Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
暂无分享,去创建一个
A Kihara | Y. Kai | A. Kihara | Tsuyoshi Inoue | K. Izui | T. Inoue | H. Matsumura | K. Terada | T Inoue | K Terada | K Izui | Y Kai | H Matsumura | Y Nagara | T Yoshinaga | K Tsumura | T. Yoshinaga | Y. Nagara | K. Tsumura | Yoshitaka Nagara | Kennji Tsumura | Tsuyoshi Inoue
[1] S. Yanagisawa,et al. Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo , 1988, FEBS letters.
[2] K. Izui,et al. The replacement of Lys620 by serine desensitizes Escherichia coli phosphoenolpyruvate carboxylase to the effects of the feedback inhibitors L-aspartate and L-malate. , 1997, European journal of biochemistry.
[3] N. Fujita,et al. Phosphoenolpyruvate carboxylase of Escherichia coli. Hydrophobic chromatography using specific elution with allosteric inhibitor. , 1982, Journal of biochemistry.
[4] Katsuki Hirohiko,et al. Nucleotide sequence of the phosphoenolpyruvate carboxylase gene of the cyanobacterium Anacystis nidulans , 1985 .
[5] K. Woo,et al. Site‐directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions , 1995, FEBS letters.
[6] A. Brunger. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .
[7] G J Barton,et al. ALSCRIPT: a tool to format multiple sequence alignments. , 1993, Protein engineering.
[8] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[9] E A Merritt,et al. Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.
[10] N. Fujita,et al. The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence. , 1984, Journal of biochemistry.
[11] M. D. Hatch,et al. C4 Photosynthesis: An Unlikely Process Full of Surprises , 1992 .
[12] K. Izui,et al. Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo. II. Kinetic studies with a reaction system containing physiological concentrations of ligands. , 1981, Journal of Biochemistry (Tokyo).
[13] John Alan Gerlt,et al. The structural enzymology of proton-transfer reactions , 1993 .
[14] F. Katagiri,et al. Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maize. , 1986, Nucleic acids research.
[15] K. Izui,et al. Molecular properties of phosphoenolpyruvate carboxylase of Escherichia coli W. , 1974, Journal of biochemistry.
[16] K. Izui,et al. Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate , 1990 .
[17] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[18] Nobuhisa Watanabe,et al. Weissenberg camera for macromolecules with imaging plate data collection system at the Photon Factory: Present status and future plan (invited) , 1995 .
[19] K. Izui,et al. Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase. , 1995, Journal of biochemistry.
[20] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[21] K. Izui,et al. Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction. , 1991, European journal of biochemistry.
[22] Y. Kai,et al. First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli. , 1989, Journal of molecular biology.
[23] J. Vidal,et al. PHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants. , 1996, Annual review of plant physiology and plant molecular biology.
[24] K. Woo,et al. Site‐directed mutagenesis of Flaveria trinervia phosphoenolpyruvate carboxylase: Arg450 and Arg767 are essential for catalytic activity and Lys829 affects substrate binding , 1996, FEBS letters.
[25] M. O'Leary. Phosphoenolpyruvate Carboxylase: An Enzymologist's View , 1982 .
[26] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[27] K. Izui,et al. Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions. , 1991, Journal of biochemistry.
[28] M. Utter,et al. 4 Formation of Oxalacetate by CO2 Fixation on Phosphoenolpyruvate , 1972 .
[29] K. Izui,et al. Molecular evolution of phosphoeno/pyruvate carboxylase , 1994 .
[30] Y. Ueno,et al. Regulatory phosphorylation of plant phosphoenolpyruvate carboxylase: role of a conserved basic residue upstream of the phosphorylation site , 1997, FEBS letters.
[31] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[32] K. Weber,et al. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. , 1969, The Journal of biological chemistry.