Publications

• Localization and characteristics of hexose 6-phosphate dehydrogenase (glucose dehydrogenase).

  Beutler E., Morrison M.

  J. Biol. Chem. 242:5289-5293(1967) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.

• Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum).

  Ragunathan S., Levy H.R.

  An NAD-preferring glucose 6-phosphate dehydrogenase of Acetobacter hansenii (formerly known as Acetobacter xylinum) has been purified to apparent homogeneity and kinetically characterized. The purified enzyme was stabilized by the use of glycerol, MgSO4, and 2-mercaptoethanol at pH 5.4. The molecu ... >> More

  An NAD-preferring glucose 6-phosphate dehydrogenase of Acetobacter hansenii (formerly known as Acetobacter xylinum) has been purified to apparent homogeneity and kinetically characterized. The purified enzyme was stabilized by the use of glycerol, MgSO4, and 2-mercaptoethanol at pH 5.4. The molecular weight of the enzyme, determined by nondenaturing gel filtration, is 243,000. The subunit molecular weight is 60,140 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that the native enzyme is a tetramer. At pH 5.4 the enzyme has Kms of 0.104 and 0.34 mM for NAD+ and NADP+, respectively; the Kms for glucose 6-phosphate are 0.071 and 0.089 mM, using NAD+ and NADP+, respectively; and the kcat values are 128,000 and 77,300 min-1 with NAD+ and NADP+, respectively. The Kms for NADP+ and glucose 6-phosphate are approximately 10 times higher than the corresponding Kms for the NADP-specific glucose 6-phosphate dehydrogenase in the same organism, but the kcat is also approximately 10-fold higher, so that the kcat/Km values for these two activities are nearly identical at pH 5.4. Both the NAD- and NADP-linked activities of the NAD-preferring enzyme are inhibited by ATP. The NADP-specific glucose 6-phosphate dehydrogenase is insensitive to ATP at pH 6.7 and 9.5, but at pH 5.4 ATP inhibits this enzyme. The possible roles of these two glucose 6-phosphate dehydrogenases in the metabolism of A. hansenii are discussed. << Less

  Arch Biochem Biophys 310:360-366(1994) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies.

  Olive C., Geroch M.E., Levy H.R.

  J. Biol. Chem. 246:2047-2057(1971) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.

  Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.

  The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by ... >> More

  The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate. << Less

  Biochemistry 37:2759-2767(1998) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase -- The archaeal Zwischenferment.

  Pickl A., Schoenheit P.

  The oxidative pentose phosphate pathway (OPPP), catalyzing the oxidation of glucose-6-phosphate to ribulose-5-phosphate is ubiquitous in eukarya and bacteria but has not yet been reported in archaea. In haloarchaea a putative 6-phosphogluconate dehydrogenase (6PGDH) is annotated, whereas a gene co ... >> More

  The oxidative pentose phosphate pathway (OPPP), catalyzing the oxidation of glucose-6-phosphate to ribulose-5-phosphate is ubiquitous in eukarya and bacteria but has not yet been reported in archaea. In haloarchaea a putative 6-phosphogluconate dehydrogenase (6PGDH) is annotated, whereas a gene coding for glucose-6-phosphate dehydrogenase (Glc6PDH) could not be identified. Here we report the purification and characterization of a novel type of Glc6PDH in Haloferax volcanii that is not related to bacterial and eukaryal Glc6PDHs and the encoding gene is designated as azf (archaeal zwischenferment). Further, recombinant H. volcanii 6PGDH was characterized. Deletion mutant analyses indicate that both, Glc6PDH and 6PGDH, are functionally involved in pentose phosphate formation in vivo. This is the first report on the operation of the OPPP in the domain of archaea. << Less

  FEBS Lett. 589:1105-1111(2015) [PubMed] [EuropePMC]