User menu

The multifunctional isopropyl alcohol dehydrogenase of Phytomonas sp. could be the result of a horizontal gene transfer from a bacterium to the trypanosomatid lineage.

Bibliographic reference Molinas, Sara M ; Altabe, Silvia G ; Opperdoes, Frederik ; Rider, Mark ; Michels, Paulus ; et. al. The multifunctional isopropyl alcohol dehydrogenase of Phytomonas sp. could be the result of a horizontal gene transfer from a bacterium to the trypanosomatid lineage.. In: The Journal of biological chemistry, Vol. 278, no. 38, p. 36169-75 (2003)
Permanent URL
  1. C. R. Acad. Sci. (Paris), 295, 547 (1982)
  2. Reid Matthew F., Fewson Charles A., Molecular Characterization of Microbial Alcohol Dehydrogenases, 10.3109/10408419409113545
  3. Bradford Marion M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, 10.1016/0003-2697(76)90527-3
  4. Chua Nam-Hai, [40] Electrophoretic analysis of chloroplast proteins, Methods in Enzymology (1980) ISBN:9780121819699 p.434-446, 10.1016/s0076-6879(80)69042-9
  5. Rider Mark H., Puype Magda, Damme Jozef, Gevaert Kris, Boeck Stefan, D'Alayer Jacques, Rasmussen Hanna H., Celis Julio E., Vandekerckhove Joel, An Agarose-Based Gel-Concentration System for Microsequence and Mass Spectrometric Characterization of Proteins Previously Purified in Polyacrylamide Gels Starting at Low Picomole Levels, 10.1111/j.1432-1033.1995.0258i.x
  6. Anal. Chem., 68, 1 (1996)
  7. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
  8. Thompson Julie D., Higgins Desmond G., Gibson Toby J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, 10.1093/nar/22.22.4673
  9. Kimura Motoo, A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences, 10.1007/bf01731581
  10. Felsenstein, J. (1993) PHYLIP (Phylogeny Inference Package), Version 3.5c, Department of Genetics, University of Washington, Seattle
  11. Strimmer K., von Haeseler A., Quartet Puzzling: A Quartet Maximum-Likelihood Method for Reconstructing Tree Topologies, 10.1093/oxfordjournals.molbev.a025664
  12. ALLERT Sylvie, ERNEST Isabelle, POLISZCZAK Annick, OPPERDOES Fred R., MICHELS Paul A. M., Molecular cloning and analysis of two tandemly linked genes for pyruvate kinase of Trypanosoma brucei, 10.1111/j.1432-1033.1991.tb21043.x
  13. Persson Bengt, Zigler J. Samuel, Jornvall Hans, A Super-Family of Medium-Chain Dehydrogenases/Reductases (MDR). Sub-Lines including zeta-Crystallin, Alcohol and Polyol Dehydrogenases, Quinone Oxidoreductases, Enoyl Reductases, VAT-1 and other Proteins, 10.1111/j.1432-1033.1994.tb20021.x
  14. Ferreyra R G, Soncini F C, Viale A M, Cloning, characterization, and functional expression in Escherichia coli of chaperonin (groESL) genes from the phototrophic sulfur bacterium Chromatium vinosum., 10.1128/jb.175.5.1514-1523.1993
  15. Brändén Carl-Ivar, Jürnvall Hans, Eklund Hans, Furugren Bo, 3 Alcohol Dehydrogenases, The Enzymes (1975) ISBN:9780121227111 p.103-190, 10.1016/s1874-6047(08)60211-5
  16. Eur. J. Cell Biol., 73, 240 (1997)
  17. Arch. Sci. Biol. (Bologna), 24, 73 (1938)
  18. Korkhin Yakov, Kalb(Gilboa) A.Joseph, Peretz Moshe, Bogin Oren, Burstein Yigal, Frolow Felix, NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii 1 1Edited by R. Huber, 10.1006/jmbi.1998.1750
  19. Uttaro Antonio D, Sanchez-Moreno Manuel, Opperdoes Fred R, Genus-specific biochemical markers for Phytomonas spp., 10.1016/s0166-6851(97)00142-4
  20. SANCHEZMORENO M, LASZTITY D, COPPENS I, OPPERDOES F, Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias, 10.1016/0166-6851(92)90111-v
  21. Maslov Dmitri A., Nawathean Pipat, Scheel John, Partial kinetoplast-mitochondrial gene organization and expression in the respiratory deficient plant trypanosomatid Phytomonas serpens, 10.1016/s0166-6851(99)00028-6
  22. Chaumont Francois, Schanck AndréN., Blum J.Joseph, Opperdoes Fred R., Aerobic and anaerobic glucose metabolism of Phytomonas sp. isolated from Euphorbia characias, 10.1016/0166-6851(94)00141-3
  23. Van Hellemond J. J., Opperdoes F. R., Tielens A. G. M., Trypanosomatidae produce acetate via a mitochondrial acetate:succinate CoA transferase, 10.1073/pnas.95.6.3036
  24. Duester Gregg, Farrés Jaume, Felder Michael R, Holmes Roger S, Höög Jan-Olov, Parés Xavier, Plapp Bryce V, Yin Shih-Jiun, Jörnvall Hans, Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family, 10.1016/s0006-2952(99)00065-9
  25. Opperdoes F R, Compartmentation of Carbohydrate Metabolism in Trypanosomes, 10.1146/annurev.mi.41.100187.001015
  26. Stryer, L. (1995) Biochemistry (Freeman, W. H., ed) 4th Ed., New York, NY
  27. Shafqat J., El-Ahmad M., Danielsson O., Martinez M. C., Persson B., Pares X., Jornvall H., Pea formaldehyde-active class III alcohol dehydrogenase: common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P)., 10.1073/pnas.93.11.5595
  28. STEINBUCHEL Alexander, SCHLEGEL Hans G., A multifunctional fermentative alcohol dehydrogenase from the strict aerobe Alcaligenes eutrophus: purification and properties, 10.1111/j.1432-1033.1984.tb08229.x
  29. KEEGAN FRANK P., BLUM J. JOSEPH, The NADP-linked Aldehyde Reductase of Leishmania donovani, 10.1111/j.1550-7408.1995.tb01575.x
  30. Arauzo S, The NADP-linked aldehyde reductase from Trypanosoma cruzi subcellular localization and some properties, 10.1016/0378-1097(89)90054-2
  31. Comp. Biochem. Physiol., 81, 1019 (1985)
  32. Uttaro Antonio D., Opperdoes Fred R., Purification and characterisation of a novel iso-propanol dehydrogenase from Phytomonas sp., 10.1016/s0166-6851(97)02830-2