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6-phospho-gluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
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-specific 6-phosphogluconate dehydrogenase
phosphogluconate dehydrogenase
-
6-PGDH
-
-
6-phosphogluconate dehydrogenase
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
-
-
-
6-phosphogluconate dehydrogenase
-
-
6-phosphogluconate dehydrogenase
-
6PGDH
-
-
EC 1.1.1.44
-
formerly
GND1
-
-
gndA
-
GNDl
-
-
gntZ
-
HVO_1830
locus name
NAD+-dependent 6-P gluconate dehydrogenase
-
NAD+-dependent 6-P gluconate dehydrogenase
-
-
NAD+-dependent 6-P-gluconate dehydrogenase
-
-
NAD+-dependent 6-P-gluconate dehydrogenase
-
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase
-
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
-
-
-
NAD-dependent PGDH
-
-
NAD-specific 6-PGDH
-
-
NAD-specific 6-PGDH
-
-
-
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
-
-
-
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
-
-
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
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
NAD-specific 6-phosphogluconate dehydrogenase
-
-
-
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6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
additional information
?
-
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
highest activity
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
the enzyme is specific for NAD+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
the enzyme is specific for NAD+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the wild type enzyme shows very low activity with NAD+, mutations at A30, R31, and T32 increase the catalytic activity with NAD+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme from the soluble fraction prefers NAD+ 8.4 times over NADP+
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
lowest activity
-
-
?
additional information
?
-
-
no NADP-dependent activity is detected
-
-
?
additional information
?
-
-
no NADP-dependent activity is detected
-
-
?
additional information
?
-
-
no NADP-dependent activity is detected
-
-
?
additional information
?
-
-
no NADP-dependent activity is detected
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
?
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6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
the wild type enzyme shows very low activity with NAD+, mutations at A30, R31, and T32 increase the catalytic activity with NAD+
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
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0.021 - 0.934
6-phospho-D-gluconate
0.021
6-phospho-D-gluconate
pH 7.5, 42°C
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
4
NAD+
mutant enzyme N32D, in 100 mM HEPES (pH 7.5), at 70°C
4.3
NAD+
wild type enzyme, 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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0.97 - 23
6-phospho-D-gluconate
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
23.3
NAD+
wild type enzyme, in 100 mM HEPES (pH 7.5), at 70°C
25.4
NAD+
mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C
29.3
NAD+
mutant enzyme N32D, 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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3.9 - 54.5
6-phospho-D-gluconate
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
5.4
NAD+
wild type enzyme, in 100 mM HEPES (pH 7.5), at 70°C
7.3
NAD+
mutant enzyme N32D, 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
9
NAD+
wild type enzyme, in 100 mM HEPES (pH 7.5), at 50°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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malfunction
gntZ mutants exhibit no detectable phenotype on glucose
malfunction
gntZ mutants grow normally on glucose
malfunction
compared to the wild type, the deletion mutant strain DELTAgndA does not grow, but growth is fully recovered by in-trans complementation with gndA. Growth of the deletion mutant can also be recovered by the addition of uridine to the medium, suggesting that Haloferax volcanii can circumvent the metabolic block for pentose phosphate formation via the oxidative pentose phosphate pathway by converting uridine to ribose-5-phosphate, catalyzed by uridine phosphorylase and phosphopentomutase
malfunction
-
gntZ mutants grow normally on glucose
-
malfunction
-
gntZ mutants exhibit no detectable phenotype on glucose
-
malfunction
-
compared to the wild type, the deletion mutant strain DELTAgndA does not grow, but growth is fully recovered by in-trans complementation with gndA. Growth of the deletion mutant can also be recovered by the addition of uridine to the medium, suggesting that Haloferax volcanii can circumvent the metabolic block for pentose phosphate formation via the oxidative pentose phosphate pathway by converting uridine to ribose-5-phosphate, catalyzed by uridine phosphorylase and phosphopentomutase
-
metabolism
-
the enzyme commits hexoses to the pentose phosphate pathway
metabolism
-
the enzyme commits hexoses to the pentose phosphate pathway
metabolism
-
the enzyme commits hexoses to the pentose phosphate pathway
-
metabolism
-
the enzyme commits hexoses to the pentose phosphate pathway
-
physiological function
GntZ does not contribute to pentose phosphate pathway fluxes during growth on glucose
physiological function
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
physiological function
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
physiological function
-
GntZ does not contribute to pentose phosphate pathway fluxes during growth on glucose
-
physiological function
-
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
-
physiological function
-
the enzyme catalyzes an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Zamboni, N.; Fischer, E.; Laudert, D.; Aymerich, S.; Hohmann, H.P.; Sauer, U.
The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway
J. Bacteriol.
186
4528-4534
2004
Bacillus subtilis, Bacillus subtilis (P12013), Bacillus subtilis 168, Bacillus subtilis 168 (P12013)
brenda
Sawada, K.; Taki, A.; Yamakawa, T.; Seki, M.
