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Article

Systematic screening for catalytic promiscuity in 4-oxalocrotonate tautomerase: enamine formation and aldolase activity.

Chembiochem : a European journal of chemical biology - 7 Mar 2011

Zandvoort Ellen, Baas Bert-Jan, Quax Wim J, Poelarends Gerrit J

Abstract excerpt

The enzyme 4-oxalocrotonate tautomerase (4-OT) is part of a catabolic pathway for aromatic hydrocarbons in Pseudomonas putida mt-2, where it catalyzes the conversion of 2-hydroxy-2,4-hexadienedioate(1) to 2-oxo-3-hexenedioate(2). 4-OT is a member of the tautomerase superfamily, a group of homologous proteins that are characterized by a β-α-β structural fold and a catalytic amino-terminal proline. In the mechanism...

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PMID: 21290551
DOI: 10.1002/cbic.201000633

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