Information on EC 1.1.1.351 - phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.351
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RECOMMENDED NAME
GeneOntology No.
phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-gluconate + NAD(P)+ = D-ribulose 5-phosphate + CO2 + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
heterolactic fermentation
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pentose phosphate pathway
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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 + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
show the reaction diagram
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
show the reaction diagram
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-ribulose 5-phosphate
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60% residual activity at 2 mM
NADH
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30-40% residual activity at 0.2 mM, the enzyme is inhibited by NADH and NADPH to a similar extend
NADPH
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25-35% residual activity at 0.2 mM, the enzyme is inhibited by NADH and NADPH to a similar extend
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.1
6-phospho-D-gluconate
0.01 - 0.5
NAD+
0.03 - 0.38
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
325
6-phospho-D-gluconate
Thermotoga maritima
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with NADP+ as cosubstrate, in 50 mM HEPES buffer (pH 7.5), at 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.023
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using NAD+ as cosubstrate, in 50 mM Tris/HCl buffer pH 8.2, at 20C
0.07
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with NADP+ as cosubstrate, at 30C and pH 8.0
0.121
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using NADP+ as cosubstrate, in 50 mM Tris/HCl buffer pH 8.2, at 20C
0.67
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with NAD+ as cosubstrate, at 30C and pH 8.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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about 70% of enzyme activities remain at pH 6.0 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
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the enzyme retains about 2 and 20% of its maximum activity at 30 and 60C, respectively
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
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isoelectric focusing
6.5
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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4 * 31000, sedimentation equilibrium analysis
32000
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4 * 32000, SDS-PAGE
53000
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x * 53000, SDS-PAGE
115000
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catalytically active form, gel filtration
126000
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native protein, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 53000, SDS-PAGE
homotetramer
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4 * 31000, sedimentation equilibrium analysis; 4 * 32000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 90
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the enzyme has half-life times of 48 and 140 h at 90 and 80C, respectively. The enzyme retains more than 90% activity for 48 h at 60 and 80C and retains about 50% enzymatic activity after 48 h at 90C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 30 days, no loss of activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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