The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the archaeon Haloferax volcanii is specific for NAD+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Archaea, Bacteria
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SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate:NAD+ 1-oxidoreductase
The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the archaeon Haloferax volcanii is specific for NAD+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+).
Substrates: the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor Products: -
Substrates: the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor Products: -
the catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
compared to the wild type, the DELTAazf strain does not grow, but growth was fully recovered by in-trans complementation with azf. 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
compared to the wild type, the DELTAazf strain does not grow, but growth was fully recovered by in-trans complementation with azf. 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
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
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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