Reactivity of cysteinyl, arginyl, and lysyl residues ofEscherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents

[1]  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.

[2]  J. Seyer,et al.  Identification of vicinal thiols of phosphoenolpyruvate carboxykinase (GTP). , 1993, Journal of Biological Chemistry.

[3]  K. Lilley,et al.  The essentail active‐site lysines of clostridial glutamate dehydrogenase , 1992 .

[4]  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.

[5]  T. Nowak,et al.  An active-site lysine in avian liver phosphoenolpyruvate carboxykinase. , 1991, Biochemistry.

[6]  L. Delbaere,et al.  Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12. , 1991, Journal of molecular biology.

[7]  H. Goldie,et al.  Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae , 1990, Journal of bacteriology.

[8]  S. Tyagi,et al.  Inhibitors directed to binding domains in neutrophil elastase. , 1990, Biochemistry.

[9]  A. M. Jabalquinto,et al.  Reactive sulfhydryl groups in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. , 1990, Biochimica et biophysica acta.

[10]  M. Encinas,et al.  Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: physicochemical characteristics of the nucleotide binding site, as deduced from fluorescent spectroscopy measurements. , 1990, Biochemistry.

[11]  Y. Hod,et al.  Mitochondrial phosphoenolpyruvate carboxykinase from the chicken. Comparison of the cDNA and protein sequences with the cytosolic isozyme. , 1990, The Journal of biological chemistry.

[12]  M. Parsons,et al.  Trypanosome glycosomal protein P60 is homologous to phosphoenolpyruvate carboxykinase (ATP). , 1989, Nucleic acids research.

[13]  J. Seyer,et al.  Cysteine 288: an essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP). , 1989, The Journal of biological chemistry.

[14]  S. Araneda,et al.  Affinity labeling of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase with the 2',3'-dialdehyde derivative of ATP. , 1988, Archives of biochemistry and biophysics.

[15]  E. Cardemil,et al.  The presence of functional arginine residues in phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. , 1987, Biochimica et biophysica acta.

[16]  J. Urbina.  The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: molecular, kinetic, and regulatory properties. , 1987, Archives of biochemistry and biophysics.

[17]  E. Gundelfinger,et al.  Nucleotide and deduced amino acid sequence of the phosphoenolpyruvate carboxykinase (GTP) from Drosophila melanogaster. , 1987, Nucleic acids research.

[18]  Y. Hod,et al.  Nucleotide sequence of the mRNA encoding the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) from the chicken. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[19]  J. Burnell.  Purification and Properties of Phosphoenolpyruvate Carboxykinase from C4 Plants , 1986 .

[20]  T. Nowak,et al.  The purification, characterization, and activation of phosphoenolpyruvate carboxykinase from chicken liver mitochondria. , 1982, The Journal of biological chemistry.

[21]  B. Sanwal,et al.  Allosteric control by calcium and mechanism of desensitization of phosphoenolpyruvate carboxykinase of Escherichia coli. , 1980, The Journal of biological chemistry.

[22]  H. Lardy,et al.  A vicinal dithiol containing an essential cysteine in phosphoenolpyruvate carboxykinase (guanosine triphosphate) from cytosol of rat liver. , 1978, Biochemistry.

[23]  H. Lardy,et al.  Phosphoenolpyruvate carboxykinase (guanosine triphosphate) from rat liver cytosol. Separation of homogeneous forms of the enzyme with high and low activity by chromatography on agarose-hexane-guanosine triphosphate. , 1978, Biochemistry.

[24]  A. Fersht.  Enzyme structure and mechanism , 1977 .

[25]  H. Holzer,et al.  Assay of phosphoenolpyruvate carboxykinase in crude yeast extracts. , 1976, Analytical biochemistry.

[26]  A. Glazer,et al.  Chemical modification of proteins: Selected methods and analytical procedures , 1975 .

[27]  J. Cannata,et al.  Phosphenolpyruvate carboxykinases from bakers' yeast. Kinetics of phosphoenolpyruvate formation. , 1974, The Journal of biological chemistry.

[28]  F. Wold.  Chemical modification of enzymes. , 1973, Birth defects original article series.

[29]  D. Keech,et al.  Sheep kidney phosphoenolpyruvate carboxylase. Further studies on the sulphydryl groups using dinitrofluorobenzene and N-ethylmaleimide. , 1972, Biochimica et biophysica acta.

[30]  M. Lane,et al.  The enzymatic carboxylation of phosphoenolpyruvate. II. Purification and properties of liver mitochondrial phosphoenolpyruvate carboxykinase. , 1966, The Journal of biological chemistry.

[31]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.