Lewicka Aleksandra J, Lyczakowski Jan J, Blackhurst Gavin, Pashkuleva Christiana, Rothschild-Mancinelli Kyle, Tautvaišas Dainius, Thornton Harry, Villanueva Hugo, Xiao Weike, Slikas Justinas, Horsfall Louise, Elfick Alistair, French Christopher
The University of Edinburgh , School of Biological Sciences, Darwin Building, King's Buildings, Mayfield Road, Edinburgh, EH9 3JR, United Kingdom.
ACS Synth Biol. 2014 Dec 19;3(12):976-8. doi: 10.1021/sb500020g.
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.
乙醇是一种重要的生物燃料。运动发酵单胞菌丙酮酸脱羧酶（Pdc）和乙醇脱氢酶（AdhB）的异源表达可提高大肠杆菌中的乙醇产量。构建了PDC和ADH的融合体并在大肠杆菌中表达。已证明该融合酶具有两种活性。与单独表达这两种酶时相比，AdhB与PDC融合时其活性显著降低。然而，表达融合蛋白的细胞比共表达Pdc和AdhB的细胞产生乙醇的速度更快且产量更高，这表明由于两种酶的融合导致了特定的速率提高。
