD+
mutant enzyme R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
15.01
NAD+
mutant enzyme R31I, in 100 mM HEPES (pH 7.5), at 50°C
25.4
NAD+
mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C
32.2
NAD+
mutant enzyme N32D/R33I/T34I, in 100 mM HEPES (pH 7.5), at 70°C
47.9
NAD+
mutant enzyme N32E/R33I7T34I, in 100 mM HEPES (pH 7.5), at 70°C
1.74
NADP+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
2.8
NADP+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.9
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
29
6-phospho-D-gluconate
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
54.5
6-phospho-D-gluconate
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
3.4
NAD+
mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C
8.3
NAD+
mutant enzyme N32D/R33I/T34I, in 100 mM HEPES (pH 7.5), at 70°C
14.8
NAD+
mutant enzyme A30C/R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
15
NAD+
mutant enzyme R31T, in 100 mM HEPES (pH 7.5), at 50°C
19.2
NAD+
mutant enzyme N32E/R33I7T34I, in 100 mM HEPES (pH 7.5), at 70°C
35.8
NAD+
mutant enzyme R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C
42.4
NAD+
mutant enzyme R31I, in 100 mM HEPES (pH 7.5), at 50°C
49
NAD+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
59
NAD+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
85.1
NAD+
mutant enzyme A30E/R31I/T32D, in 100 mM HEPES (pH 7.5), at 50°C
484.2
NAD+
mutant enzyme A30D/R31I/T32I, in 100 mM HEPES (pH 7.5), at 50°C
1.2
NADP+
pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme
2
NADP+
pH 7.5, temperature not specified in the publication, membrane-purified enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
0.2
-
using NADP+ as cosubstrate, pH and temperature not specified in the publication
4
-
using NAD+ as cosubstrate, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
