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

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Why is it important?

Our switch from bovine to clostridial GluDH in pursuit of a structure forced us to start again on kinetic characterisation. This paper provides the basic information including the fact that this GDH, though with a somewhat small subunit than bovine GluDH, still shows homotropic allosteric behaviour. The dye chromatography described here has provided many subsequent Ph.D. students with a 1-step dream purification