1.1.1.343: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
This is an abbreviated version!
For detailed information about phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating), go to the full flat file.
Word Map on EC 1.1.1.343
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1.1.1.343
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1.1.1.44
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glucose-6-phosphate
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4.1.3.8
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5.3.1.9
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3.1.3.11
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industry
- 1.1.1.343
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1.1.1.44
- glucose-6-phosphate
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4.1.3.8
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5.3.1.9
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3.1.3.11
- industry
Reaction
Synonyms
6-PGDH, 6-phospho-gluconate dehydrogenase, 6-phosphogluconate dehydrogenase, 6PGDH, EC 1.1.1.44, GND1, gndA, GNDl, gntZ, Gox1705, 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, phosphogluconate dehydrogenase
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General Information
General Information on EC 1.1.1.343 - phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
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malfunction
metabolism
physiological function
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
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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
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the enzyme commits hexoses to the pentose phosphate pathway
metabolism
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the enzyme commits hexoses to the pentose phosphate pathway
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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
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GntZ does not contribute to pentose phosphate pathway fluxes during growth on glucose
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physiological function
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the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
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physiological function
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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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