| Title | Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in Escherichia coli. |
| Publication Type | Journal Article |
| Year of Publication | 2014 |
| Authors | Lewicka AJ, Lyczakowski JJ, Blackhurst G, Pashkuleva C, Rothschild-Mancinelli K, Tautvaišas D, Thornton H, Villanueva H, Xiao W, Slikas J, Horsfall L, Elfick A, French C |
| Journal | ACS Synth Biol |
| Volume | 3 |
| Issue | 12 |
| Pagination | 976-8 |
| Date Published | 2014 Dec 19 |
| ISSN | 2161-5063 |
| Keywords | Alcohol Dehydrogenase, Escherichia coli, Ethanol, Models, Molecular, Pyruvate Decarboxylase, Recombinant Fusion Proteins |
| Abstract | Ethanol is an important biofuel. Heterologous expression of Zymomonas mobilis pyruvate decarboxylase (Pdc) and alcohol dehydrogenase (AdhB) increases ethanol production in Escherichia coli. A fusion of PDC and ADH was generated and expressed in E. coli. The fusion enzyme was demonstrated to possess both activities. AdhB activity was significantly lower when fused to PDC than when the two enzymes were expressed separately. However, cells expressing the fusion protein generated ethanol more rapidly and to higher levels than cells coexpressing Pdc and AdhB, suggesting a specific rate enhancement due to the fusion of the two enzymes. |
| DOI | 10.1021/sb500020g |
| Alternate Journal | ACS Synth Biol |
| PubMed ID | 25524103 |
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