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Gene Review

zwf  -  glucose-6-phosphate 1-dehydrogenase

Escherichia coli UTI89

 
 
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Disease relevance of zwf

 

Psychiatry related information on zwf

 

High impact information on zwf

  • Moreover, results reported here show that an increase of the AdoMet pool represses the transcription of the glucose-6-phosphate dehydrogenase gene [6].
  • Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur [6].
  • Among a large number of glucose-6-phosphate dehydrogenase (G6PD) variants associated with different severity of clinical manifestations, enzyme deficiency, and kinetic abnormalities found in humans, only one variant exhibits no measurable activity and lacks an immunologically cross-reacting material in blood cells and other tissues [7].
  • As shown earlier, LPS stimulates the gene expression of GLUT1 glucose transporter, glucose-6-phosphate dehydrogenase (G6PD), superoxide dismutases, and glutathione peroxidase in hepatic endothelial cells [8].
  • NADPH-dependent peroxidase, NADH/NADP+ transhydrogenase, and glucose-6-phosphate dehydrogenase were most strongly induced, increasing 2.5-3-fold [9].
 

Chemical compound and disease context of zwf

 

Biological context of zwf

 

Anatomical context of zwf

 

Associations of zwf with chemical compounds

  • The expression of zwf is independent of the growth rate, but is repressed in the presence of glucose [2].
  • In this paper, we show that the engineering of the pentose phosphate pathway by modulation of the zwf gene expression level partially overcomes the possible bottleneck for the supply of building blocks and reducing power synthesized through the PP pathway, that are required for plasmid replication and plasmid-encoded protein expression [21].
  • The amount of PHB increased after enforcing the genes; especially the zwf gene an increase of around 41%, due to the rise in NADPH and the depressed TCA cycle, leading to the metabolic flux of intermediates to the pathway for the biosynthesis of PHB [4].
  • Treatment with reduced dithiothreitol or glutathione led to inactivation of plastidic G6PDH, whereas the activity of the cytosolic isoenzyme was not influenced by reduction [22].
  • Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase [22].
 

Other interactions of zwf

 

