Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg2+–oxalate ternary complex of Escherichia coli PEP carboxykinase
暂无分享,去创建一个
[1] L. Delbaere,et al. Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. , 1996, Journal of molecular biology.
[2] P. Frey,et al. Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458. , 1995, Biochemistry.
[3] A G Murzin,et al. SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.
[4] H. Goldie,et al. Identification of reactive lysines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae , 1995, FEBS letters.
[5] F. Bosch,et al. Transgenic mice overexpressing phosphoenolpyruvate carboxykinase develop non-insulin-dependent diabetes mellitus. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[6] A. Lesk,et al. Structural mechanisms for domain movements in proteins. , 1994, Biochemistry.
[7] T. Traut. The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. , 1994, European journal of biochemistry.
[8] Y. Patel,et al. Phosphoenolpyruvate carboxykinase (GTP): the gene and the enzyme. , 1994, Advances in enzymology and related areas of molecular biology.
[9] H. Goldie,et al. Reactivity of cysteinyl, arginyl, and lysyl residues ofEscherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents , 1993, Journal of protein chemistry.
[10] R. Hilgenfeld,et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements , 1993, Nature.
[11] C. Sander,et al. Protein structure comparison by alignment of distance matrices. , 1993, Journal of molecular biology.
[12] R. G. Kemp,et al. Identification of reactive vicinal cysteines in Saccharomyces cerevisiae (ATP) and cytosolic rat liver (GTP) phospho enol pyruvate carboxykinases. , 1993, Biochimica et biophysica acta.
[13] S V Evans,et al. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. , 1993, Journal of molecular graphics.
[14] P. Walter,et al. A physiological role of Mn2+ in the regulation of cytosolic phosphoenolpyruvate carboxykinase from rat liver is unlikely. , 1993, The Biochemical journal.
[15] H. Goldie,et al. Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phospho enol pyruvate carboxykinases. , 1993, Biochimica et biophysica acta.
[16] A. M. Jabalquinto,et al. The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase. , 1993, Biochimica et biophysica acta.
[17] G. Schulz,et al. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. , 1992, Journal of molecular biology.
[18] R. G. Kemp,et al. ATP-dependent Saccharomyces cerevisiae phospho enol pyruvate carboxykinase: isolation and sequence of a peptide containing a highly reactive cysteine. , 1992, Biochimica et biophysica acta.
[19] T. Steitz,et al. Structure of the recA protein–ADP complex , 1992, Nature.
[20] G. Schulz,et al. Induced-fit movements in adenylate kinases. , 1990, Faraday discussions.
[21] J. Coggins,et al. Evidence for an ancestral core structure in nucleotide-binding proteins with the type A motif. , 1991, Journal of molecular biology.
[22] T. Nowak,et al. An active-site lysine in avian liver phosphoenolpyruvate carboxykinase. , 1991, Biochemistry.
[23] R. Huber,et al. Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .
[24] L. Delbaere,et al. Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12. , 1991, Journal of molecular biology.
[25] D. Wigley,et al. Crystal structure of an N-terminal fragment of the DNA gyrase B protein , 1991, Nature.
[26] V. Schramm,et al. Isotope trapping and positional isotope exchange with rat and chicken liver phosphoenolpyruvate carboxykinases. , 1991, Biochemistry.
[27] P. R. Sibbald,et al. The P-loop--a common motif in ATP- and GTP-binding proteins. , 1990, Trends in biochemical sciences.
[28] V. Schramm,et al. Mammalian and avian liver phosphoenolpyruvate carboxykinase. Alternate substrates and inhibition by analogues of oxaloacetate. , 1990, The Journal of biological chemistry.
[29] K. Cheng,et al. A histidine residue at the active site of avian liver phosphoenolpyruvate carboxykinase. , 1989, The Journal of biological chemistry.
[30] W. Kabsch,et al. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation , 1989, Nature.
[31] T. Nowak,et al. A reactive cysteine in avian liver phosphoenolpyruvate carboxykinase. , 1989, The Journal of biological chemistry.
[32] T. Higashi. The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography , 1989 .
[33] J. Seyer,et al. Cysteine 288: an essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP). , 1989, The Journal of biological chemistry.
[34] E. Cardemil,et al. The presence of functional arginine residues in phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. , 1987, Biochimica et biophysica acta.
[35] P. Frey,et al. Stereochemical course of thiophosphoryl transfer catalyzed by cytosolic phosphoenolpyruvate carboxykinase. , 1986, Biochemistry.
[36] G. Rose,et al. Turns in peptides and proteins. , 1985, Advances in protein chemistry.
[37] K F Sheu,et al. Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase. , 1984, Biochemistry.
[38] Noriyoshi Sakabe,et al. A Focusing Weissenberg Camera with Multi-Layer-Line Screens for Macromolecular Crystallography , 1983 .
[39] T. Nowak,et al. Phosphoenolpyruvate carboxykinase. Mn2+ and Mn2+ substrate complexes. , 1982, The Journal of biological chemistry.
[40] T. Nowak,et al. The role of cations in avian liver phosphoenolpyruvate carboxykinase catalysis. Activation and regulation. , 1981, The Journal of biological chemistry.
[41] T. Steitz,et al. Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 A resolution. , 1980, Journal of molecular biology.
[42] T. Steitz,et al. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. , 1980, Journal of molecular biology.
[43] W. A. Bridger,et al. The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli. , 1980, Canadian journal of biochemistry.
[44] S. French,et al. On the treatment of negative intensity observations , 1978 .
[45] V. Schramm,et al. Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions. , 1978, The Journal of biological chemistry.
[46] D. Pérahia,et al. Molecular orbital calculations on the conformation of nucleic acids and their constituents , 1973 .
[47] M. Sundaralingam,et al. Conformational analysis of the sugar ring in nucleosides and nucleotides. A new description using the concept of pseudorotation. , 1972, Journal of the American Chemical Society.
[48] M. Utter,et al. 4 Formation of Oxalacetate by CO2 Fixation on Phosphoenolpyruvate , 1972 .
[49] P. Schimmel,et al. Nanosecond relaxation processes in aqueous mononucleoside solutions. , 1971, Biochemistry.
[50] M. Lane,et al. The enzymatic carboxylation of phosphoenolpyruvate. V. Kinetic and 18-O studies on liver mitochondrial phosphoenolpyruvate carboxykinase. , 1968, The Journal of biological chemistry.
[51] B. Matthews. Solvent content of protein crystals. , 1968, Journal of molecular biology.
[52] J. Williamson. Effects of fatty acids, glucagon and anti-insulin serum on the control of gluconeogenesis and ketogenesis in rat liver. , 1967, Advances in enzyme regulation.
[53] G. N. Ramachandran,et al. Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. , 1965, Biophysical journal.