Literature summary for 4.2.1.8 extracted from

Rakus, J.F.; Fedorov, A.A.; Fedorov, E.V.; Glasner, M.E.; Vick, J.E.; Babbitt, P.C.; Almo, S.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans (2007), Biochemistry, 46, 12896-12908.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Novosphingobium aromaticivorans

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method at room temperature. Structures of the wild type ManD from are 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 is determined at pH 5.5 in the presence of the D-mannonate substrate	Novosphingobium aromaticivorans

Organism

Organism	UniProt	Comment	Textmining
Novosphingobium aromaticivorans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Novosphingobium aromaticivorans

Synonyms

Synonyms	Comment	Organism
D-mannonate dehydratase	-	Novosphingobium aromaticivorans
ManD	-	Novosphingobium aromaticivorans

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Release 2023.1 (January 2023)