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Evolution Of Enzymatic Activities In The Enolase Superfamily: L-Fuconate Dehydratase From Xanthomonas Campestris, Wen Yew, Alexander Fedorov, Elena Federov, John Rakus, Richard Pierce, Steven Almo, John Gerlt
Evolution Of Enzymatic Activities In The Enolase Superfamily: L-Fuconate Dehydratase From Xanthomonas Campestris, Wen Yew, Alexander Fedorov, Elena Federov, John Rakus, Richard Pierce, Steven Almo, John Gerlt
John F. Rakus
Many members of the mechanistically diverse enolase superfamily have unknown functions. In this report we use both genome (operon) context and screening of a library of acid sugars to assign the l-fuconate dehydratase (FucD) function to a member of the mandelate racemase (MR) subgroup of the superfamily encoded by the Xanthomonas campestris pv. campestris str. ATCC 33913 genome (GI:21233491). Orthologues of FucD are found in both bacteria and eukaryotes, the latter including the rTS beta protein in Homo sapiens that has been implicated in regulating thymidylate synthase activity. As suggested by sequence alignments and confirmed by high-resolution structures in the …
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
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 …