Information on EC 1.1.1.343 - phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.343
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RECOMMENDED NAME
GeneOntology No.
phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pentose phosphate pathway
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Pentose phosphate pathway
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain SN-G42 and 124A
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Manually annotated by BRENDA team
strain SN-G42 and 124A
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Manually annotated by BRENDA team
no activity in Lactobacillus salivarius strain SHO-69
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Manually annotated by BRENDA team
no activity in Streptoccus equinus strain SHO-50
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Manually annotated by BRENDA team
no activity in Streptoccus gallinarum strain SHO-31
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Manually annotated by BRENDA team
no activity in Streptoccus lactis strain SHO-53
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Manually annotated by BRENDA team
no activity in Streptoccus uberis strain SHO-22
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Manually annotated by BRENDA team
no activity in Streptococcus faecium strain SHO-55
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Manually annotated by BRENDA team
no activity in Streptococcus faecium strain SHO-57
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Manually annotated by BRENDA team
no activity in Streptococcus faecium strain SHO-59
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Manually annotated by BRENDA team
cf EC 1.1.1.44
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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
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lowest activity
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?
additional information
?
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
highest activity at about 1 M KCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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75% residual activity at 10 mM
D-ribulose 5-phosphate
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65% residual activity at 2 mM
NADH
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1% residual activity at 0.2 mM
NADPH
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25% residual activity at 0.2 mM
additional information
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not inhibited by NaF
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.44
6-phospho-D-gluconate
0.01187 - 7.5
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23
6-phospho-D-gluconate
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
5.75 - 47.9
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54.5
6-phospho-D-gluconate
in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C
3.4 - 484.2
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.089
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crude extract, at 37°C and pH 8.3
0.2
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using NADP+ as cosubstrate, pH and temperature not specified in the publication
0.67
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crude extract, at pH 8.0 and 30°C
1.5
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at pH 7.5 and 30°C
1.6
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at pH 7.5 and 30°C
1.9
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at pH 7.5 and 30°C
4.4
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at pH 7.5 and 30°C
31.16
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after 350fold purification, at 37°C and pH 8.3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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4 * 33000, SDS-PAGE
35900
4 * 35900, SDS-PAGE
37000
4 * 37000, SDS-PAGE
130000
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gel filtration
135000
native PAGE
143000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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the enzyme is stable after a treatment at 60°C for 30 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 3 days, 90% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue-Sepharose CL-6B column chromatography, DEAE-Sephacel gel filtration, and Sephadex G200 gel filtration
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ammonium sulfate precipitation, Red Sepharose column chromatography, DEAE TSK column chromatography, and TSK HW55 gel filtration
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Ni-NTA resin column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DF214 cells
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expressed in Escherichia coli TOP10 and BL21(DE3) cells
expressed in Saccharomyces cerevisiae
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homologous overexpression of the his-tagged protein in Haloferax volcanii
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A30C/R31I/T32K
the catalytic efficiency of the mutant for NAD+ is increased by about 1.6fold compared to the wild type enzyme
A30D/R31I/T32I
the catalytic efficiency of the mutant for NAD+ is increased by 54fold, with a 4278fold reversal of coenzyme selectivity from NADP+ to NAD+
A30E/R31I/T32D
the catalytic efficiency of the mutant for NAD+ is increased by about 9.5fold compared to the wild type enzyme
R31I
the catalytic efficiency of the mutant for NAD+ is increased by about 4.7fold compared to the wild type enzyme
R31I/T32G
the catalytic efficiency of the mutant for NAD+ is increased by about 4fold compared to the wild type enzyme
R31T
the catalytic efficiency of the mutant for NAD+ is increased by about 1.7fold compared to the wild type enzyme
N32D
the mutant exhibits an about 1.3fold increase of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32D/R33I/T34I
the mutant exhibits an about 1.5fold increase of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32D/R33L/T34S
the mutant exhibits an about 0.6fold decrease of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32E/R33I/T34I
the mutant exhibits an about 3.5fold increase of catalytic efficiency with NAD+ as cofactor, with about 64000fold reversal of the coenzyme selectivity from NADP+ to NAD+ compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
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