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Evolution Of Enzymatic Activities In The Enolase Superfamily: D-Mannonate Dehydratase From Novosphingobium Aromaticivorans, John Rakus, Alexander Fedorov, Elena Federov, Margaret Glasner, Jacob Vick, Patricia Babbitt, Steven Almo, John Gerlt

John F. Rakus

The D-mannonate dehydratase (ManD) function was assigned to a group of orthologous proteins in the mechanistically diverse enolase superfamily by screening a library of acid sugars. Structures of the wild type ManD from Novosphingobium aromaticivorans were determined at pH 7.5 in the presence of Mg2+ and also in the presence of Mg2+ and the 2-keto-3-keto-d-gluconate dehydration product; the structure of the catalytically active K271E mutant was determined at pH 5.5 in the presence of the d-mannonate substrate. As previously observed in the structures of other members of the enolase superfamily, ManD contains two domains, an N-terminal α+β capping domain and …