Steady state kinetics of the glutamate dehydrogenase from an archaebacterial extreme thermophile, isolate AN1.

[1]  R. Daniel,et al.  Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1. , 1993, Biochimica et biophysica acta.

[2]  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.

[3]  R. Chiaraluce,et al.  Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. , 1991, European journal of biochemistry.

[4]  R. Chiaraluce,et al.  Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. , 1991, European journal of biochemistry.

[5]  M. Scully,et al.  The acceleration of the inhibition of platelet prothrombinase complex by heparin. , 1986, The Biochemical journal.

[6]  D. Hornby,et al.  The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate. , 1984, The Biochemical journal.

[7]  T. A. Venkitasubramanian,et al.  Isolation and characterisation of glutamate dehydrogenase from Mycobacterium smegmatis CDC 46. , 1980, Biochimica et biophysica acta.

[8]  W. Cleland,et al.  Kinetic mechanism of glutamate dehydrogenase. , 1980, Biochemistry.

[9]  S. Stone,et al.  Glutamate dehydrogenase of lupin nodules: kinetics of the amination reaction. , 1980, Archives of biochemistry and biophysics.

[10]  Paul C. Engel,et al.  Enzyme Kinetics: The Steady-State Approach , 1977 .

[11]  P. Engel,et al.  A product-inhibition study of bovine liver glutamate dehydrogenase. , 1975, The Biochemical journal.

[12]  E. Silverstein Equilibrium kinetic study of bovine liver glutamate dehydrogenase at high pH. , 1974, Biochemistry.

[13]  J. Coulton,et al.  Studies on the kinetics and regulation of glutamate dehydrogenase of Salmonella typhimurium. , 1973, Canadian journal of microbiology.

[14]  H. Mor,et al.  The isozymic nature and kinetic properties of glutamate dehydrogenase from safflower seedlings , 1973 .

[15]  J. King,et al.  Partial purification and kinetic properties of glutamic dehydrogenase from soybean cotyledons , 1971 .

[16]  P. Engel,et al.  Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate. , 1970, The Biochemical journal.

[17]  P. Engel,et al.  Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes. , 1969, The Biochemical journal.

[18]  J. Wright,et al.  Glutamate Dehydrogenases of Thiobacillus novellus KINETIC PROPERTIES AND A POSSIBLE CONTROL MECHANISM , 1968 .

[19]  W. Cleland The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. , 1963, Biochimica et biophysica acta.

[20]  Carl Frieden Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction. , 1959, The Journal of biological chemistry.