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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Single mutation at a highly conserved region of chloramphenicol acetyltransferase enables isobutyl acetate production directly from cellulose by Clostridium thermocellum at elevated temperatures

Fig. 1

Broad substrate specificity of CATSa. a Acetylation of chloramphenicol and alcohol by a chloramphenicol acetyltransferase (CAT) and an alcohol acetyltransferase (AAT), respectively. b Comparison between the predicted binding free energies for various alcohols bound to the binding pocket of CATSa and the titer of esters produced by an CATSa-overexpressing E. coli with external supply of alcohols. c Structure of the CATSa homology model. The red arrows indicate the binding pockets (in yellow cloud) formulated by the trimeric structure of CATSa

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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