Communication

Facilitated Substrate Channeling in a Self-Assembled Trifunctional Enzyme Complex^†

Dr. Chun You

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

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Suwan Myung,

Suwan Myung

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

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Y.-H. Percival Zhang,

Corresponding Author

Y.-H. Percival Zhang

[email protected]

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

Institute of Critical Technology and Applied Science (ICTAS), Virginia Tech, Blacksburg, VA 24061 (USA)

DOE BioEnergy Science Center, Oak Ridge, TN 37831 (USA)

Gate Fuels Inc., Blacksburg, VA 24060 (USA)

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com Search for more papers by this author

Dr. Chun You,

Dr. Chun You

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

Search for more papers by this author

Suwan Myung,

Suwan Myung

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

Search for more papers by this author

Y.-H. Percival Zhang,

Corresponding Author

Y.-H. Percival Zhang

[email protected]

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com

Institute of Critical Technology and Applied Science (ICTAS), Virginia Tech, Blacksburg, VA 24061 (USA)

DOE BioEnergy Science Center, Oak Ridge, TN 37831 (USA)

Gate Fuels Inc., Blacksburg, VA 24060 (USA)

Biological Systems Engineering Department, Virginia Tech, 304 Seitz Hall, Blacksburg, VA 24061 (USA) http://www.sugarcar.com Search for more papers by this author

First published: 23 July 2012

https://doi.org/10.1002/anie.201202441

Citations: 170

^†

This work was supported partially by the DOE BioEnergy Science Center (BESC) and DOE ARPA-E Petro project. This work was also partially supported by the College of Agriculture and Life Sciences Bioprocessing and Biodesign Research Center at Virginia Tech.

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Graphical Abstract

Three enzymes, triosephosphate isomerase (orange in picture), aldolase (cyan), and fructose 1,6-bisphosphatase (purple), which contained dockerins (red), self-assembled into a static trifunctional enzyme complex through interaction with a mini-scaffoldin protein consisting of three different cohesins (green). The synthetic enzyme complex exhibited an enhanced reaction rate compared to the noncomplexed three-enzyme mixture at the same enzyme concentration.

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Volume51, Issue35

August 27, 2012

Pages 8787-8790

Facilitated Substrate Channeling in a Self-Assembled Trifunctional Enzyme Complex^†

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Facilitated Substrate Channeling in a Self-Assembled Trifunctional Enzyme Complex†

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Facilitated Substrate Channeling in a Self-Assembled Trifunctional Enzyme Complex^†