Histidine-phosphorylation of succinyl CoA synthetase from Trypanosoma brucei.
作者： Isabel Hunger-Glaser , Markus Linder , Thomas Seebeck
DOI: 10.1016/S0166-6851(99)00025-0
关键词: Trypanosoma brucei 、 Succinyl coenzyme A synthetase 、 Biology 、 Nucleotide 、 Nucleoside-diphosphate kinase 、 Enzyme 、 Citric acid cycle 、 Phosphorylation 、 Biochemistry 、 Histidine
摘要: The insect form of Trypanosoma brucei depends on respiration for its energy requirements. It contains a fully functional mitochondrion with complete citric acid cycle. Most enyzmes have been characterized to date. current study presents the characterization histidine phosphorylation activity one few remaining enzymes, succinyl CoA synthetase. trypanosomal enyzme was identified by partial purification, followed direct protein sequencing. is rapidly phosphorylated, presumably through auto-phosphorylation, using either ATP or GTP as phosphate donors. occurs exclusively residues. histidine-bound can be donated suitable acceptors in rapid reaction. This phosphotransfer reaction highly nucleotide selective, only ADP, but none other nucleoside-diphosphates tested, used acceptor.
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sci-hub.se 参考文章(29)
Schönenberger, R Brun, Cultivation and in vitro cloning or procyclic culture forms of Trypanosoma brucei in a semi-defined medium. Short communication Acta Tropica. ,vol. 36, pp. 289- 292 ,(1979)
Timothy M. Jenkins, Robert Eisenthal, P.David J. Weitzman, Two distinct succinate thiokinases in both bloodstream and procyclic forms of Trypanosomabrucei Biochemical and Biophysical Research Communications. ,vol. 151, pp. 257- 261 ,(1988) , 10.1016/0006-291X(88)90587-6
Ying-Fei Wei, Harry R. Matthews, Identification of phosphohistidine in proteins and purification of protein-histidine kinases. Methods in Enzymology. ,vol. 200, pp. 388- 414 ,(1991) , 10.1016/0076-6879(91)00156-Q
Two-component signal transduction ASM Press. ,(1995) , 10.1128/9781555818319
N Weigel, M A Kukuruzinska, A Nakazawa, E B Waygood, S Roseman, Sugar transport by the bacterial phosphotransferase system. Phosphoryl transfer reactions catalyzed by enzyme I of Salmonella typhimurium. Journal of Biological Chemistry. ,vol. 257, pp. 14477- 14491 ,(1982) , 10.1016/S0021-9258(19)45405-7
W.T. Wolodko, M.E. Fraser, M.N.G. James, W.A. Bridger, The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Journal of Biological Chemistry. ,vol. 269, pp. 10883- 10890 ,(1994) , 10.2210/PDB1SCU/PDB
C. Bordier, Phase separation of integral membrane proteins in Triton X-114 solution. Journal of Biological Chemistry. ,vol. 256, pp. 1604- 1607 ,(1981) , 10.1016/S0021-9258(19)69848-0
Friedemann Hesse, Paul M. Selzer, Kerstin Mühlstädt, Michael Duszenko, A novel cultivation technique for long-term maintenance of bloodstream form trypanosomes in vitro Molecular and Biochemical Parasitology. ,vol. 70, pp. 157- 166 ,(1995) , 10.1016/0166-6851(95)00027-X
A. J. Ninfa, E. G. Ninfa, A. N. Lupas, A. Stock, B. Magasanik, J. Stock, Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 85, pp. 5492- 5496 ,(1988) , 10.1073/PNAS.85.15.5492
Christine E. Clayton, Paul Michels, Metabolic compartmentation in African trypanosomes Parasitology Today. ,vol. 12, pp. 465- 471 ,(1996) , 10.1016/S0169-4758(96)10073-9