Cooperativity between trimers of the hexameric glutamate dehydrogenase from Clostridium symbiosum.

[1]  P. Engel,et al.  Positive cooperativity with Hill coefficients of up to 6 in the glutamate concentration dependence of steady-state reaction rates measured with clostridial glutamate dehydrogenase and the mutant A163G at high pH. , 1995, Biochemistry.

[2]  L. A. Basso,et al.  Initial formation of a non-covalent enzyme-reagent complex during the inactivation of clostridial glutamate dehydrogenase by Ellman's reagent: determination of the enzyme's dissociation constant for the binary complex with NAD+ from protection studies. , 1994, Biochimica et biophysica acta.

[3]  P. Engel,et al.  Identification of the reactive cysteine in clostridial glutamate dehydrogenase by site-directed mutagenesis and proof that this residue is not strictly essential. , 1994, Protein engineering.

[4]  K. Britton,et al.  The catalytic role of aspartate in the active site of glutamate dehydrogenase. , 1994, The Biochemical journal.

[5]  D. Hornby,et al.  Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding. , 1994, The Biochemical journal.

[6]  D W Rice,et al.  Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. , 1993, Journal of molecular biology.

[7]  L. A. Basso,et al.  The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination. , 1993, European journal of biochemistry.

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

[9]  M. McPherson,et al.  The glutamate dehydrogenase gene of Clotridium symbiosum , 1992 .

[10]  J. Shaw,et al.  The mechanism of ligand binding to the periplasmic C4-dicarboxylate binding protein (DctP) from Rhodobacter capsulatus. , 1992, The Journal of biological chemistry.

[11]  K. Britton,et al.  Subunit assembly and active site location in the structure of glutamate dehydrogenase , 1992, Proteins.

[12]  D. M. Parker,et al.  Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum. , 1991, Biochimica et biophysica acta.

[13]  D. Ballou,et al.  Determination of the dead time of a stopped-flow fluorometer. , 1989, Analytical biochemistry.

[14]  G. Roberts,et al.  Correction for light absorption in fluorescence studies of protein-ligand interactions. , 1983, Analytical biochemistry.

[15]  H. Nakatani,et al.  Analysis of signal amplitude in stopped-flow method for enzyme-ligand systems. , 1980, Journal of biochemistry.

[16]  H. Gutfreund Kinetic analysis of the properties and reactions of enzymes. , 1975, Progress in biophysics and molecular biology.

[17]  Clive R. Bagshaw,et al.  The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation. , 1974, The Biochemical journal.

[18]  S. Halford,et al.  A substate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli. , 1969, The Biochemical journal.