Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli

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

doi:10.1021/sb500020g

Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	976-978
Number of pages	3
Journal	ACS Synthetic Biology
Volume	3
Issue number	12
DOIs	https://doi.org/10.1021/sb500020g
Publication status	Published - 1 Jan 2014

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Lewicka, A. J., Lyczakowski, J. J., Blackhurst, G., Pashkuleva, C., Rothschild-Mancinelli, K., Tautvaišas, D., Thornton, H., Villanueva, H., Xiao, W., Slikas, J., Horsfall, L., Elfick, A., & French, C. (2014). Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli. ACS Synthetic Biology, 3(12), 976-978. https://doi.org/10.1021/sb500020g

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title = "Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli",

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.",

author = "Lewicka, {Aleksandra J.} and Lyczakowski, {Jan J.} and Gavin Blackhurst and Christiana Pashkuleva and Kyle Rothschild-Mancinelli and Dainius Tautvai{\v s}as and Harry Thornton and Hugo Villanueva and Weike Xiao and Justinas Slikas and Louise Horsfall and Alistair Elfick and Christopher French",

year = "2014",

month = jan,

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doi = "10.1021/sb500020g",

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volume = "3",

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journal = "ACS Synthetic Biology",

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publisher = "American Chemical Society",

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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 2014, 'Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli', ACS Synthetic Biology, vol. 3, no. 12, pp. 976-978. https://doi.org/10.1021/sb500020g

TY - JOUR

T1 - Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli

AU - Lewicka, Aleksandra J.

AU - Lyczakowski, Jan J.

AU - Blackhurst, Gavin

AU - Pashkuleva, Christiana

AU - Rothschild-Mancinelli, Kyle

AU - Tautvaišas, Dainius

AU - Thornton, Harry

AU - Villanueva, Hugo

AU - Xiao, Weike

AU - Slikas, Justinas

AU - Horsfall, Louise

AU - Elfick, Alistair

AU - French, Christopher

PY - 2014/1/1

Y1 - 2014/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84919643583&partnerID=8YFLogxK

U2 - 10.1021/sb500020g

DO - 10.1021/sb500020g

M3 - Article

AN - SCOPUS:84919643583

SN - 2161-5063

VL - 3

SP - 976

EP - 978

JO - ACS Synthetic Biology

JF - ACS Synthetic Biology

IS - 12

ER -

Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli

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