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. 1995 Dec;4(12):2625-8.
doi: 10.1002/pro.5560041222.

Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands

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Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands

A R Raine et al. Protein Sci. 1995 Dec.

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.

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