Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase
Data presented is related to an article titled “Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase” (Bhokisham et al., 2016) [1]. In this article, we have presented western blot and flux data associated with assembly of Pfs–LuxS enzyme comple...
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doaj-439eec5c30924bdd80bd16755ce75fdc2020-11-25T02:02:58ZengElsevierData in Brief2352-34092016-09-01810311035Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminaseNarendranath Bhokisham0Haig Pakhchanian1David Quan2Tanya Tschirhart3Chen-Yu Tsao4Gregory F. Payne5William E. Bentley6Biological Sciences Graduate Program - College of Computer, Mathematical and Natural Sciences, University of Maryland, 4066 Campus Drive, College Park, MD 20742, United States; Institute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United StatesFischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United StatesInstitute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United States; Fischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United StatesInstitute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United States; Fischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United StatesInstitute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United States; Fischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United StatesInstitute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United States; Fischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United StatesBiological Sciences Graduate Program - College of Computer, Mathematical and Natural Sciences, University of Maryland, 4066 Campus Drive, College Park, MD 20742, United States; Institute of Bioscience and Biotechnology Research, University of Maryland, College Park, 5115 Plant Science and Landscape Architecture Building, College Park, MD 20742, United States; Fischell Department of Bioengineering, University of Maryland, Room 3122, Jeong H. Kim Engineering Building (Bldg. #225), College Park, MD 20742, United States; Corresponding author at: Fischell Department of Bioengineering, Room 3122, Jeong H.Kim Engineering Building (Bldg.#225), University of Maryland, College Park, MD 20742, United States.Data presented is related to an article titled “Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase” (Bhokisham et al., 2016) [1]. In this article, we have presented western blot and flux data associated with assembly of Pfs–LuxS enzyme complexes on beads using uni-tagged and bi-tagged LuxS enzymes. We have also presented biochemical flux following changes in enzyme stoichiometries. We covalently coupled a Pfs-LuxS complex with Protein G, an antibody binding non-enzyme component and directed these complexes to the surfaces of bacterial cells via anti-Escherichia coli antibodies. Fluorescence microscopy images represented the altered behavior of bacterial cells in response to the autoinducer-2 that is synthesized by the Protein G-enzyme complexes. Keywords: Biofabrication, Metabolic flux, Engineered tags, Transglutaminase, Quorum sensinghttp://www.sciencedirect.com/science/article/pii/S2352340916304401 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Narendranath Bhokisham Haig Pakhchanian David Quan Tanya Tschirhart Chen-Yu Tsao Gregory F. Payne William E. Bentley |
spellingShingle |
Narendranath Bhokisham Haig Pakhchanian David Quan Tanya Tschirhart Chen-Yu Tsao Gregory F. Payne William E. Bentley Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase Data in Brief |
author_facet |
Narendranath Bhokisham Haig Pakhchanian David Quan Tanya Tschirhart Chen-Yu Tsao Gregory F. Payne William E. Bentley |
author_sort |
Narendranath Bhokisham |
title |
Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
title_short |
Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
title_full |
Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
title_fullStr |
Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
title_full_unstemmed |
Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
title_sort |
data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase |
publisher |
Elsevier |
series |
Data in Brief |
issn |
2352-3409 |
publishDate |
2016-09-01 |
description |
Data presented is related to an article titled “Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase” (Bhokisham et al., 2016) [1]. In this article, we have presented western blot and flux data associated with assembly of Pfs–LuxS enzyme complexes on beads using uni-tagged and bi-tagged LuxS enzymes. We have also presented biochemical flux following changes in enzyme stoichiometries. We covalently coupled a Pfs-LuxS complex with Protein G, an antibody binding non-enzyme component and directed these complexes to the surfaces of bacterial cells via anti-Escherichia coli antibodies. Fluorescence microscopy images represented the altered behavior of bacterial cells in response to the autoinducer-2 that is synthesized by the Protein G-enzyme complexes. Keywords: Biofabrication, Metabolic flux, Engineered tags, Transglutaminase, Quorum sensing |
url |
http://www.sciencedirect.com/science/article/pii/S2352340916304401 |
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