Kinetic studies on the binding of 1,N6-etheno-NAD+ to glutamate dehydrogenase from Clostridium symbiosum
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference33 articles.
1. The glutamate dehydrogenase gene of Clotridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli
2. 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
3. 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
4. The essentail active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phophate
5. Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding
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