What is it about?
Native clostridial GDH is a hexamer but detailed sequence and structure allow us to destabilise particular subunit interfaces to see if one can make stable trimers, dimers, monomers. In this study we constrcucted stable dimers.
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Why is it important?
We wanted to know first whether smaller oligomers are active and secondly, if so, whether they retain allosteric properties. These dimers ,though stable and well-folded are not active. In fact subsequent studies would seem to indicate that intersubunits interaction in formation of the complete hexamer is required to permit activity.
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This page is a summary of: Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, October 1996, Elsevier,
DOI: 10.1016/s0167-4838(96)00017-9.
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