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Protein recognition of ammonium cations using side‐chain aromatics: A structural variation for secondary ammonium ligands
Author(s) -
Raine Andrew R.C.,
Yang ChienChih,
Packman Leonard C.,
White Scott A.,
Mathews F. Scott,
Scrutton Nigel S.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041222
Subject(s) - dimethylamine , trimethylamine , chemistry , ammonium , dehydrogenase , amine gas treating , hydrogen bond , protein quaternary structure , substrate (aquarium) , stereochemistry , crystallography , enzyme , biochemistry , organic chemistry , molecule , biology , protein subunit , gene , ecology
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‐7r bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation‐7r and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.