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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Main Authors: Narendranath Bhokisham, Haig Pakhchanian, David Quan, Tanya Tschirhart, Chen-Yu Tsao, Gregory F. Payne, William E. Bentley
Format: Article
Language:English
Published: Elsevier 2016-09-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340916304401
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spelling 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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