Article
Mutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations.
Chembiochem : a European journal of chemical biology - 1 Jul 2016
Rahimi Mehran, van der Meer Jan-Ytzen, Geertsema Edzard M, Poddar Harshwardhan, Baas Bert-Jan, Poelarends Gerrit J
Abstract excerpt
The enzyme 4-oxalocrotonate tautomerase (4-OT), which catalyzes enol-keto tautomerization as part of a degradative pathway for aromatic hydrocarbons, promiscuously catalyzes various carbon-carbon bond-forming reactions. These include the aldol condensation of acetaldehyde with benzaldehyde to yield cinnamaldehyde. Here, we demonstrate that 4-OT can be engineered into a more efficient aldolase for this...
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