Identification of 2-enolbutyrate as the product of the reaction of maize leaf phosphoenolpyruvate carboxylase with (Z)- and (E)-2-phosphoenolbutyrate: evidence from NMR and kinetic measurements

[1]  A. Iglesias,et al.  Higher plant phosphoenolpyruvate carboxylase , 1987 .

[2]  A. Iglesias,et al.  Interaction of acetyl phosphate and carbamyl phosphate with plant phosphoenolpyruvate carboxylase. , 1987, The Biochemical journal.

[3]  A. Iglesias,et al.  On the molecular mechanism of maize phosphoenolpyruvate carboxylase activation by thiol compounds. , 1984, Plant physiology.

[4]  N. Fujita,et al.  Reaction mechanism of phosphoenolpyruvate carboxylase. Bicarbonate-dependent dephosphorylation of phosphoenol-alpha-ketobutyrate. , 1984, Biochemistry.

[5]  G. Robillard,et al.  Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: stereospecificity of proton transfer in the phosphorylation of enzyme I from (Z)-phosphoenolbutyrate. , 1983, Biochemistry.

[6]  M. O'Leary Phosphoenolpyruvate Carboxylase: An Enzymologist's View , 1982 .

[7]  T. Nowak,et al.  Stereospecificity of (E)- and (Z)-phosphoenol-alpha-ketobutyrate with chicken liver phosphoenolpyruvate carboxykinase and related phosphoenolpyruvate-utilizing enzymes. , 1982, Biochemistry.

[8]  M. O'Leary,et al.  Kinetic and isotope effect studies of maize phosphoenolpyruvate carboxylase. , 1981, Biochemistry.

[9]  I. A. Rose,et al.  PHYSICAL, CHEMICAL, AND ENZYMOLOGICAL CHARACTERIZATION OF ENOLPYRUVATE , 1979 .

[10]  I. A. Rose,et al.  Evidence that carboxyphosphate is a kinetically competent intermediate in the carbamyl phosphate synthetase reaction. , 1979, The Journal of biological chemistry.

[11]  A. Meister,et al.  Carbonic-phosphoric anhydride (carboxy phosphate). Significance in catalysis and regulation of glutamine-dependent carbamyl phosphate synthetase. , 1978, The Journal of biological chemistry.

[12]  H. Penefsky Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. , 1977, The Journal of biological chemistry.

[13]  J. Sedmak,et al.  A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. , 1977, Analytical biochemistry.

[14]  A. Meister,et al.  Identification of enzyme-bound activated CO2 as carbonic-phosphoric anhydride: isolation of the corresponding trimethyl derivative from the active site of glutamine-dependent carbamyl phosphate synthetase. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[15]  H. Wood,et al.  The carboxylation of phosphoenolpyruvate and pyruvate. II. The active species of "CO2" utilized by phosphoenlpyruvate carboxylase and pyruvate carboxylase. , 1971, The Journal of biological chemistry.

[16]  G. L. Kenyon,et al.  Analogs of phosphoenolpyruvate. On the specificity of pyruvate kinase from rabbit muscle. , 1971, Biochemistry.

[17]  A. E. Woods,et al.  Synthetic homologs of phosphoenolpyruvate and specificity of pyruvate kinase. , 1970, Biochemistry.

[18]  I. A. Rose,et al.  Stereochemistry of the enzymatic carboxylation of phosphoenolpyruvate. , 1969, The Journal of biological chemistry.

[19]  M. Lane,et al.  The enzymatic carboxylation of phosphoenolpyruvate. I. Purification and properties of phosphoenolpyruvate carboxylase. , 1966, The Journal of biological chemistry.