User menu

NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase.

Bibliographic reference Miclet, E ; Stoven, V ; Michels, Paulus ; Opperdoes, Frederik ; Lallemand, J Y ; et. al. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase.. In: The Journal of biological chemistry, Vol. 276, no. 37, p. 34840-6 (2001)
Permanent URL
  1. Baca Arthur M., Hol Wim G.J., Overcoming codon bias: A method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli, 10.1016/s0020-7519(00)00019-9
  2. Mehta Atul, Mason Philip J., Vulliamy Tom J., Glucose-6-phosphate dehydrogenase deficiency, 10.1053/beha.1999.0055
  3. Lauriere M., A Semidry Electroblotting System Efficiently Transfers Both High- and Low-Molecular-Weight Proteins Separated by SDS-PAGE, 10.1006/abio.1993.1313
  4. Pons Jean-Luc, Malliavin Th�r�seE., Delsuc MarcA., Gifa V. 4: A complete package for NMR data set processing, 10.1007/bf00228146
  5. Blackwell John R., Horgan Roger, A novel strategy for production of a highly expressed recombinant protein in an active form, 10.1016/0014-5793(91)81372-f
  6. Medina-Puerta, Biochem. Int., 16, 571 (1988)
  7. Breitmaier E. Voelter W. (1987) Carbon-13 NMR Spectroscopy: High-resolution Methods and Applications in Organic Chemistry and Biochemistry (VCH Publishers, Inc. Weinheim, Germany), 3rd Ed.
  8. Mathematical Biology, ISBN:0387952284, 10.1007/b98869
  9. Clarke Julia L., Scopes Deborah A., Sodeinde Olugbemiro, Mason Philip J., Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase : A novel bifunctional enzyme in malaria parasites, 10.1046/j.1432-1327.2001.02078.x
  10. Cosgrove Michael S., Gover Sheila, Naylor Claire E., Vandeputte-Rutten Lucy, Adams Margaret J., Levy H. Richard, An Examination of the Role of Asp-177 in the His-Asp Catalytic Dyad ofLeuconostoc mesenteroidesGlucose 6-Phosphate Dehydrogenase:  X-ray Structure and pH Dependence of Kinetic Parameters of the D177N Mutant Enzyme†,‡, 10.1021/bi0014608
  11. Walsh C. (1979) Enzymatic Reaction Mechanisms (W. H. Freeman Co. San Francisco, CA).
  12. Jarori Gotam K., Maitra Pabitra K., Nature of primary product(s) of D-glucose 6-phosphate dehydrogenase reaction13C and31P NMR study, 10.1016/0014-5793(91)80127-o
  13. UEBERSCHAR Karl-Heinz, BLACHNITZKY Ernst-Otto, KURZ Gerhart, Reaction Mechanism of d-Galactose Dehydrogenases from Pseudomonas saccharophila and Pseudomonas fluorescens. Formation and Rearrangement of Aldono-1,5-lactones, 10.1111/j.1432-1033.1974.tb03780.x
  14. Barton Patrick, Laws Andrew P., Page Michael I., Structure–activity relationships in the esterase-catalysed hydrolysis and transesterification of esters and lactones, 10.1039/p29940002021
  15. G. Davis Benjamin, Recent developments in glycoconjugates, 10.1039/a809773i
  16. Beránek Martin, Dršata Jaroslav, Palička Vladimír, 10.1023/a:1007280913732
  17. Swamy-Mruthinti S, Glycation decreases calmodulin binding to lens transmembrane protein, MIP, 10.1016/s0925-4439(01)00031-x
  18. Schmidt Thomas J., Helenanolide-type sesquiterpene lactones—III. Rates and stereochemistry in the reaction of helenalin and related helenanolides with sulfhydryl containing biomolecules, 10.1016/s0968-0896(97)00003-5
  19. Snyder Carroll A., Garte Seymour J., Sellakumar Arthur R., Albert Roy E., Relationships between the levels of binding to DNA and the carcinogenic potencies in rat nasal mucosa for three alkylating agents, 10.1016/0304-3835(86)90022-4
  20. Geoghegan Kieran F., Dixon Henry B.F., Rosner Philip J., Hoth Lise R., Lanzetti Anthony J., Borzilleri Kris A., Marr Eric S., Pezzullo Linda H., Martin LeRoy B., LeMotte Peter K., McColl Alexander S., Kamath Ajith V., Stroh Justin G., Spontaneous α-N-6-Phosphogluconoylation of a “His Tag” inEscherichia coli:The Cause of Extra Mass of 258 or 178 Da in Fusion Proteins, 10.1006/abio.1998.2990
  21. Kim Kristine M., Yi Eugene C., Baker David, Zhang Kam Y. J., Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase, 10.1107/s0907444901002918
  22. Kupor, J. Biol. Chem., 247, 1904 (1972)
  23. Mason Philip J., Stevens David, Diez Amalia, Knight Stuart W., Scopes Deborah A., Vulliamy Tom J., Human Hexose-6-phosphate Dehydrogenase (Glucose 1-Dehydrogenase) Encoded at 1p36: Coding Sequence and Expression, 10.1006/bcmd.1999.0224
  24. BAUER Hans Peter, SRIHARI Thota, JOCHIMS Johannes C., HOFER Hans Werner, 6-Phosphogluconolactonase. Purification, Properties and Activities in Various Tissues, 10.1111/j.1432-1033.1983.tb07442.x
  25. Collard François, Collet Jean-François, Gerin Isabelle, Veiga-da-Cunha Maria, Van Schaftingen Emile, Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway, 10.1016/s0014-5793(99)01247-8
  26. Hager P. W., Calfee M. W., Phibbs P. V., The Pseudomonas aeruginosa devB/SOL Homolog, pgl, Is a Member of the hex Regulon and Encodes 6-Phosphogluconolactonase, 10.1128/jb.182.14.3934-3941.2000
  27. Rakitzis Emmanuel T., Papandreou Photini, Reactivity of 6-phosphogluconolactone with hydroxylamine: The possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions, 10.1016/s0009-2797(98)00026-x
  28. Duffieux F., Molecular characterisation of the first two enzymes of the pentose-phosphate pathway of trypanosoma brucei, 10.1074/jbc.m004266200
  29. O'Brien Estella, Kurdi-Haidar Buran, Wanachiwanawin Wanchai, Carvajal Jose-Luis, Vulliamy Tom J., Cappadoro Marina, Mason Philip J., Luzzatto Lucio, Cloning of the glucose 6-phosphate dehydrogenase gene from Plasmodium f alciparum, 10.1016/0166-6851(94)00028-x
  30. Shahabuddin M., Rawlings D.J., Kaslow D.C., A novel glucose-6-phosphate dehydrogenase in Plasmodium falciparum, 10.1016/0167-4781(94)90269-0