Structure-function studies of the phosphoryl-transfer enzyme: phosphoenolpyruvate carboxykinase

• Autorzy: Delbaere L T J , Sudom A.M. , Prasad L. , Leduc Y. , Goldie H.
• Języki publikacji: EN

Słowa kluczowe

EN

nucleoside triphosphate; structure; carbon dioxide; carbohydrate metabolism; nucleoside diphosphate; metal cation; phosphoenolpyruvate carboxykinase; blood glucose level; oxaloacetate; Escherichia coli; metal ion

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2003
• Tom: 08
• Numer: 2A
• Opis fizyczny: p.519-521

Twórcy

autor

Delbaere L T J

• University of Saskatchewan, Saskatoon, Saskatchewan, S7N 5E5 Canada

autor

Sudom A.M.

autor

Prasad L.

autor

Leduc Y.

autor

Goldie H.

Bibliografia

• 1. Matte, A., Goldie, H., Sweet, R.M. and Delbaere, L.T.J. Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. J. Mol. Biol. 256 (1996) 126-143.
• 2. Tari, L.W., Matte, A., Goldie, H. and Delbaere, L.T.J. Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli phosphoenolpyruvate carboxykinase. Nature Struc. Biol. 3 (1996) 355-363.
• 3. Murzin, A.G., Brenner, S.E., Hubbard, T. and Chothia, C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540.
• 4. Trapani, S., Linss, J., Goldenberg, S. Fischer, H., Craievich, A.F. and Oliva, G. Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution. J. Mol. Biol.. 313 (2001) 1059-1072.
• 5. Dunten, P., Belunis, C., Crowther, R., Hollfelder, K., Kammlott, U., Levin, W., Michel, H., Ramsey, G.B., Swain, A., Weber, D. and Wertheimer, S.J. Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J. Mol. Biol. 316 (2002) 57-264.
• 6. Márquez, J.A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russel, R.B., Hengstenberg, W. and Scheffzek, K. Structure of the full-length Hpr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: Mimicking the product/substrate of the phospho transfer reactions. Proc. Natl. Acad. Sci. USA 99 (2002) 3458-3463.
• 7. Russell, R.B., Márquez, J.A., Hengstenberg, W. and Scheffzek, K. Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP-carboxykinase: expanding the P-loop nucleotidyl transferase superfamily. FEBS Lett. 517 (2002) 1-6.
• 8. Galinier, A., Lavergne, J-P., Geourjon, C., Fieulaine, S., Nessler, S. and Jault, J.-M. A new family of phosphotransferases with a P-loop motif. J. Biol. Chem. 277 (2002) 11362-11367.
• 9. Fieulaine, S., Morera, S., Poncet, S., Mijakovic, I., Galinier, A., Janin, J., Deutscher, J. and Nessler, S. X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc. Natl. Acad. Sci. USA 99 (2002) 13437-13441.
• 10. Sudom, A.M., Walters, R., Pastushok, L., Goldie, D., Prasad, L., Delbaere, L.T.J. and Goldie, H. Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitisation by trypsin. J. Bacteriology (2003) in press.
• 11. Sudom, A.M., Prasad, L., Goldie, H. and Delbaere, L.T.J. The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF3. J. Mol. Biol. 314 (2001) 83-92.