Key role for transketolase activity in erythritol production by Trichosporonoides megachiliensis SN-G42
J. Biosci. Bioeng.
108
385-390
2009
Moniliella megachiliensis, Moniliella megachiliensis SN-G42
brenda
Ohara, H.; Russell, R.A.; Uchida, K.; Kondo, H.
Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54
J. Biosci. Bioeng.
98
126-128
2004
Leuconostoc lactis, Leuconostoc lactis SHO-54
brenda
Rauch, B.; Pahlke, J.; Schweiger, P.; Deppenmeier, U.
Characterization of enzymes involved in the central metabolism of Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
88
711-718
2010
Gluconobacter oxydans (G5EBD7)
brenda
Ohara, H.; Uchida, K.; Yahata, M.; Kondo, H.
NAD-specific 6-phosphogluconate dehydrogenase in lactic acid bacteria
Biosci. Biotechnol. Biochem.
60
692-693
1996
Levilactobacillus brevis, Weissella viridescens, Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. dextranicum, Leuconostoc lactis, Weissella paramesenteroides, Leuconostoc mesenteroides subsp. mesenteroides, no activity in Streptococcus uberis strain SHO-22, no activity in Streptococcus gallinarum strain SHO-31, no activity in Streptococcus equinus strain SHO-50, no activity in Streptococcus faecium strain SHO-55, no activity in Streptococcus faecium strain SHO-57, no activity in Streptococcus faecium strain SHO-59, no activity in Lactobacillus salivarius strain SHO-69, Leuconostoc sp., Weissella viridescens SHO-94, Leuconostoc mesenteroides subsp. mesenteroides SHO-93, Leuconostoc lactis NRIC 1540, Leuconostoc sp. SHO-54, Leuconostoc mesenteroides subsp. cremoris SHO-90, Leuconostoc mesenteroides subsp. dextranicum NRIC 1539, Leuconostoc sp. SHO-47, Weissella paramesenteroides SHO-89, Levilactobacillus brevis SHO-82
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Kiriuchin, M.; Kletsova, L.; Chistoserdov, A.; Tsygankov, Y.
Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT
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1988
Methylobacillus flagellatus, Methylobacillus flagellatus KT1
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Sauerstein, J.; Jacob, J.; Reuter, G.
Demonstration of an NAD-dependent 6-phosphogluconate dehydrogenase in Pseudomonas syringae pv. phaseolicola
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Pseudomonas savastanoi pv. phaseolicola
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Chistoserdova, L.; Gomelsky, L.; Vorholt, J.A.; Gomelsky, M.; Tsygankov, Y.D.; Lidstrom, M.E.
Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph
Microbiology
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Methylobacillus flagellatus
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Sosa-Saavedra, F.; Len-Barrios, M.; Perez-Galdona, R.
Pentose phosphate pathway as the main route for hexose catabolism in bradyrhizobium sp. lacking Entner-Doudoroff pathway. A role for NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating)
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Bradyrhizobium japonicum, Bradyrhizobium sp., Bradyrhizobium japonicum USDA 110, Bradyrhizobium sp. BGA-1
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Ohara, H.; Yahata, M.; Uchida, K.; Kondo, H.
Identification and growth of Leuconostoc lactis SHO-54, producing high amounts of NAD-specific 6-phosphogluconate dehydrogenase.
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1998
Leuconostoc lactis, Leuconostoc lactis SHO-54
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Pickl, A.; Schnheit, P.
The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase - The archaeal Zwischenferment
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2015
Haloferax volcanii (D4GST8), Haloferax volcanii DSM 3757 (D4GST8)
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Papapetridis, I.; van Dijk, M.; Dobbe, A.P.; Metz, B.; Pronk, J.T.; van Maris, A.J.
Improving ethanol yield in acetate-reducing Saccharomyces cerevisiae by cofactor engineering of 6-phosphogluconate dehydrogenase and deletion of ALD6
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Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
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Huang, R.; Chen, H.; Zhong, C.; Kim, J.E.; Zhang, Y.H.
High-throughput screening of coenzyme preference change of thermophilic 6-phosphogluconate dehydrogenase from NADP+ to NAD+
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Moorella thermoacetica (A0A1J5NX54)
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Chen, H.; Zhu, Z.; Huang, R.; Zhang, Y.P.
Coenzyme engineering of a hyperthermophilic 6-phosphogluconate dehydrogenase from NADP+ to NAD+ with its application to biobatteries
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36311
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Thermotoga maritima (Q9WYR9)
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Sarmiento-Pavia, P.D.; Rodriguez-Hernandez, A.; Rodriguez-Romero, A.; Sosa-Torres, M.E.
The structure of a novel membrane-associated 6-phosphogluconate dehydrogenase from Gluconacetobacter diazotrophicus (Gd6PGD) reveals a subfamily of short-chain 6PGDs
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2021
Gluconacetobacter diazotrophicus (A9H324), Gluconacetobacter diazotrophicus ATCC 49037 (A9H324)
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