Analytical, diagnostic and therapeutic context of zwf

References

  1. The unique cyanobacterial protein OpcA is an allosteric effector of glucose-6-phosphate dehydrogenase in Nostoc punctiforme ATCC 29133. Hagen, K.D., Meeks, J.C. J. Biol. Chem. (2001) [Pubmed]
  2. Molecular analysis of the Erwinia chrysanthemi region containing the kdgA and zwf genes. Hugouvieux-Cotte-Pattat, N., Robert-Baudouy, J. Mol. Microbiol. (1994) [Pubmed]
  3. Atypical genetic locus associated with the zwf gene encoding the glucose 6-phosphate dehydrogenase from Enterococcus mundtii CRL35. Saavedra, L., Sesma, F. Curr. Microbiol. (2005) [Pubmed]
  4. Amplification of the NADPH-related genes zwf and gnd for the oddball biosynthesis of PHB in an E. coli transformant harboring a cloned phbCAB operon. Lim, S.J., Jung, Y.M., Shin, H.D., Lee, Y.H. J. Biosci. Bioeng. (2002) [Pubmed]
  5. The glucose-6-phosphate dehydrogenase from Trypanosoma cruzi: Its role in the defense of the parasite against oxidative stress. Igoillo-Esteve, M., Cazzulo, J.J. Mol. Biochem. Parasitol. (2006) [Pubmed]
  6. Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur. Thomas, D., Cherest, H., Surdin-Kerjan, Y. EMBO J. (1991) [Pubmed]
  7. Molecular abnormalities of a human glucose-6-phosphate dehydrogenase variant associated with undetectable enzyme activity and immunologically cross-reacting material. Maeda, M., Constantoulakis, P., Chen, C.S., Stamatoyannopoulos, G., Yoshida, A. Am. J. Hum. Genet. (1992) [Pubmed]
  8. Endotoxin stimulates hydrogen peroxide detoxifying activity in rat hepatic endothelial cells. Spolarics, Z., Stein, D.S., Garcia, Z.C. Hepatology (1996) [Pubmed]
  9. Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III). Brumaghim, J.L., Li, Y., Henle, E., Linn, S. J. Biol. Chem. (2003) [Pubmed]
  10. Functional expression of human glucose-6-phosphate dehydrogenase in Escherichia coli. Persico, M.G., Ciccodicola, A., Martini, G., Rosner, J.L. Gene (1989) [Pubmed]
  11. Anaerobic biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli. Effects of diazenedicarboxylic acid bis(N,N'-dimethylamide) (diamide). Privalle, C.T., Fridovich, I. J. Biol. Chem. (1990) [Pubmed]
  12. Endotoxin stimulates the expression of glucose-6-phosphate dehydrogenase in Kupffer and hepatic endothelial cells. Spolarics, Z., Navarro, L. J. Leukoc. Biol. (1994) [Pubmed]
  13. Oxidative inactivation of reduced NADP-generating enzymes in E. coli: iron-dependent inactivation with affinity cleavage of NADP-isocitrate dehydrogenase. Murakami, K., Tsubouchi, R., Fukayama, M., Ogawa, T., Yoshino, M. Arch. Microbiol. (2006) [Pubmed]
  14. Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins. Li, Z., Demple, B. Mol. Microbiol. (1996) [Pubmed]
  15. Interdependence of the position and orientation of SoxS binding sites in the transcriptional activation of the class I subset of Escherichia coli superoxide-inducible promoters. Wood, T.I., Griffith, K.L., Fawcett, W.P., Jair, K.W., Schneider, T.D., Wolf, R.E. Mol. Microbiol. (1999) [Pubmed]
  16. Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli. Wu, J., Weiss, B. J. Bacteriol. (1992) [Pubmed]
  17. Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide. Fawcett, W.P., Wolf, R.E. J. Bacteriol. (1995) [Pubmed]
  18. Molecular cloning of DNA sequences complementary to rat liver glucose-6-phosphate dehydrogenase mRNA. Nutritional regulation of mRNA levels. Kletzien, R.F., Prostko, C.R., Stumpo, D.J., McClung, J.K., Dreher, K.L. J. Biol. Chem. (1985) [Pubmed]
  19. Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Nunoshiba, T., DeRojas-Walker, T., Tannenbaum, S.R., Demple, B. Infect. Immun. (1995) [Pubmed]
  20. Diurnal fluctuation of leukocyte G6PD activity. A possible explanation for the normal neutrophil bactericidal activity and the low incidence of pyogenic infections in patients with severe G6PD deficiency in Israel. Wolach, B., Ashkenazi, M., Grossmann, R., Gavrieli, R., Friedman, Z., Bashan, N., Roos, D. Pediatr. Res. (2004) [Pubmed]
  21. Growth-rate recovery of Escherichia coli cultures carrying a multicopy plasmid, by engineering of the pentose-phosphate pathway. Flores, S., de Anda-Herrera, R., Gosset, G., Bolívar, F.G. Biotechnol. Bioeng. (2004) [Pubmed]
  22. Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase. Wenderoth, I., Scheibe, R., von Schaewen, A. J. Biol. Chem. (1997) [Pubmed]
  23. Genetic and physical analyses of the growth rate-dependent regulation of Escherichia coli zwf expression. Rowley, D.L., Pease, A.J., Wolf, R.E. J. Bacteriol. (1991) [Pubmed]
  24. Effect of zwf gene knockout on the metabolism of Escherichia coli grown on glucose or acetate. Zhao, J., Baba, T., Mori, H., Shimizu, K. Metab. Eng. (2004) [Pubmed]
  25. Purification, characterization, and cDNA sequence of glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.). Graeve, K., von Schaewen, A., Scheibe, R. Plant J. (1994) [Pubmed]
 
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