Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) from Zea mays

Biophysical Chemistry - Tập 92 - Trang 53-64 - 2001
Joachim Frank1, Ronald J. Clarke2, Joachim Vater3, Josef F. Holzwarth1
1Fritz-Haber-Institut, Max-Planck-Society, Faradayweg 4-6, D-14195 Berlin, Germany
2School of Chemistry, University of Sydney, Sydney, NSW 2006, Australia
3Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Franklinstr. 29, D-10587 Berlin, Germany

Tài liệu tham khảo

Janc, 1992, A kinetic investigation of phosphoenolpyruvate carboxylase from Zea mays, Biochemistry, 31, 6421, 10.1021/bi00143a009 O'Leary, 1982, Phosphoenolpyruvate carboxylase: an enzymologist's view, Annu. Rev. Plant Physiol., 33, 297, 10.1146/annurev.pp.33.060182.001501 Andreo, 1987, Higher plant phosphoenolpyruvate carboxylase, FEBS Lett., 213, 1, 10.1016/0014-5793(87)81454-0 Stiborova’, 1983, Isolation and partial characterisation of two phosphoenolpyruvate carboxylases from maize (Zea mays L.), Photosynthetica, 17, 379 Wu, 1990, Regulation of the aggregation state of maize phosphoenolpyruvate carboxylase: evidence from dynamic light-scattering measurements, Arch. Biochem. Biophys., 281, 324, 10.1016/0003-9861(90)90451-4 Iglesias, 1986, The C4 pathway of photosynthesis and its regulation, Biochem. Educ., 14, 98, 10.1016/0307-4412(86)90166-4 Hatch, 1978, Regulation of enzymes in C4 photosynthesis, Curr. Top. Cell. Regul., 14, 1, 10.1016/B978-0-12-152814-0.50005-8 Frank, 1999, Kinetics and equilibrium binding of phosphoenolpyruvate to phosphoenolpyruvate carboxylase from Zea mays, Phys. Chem. Chem. Phys., 1, 455, 10.1039/a808087i Monod, 1965, On the nature of allosteric transitions. A plausible model, J. Mol. Biol., 12, 88, 10.1016/S0022-2836(65)80285-6 Frank, 1996, Kinetics and molecular modelling of ligand binding to ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO), Ber. Bunsenges. Phys. Chem., 100, 2112, 10.1002/bbpc.19961001233 Jawali, 1990, The dimeric form of phosphoenolpyruvate carboxylase isolated from maize: physical and kinetic properties, Arch. Biochem. Biophys., 277, 61, 10.1016/0003-9861(90)90550-I Warburg, 1941, Isolierung und Kristallisation des Gärungsfermentes Enolase, Biochem. Z., 310, 384 Turner, 1968, Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates, Biochemistry, 7, 3381, 10.1021/bi00850a011 Camerman, 1969, 2-p-Toluidinyl-6-naphthalene sulfonate: relation of structure to fluorescence properties in different media, Science, 165, 493, 10.1126/science.165.3892.493 Willeford, 1990, The role of oligomerization in regulation of maize phosphoenolpyruvate carboxylase activity, Biochem. Biophys. Res. Commun., 168, 778, 10.1016/0006-291X(90)92389-H Koshland, 1966, Comparison of experimental binding data and theoretical models in proteins containing subunits, Biochemistry, 5, 365, 10.1021/bi00865a047 Bernasconi, 1976 Kirschner, 1971, Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I: Equilibrium and temperature jump studies at pH 8.5 and 40°C, J. Mol. Biol., 58, 29, 10.1016/0022-2836(71)90230-0 Kirschner, 1971, Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II: Stopped flow studies at pH 8.5 and 40°C, J. Mol. Biol., 58, 51, 10.1016/0022-2836(71)90231-2 McClure, 1967, Fluorescent probes for conformational states of proteins. III. The activation of chymotrypsinogen, Biochemistry, 6, 567, 10.1021/bi00854a026 McClure, 1966, Fluorescence probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate, a hydrophobic probe, Biochemistry, 5, 1908, 10.1021/bi00870a018 McClure, 1967, Fluorescent probes for conformational states of proteins. II. The binding of 2-p-toluidinylnaphthalene-6-sulfonate to α-chymotrypsin, Biochemistry, 6, 559, 10.1021/bi00854a025 Frank, 1998, Thermodynamics and Kinetics of sugar phosphate binding to d-ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO), J. Chem. Soc., Faraday Trans., 94, 2127, 10.1039/a802124d Utter, 1972, Formation of oxaloacetate by CO2 fixation on phosphoenolpyruvate, 6, 117 Morikawa, 1980, Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo, J. Biochem. (Tokyo), 87, 441, 10.1093/oxfordjournals.jbchem.a132764 Izui, 1981, Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo. II. Kinetic studies with a reaction system containing physiological concentrations of ligands, J. Biochem. (Tokyo), 90, 1321, 10.1093/oxfordjournals.jbchem.a133597 Tovar-Méndez, 1995, Binding of ligands to the glucose-6-phosphate allosteric site in maize-leaf phosphoenolpyruvate carboxylase, 5, 155 Mújica-Jiménez, 1998, Studies of the allosteric properties of maize leaf phosphoenolpyruvate carboxylase with the phosphoenolpyruvate analog phosphomycin as activator, Biochim. Biophys. Acta, 1386, 132, 10.1016/S0167-4838(98)00093-4 Kai, 1999, Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition, Proc. Natl. Acad. Sci. USA, 96, 823, 10.1073/pnas.96.3.823 Tovar-Mendez, 1997, Desensitization to glucose 6-phosphate of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal 5′-phosphate, Biochim. Biophys. Acta, 1337, 207, 10.1016/S0167-4838(96)00166-5