title: Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.
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.
authors.affiliation: Department of Biochemistry, University of Cambridge, United Kingdom.
authors.forename: A R
authors.initials: AR
authors.lastname: Raine
authors.forename: C C
authors.initials: CC
authors.lastname: Yang
authors.forename: L C
authors.initials: LC
authors.lastname: Packman
authors.forename: S A
authors.initials: SA
authors.lastname: White
authors.forename: F S
authors.initials: FS
authors.lastname: Mathews
authors.forename: N S
authors.initials: NS
authors.lastname: Scrutton
mesh_terms: D001665:Binding Sites; D002412:Cations; D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry* / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*
chemical_list: D002412:Cations; D000644:Quaternary Ammonium Compounds; D010089:Oxidoreductases, N-Demethylating; C020064:dimethylamine dehydrogenase