BioChem - DOS

Fusion of Pyruvate Decarboxylase and Alcohol Dehydrogenase Increases Ethanol Production in Escherichia coli

ACS Synthetic biology

Lewicka, Aleksandra J.; Lyczakowski, Jan J.; Blackhurst, Gavin; Pashkuleva, Christiana; Rothschild-Mancinelli, Kyle; Tautvaiš as, Dainius; Thornton, Harry; Villanueva, Hugo; Xiao, Weike; Slikas, Justinas; Horsfall, Louise; Elfick, Alistair; French, Christopher

<P>Ethanol is an important biofuel. Heterologous expression of <I>Zymomonas mobilis</I> pyruvate decarboxylase (Pdc) and alcohol dehydrogenase (AdhB) increases ethanol production in <I>Escherichia coli</I>. A fusion of PDC and ADH was generated and expressed in <I>E. coli</I>. 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.</P><P><B>Graphic Abstract</B><BR><IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/asbcd6/2014/asbcd6.2014.3.issue-12/sb500020g/production/images/medium/sb-2014-00020g_0003.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/sb500020g'>ACS Electronic Supporting Info</A></P>

2014

American Chemical Society

2161-5063

3

12

pp.976-978

10.1021/sb500020g

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART71047825