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Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium
A R Raine1, C C Yang, L C Packman
1Department of Biochemistry, University of Cambridge, United Kingdom.
Protein Science : a Publication of the Protein Society
|December 1, 1995
Abstract:
A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-pi bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-pi and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.