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Authors: Pallavi Subhraveti Ron Caspi Peter Midford Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000301935Cyc: Acinetobacter baumannii AB_2008-15-52 Cellular Overview Connections between pathways are omitted for legibility.

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Corynebacterium Glutamicum Mycoredoxin 3 Protects Against Multiple Oxidative Stresses
Advance Publication J. Gen. Appl. Microbiol. doi 10.2323/jgam.2019.10.003 ©2020 Applied Microbiology, Molecular and Cellular Biosciences Research Foundation Full Paper 1 Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses 2 and displays thioredoxin-like activity 3 (Received September 24, 2019; Accepted October 28, 2019; J-STAGE Advance publication date: October 30, 2020) 4 Tao Su#, Chengchuan Che#, Ping Sun, Xiaona Li, Zhijin Gong, Jinfeng Liu, Ge Yang * 5 6 College of Life Sciences, Qufu Normal University, Qufu, Shandong 273165, China; 7 8 Running title: Feature of C. glutamicum mycoredoxin 3 9 10 11 # These authors contributed equally to this work. 12 13 * Corresponding authors: 14 Ge Yang 15 16 E-mail [email protected] 17 Tel: 86-13953760056 18 19 20 21 22 23 24 25 26 27 Abstract 28 Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative 29 conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a 30 high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. 31 Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection 32 against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in 33 ribonucleotide reductase (RNR), insulin and 5, 5’-dithiobis-(2-nitro-benzoicacid) (DTNB), but 34 also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was 35 exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol 36 mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 37 were necessary to maintain its activity.
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Generate Metabolic Map Poster
Authors: Peter D. Karp Suzanne Paley Julio Collado-Vides John L Ingraham Ingrid Keseler Markus Krummenacker Cesar Bonavides-Martinez Robert Gunsalus An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Carol Fulcher Ian Paulsen Socorro Gama-Castro Robert LaRossa Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. EcoCyc: Escherichia coli K-12 substr. MG1655 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari Amanda Mackie Alberto Santos-Zavaleta succinate phosphate succinate N-acetyl-DL-methionine + L-ornithine glutathione + L-methionine S-oxide D-fructofuranose γ Ag+ molybdate ferroheme b L,L-homocystine asp lys cys L-alanyl- -D- D-mannopyranose 6-phosphate 2+ 2+ H D-methionine 2-deoxy-D-glucose succinate formate formate succinate D-tartrate putrescine agmatine cadaverine L-tartrate D-fructofuranose 6-phosphate + nitrate nitrate Cu thiosulfate deoxycholate L,L-homocystine D-cystine D-cycloserine methyl β-D-glucoside putrescine asp spermidine (S)-2-hydroxybutanoate (S)-2-hydroxybutanoate arg L-homoserine lactone magnesium hydrogenphosphate magnesium hydrogenphosphate antimonous acid glutamyl-meso- Co2+ Cd2+ lactulose poly-β-1,6- met cob(I)inamide 2,3-dioxo-
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Tannin Degradation by Phytopathogen's Tannase: a Plant's
Biocatalysis and Agricultural Biotechnology 21 (2019) 101342 Contents lists available at ScienceDirect Biocatalysis and Agricultural Biotechnology journal homepage: http://www.elsevier.com/locate/bab Tannin degradation by phytopathogen’s tannase: A Plant’s defense perspective Kanti Prakash Sharma Department of Biosciences, Mody University of Science and Technology, Lakshmangarh, Sikar, Rajasthan, 332311, India ARTICLE INFO ABSTRACT Keywords: Tannins are plant secondary metabolites and characterized as plant defensive molecules. They impose a barrier Tannin against phytopathogens invasion in plants and thus oppose diseases occurrence in them. Tannase is an enzyme Tannase known for its ability to degrade plant tannins. Important plant pathogens also possess tannase coding sequence in Plant defense their genome. Researches on tannase are till date focused on its applications in animal nutrition, in bioreme Pathogen diation and in food industries etc. The information about tannase role with respect to pathogen’s virulence is Virulence very scanty or almost nil in scientific literature. The presence of tannase in pathogen’s genome is an adaptive feature which may be a part of its strategy to overcome the negative effects of plants tannins. The present review summarizes important aspects of tannase and its possible role in disease causing ability of pathogens in plants. 1. Introduction hydrolyzable tannins (Zhang et al., 2001). In complex tannins, a cate chin or epicatechin unit is bound glycosidically to a gallotannin or an Tannins are universally present in plants and represent the fourth ellagitannin unit to yield catechin or epicatechin and gallic acid or most abundant group of secondary metabolites after cellulose, hemi ellagic acid upon hydrolysis.
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The Role of Intermembrane Space Redox Factors in Glutathione Metabolism and Intracellular Redox Equilibrium Hatice Kubra Ozer University of South Carolina
University of South Carolina Scholar Commons Theses and Dissertations 2015 The Role of Intermembrane Space Redox Factors In Glutathione Metabolism And Intracellular Redox Equilibrium Hatice Kubra Ozer University of South carolina Follow this and additional works at: https://scholarcommons.sc.edu/etd Part of the Chemistry Commons Recommended Citation Ozer, H. K.(2015). The Role of Intermembrane Space Redox Factors In Glutathione Metabolism And Intracellular Redox Equilibrium. (Doctoral dissertation). Retrieved from https://scholarcommons.sc.edu/etd/3702 This Open Access Dissertation is brought to you by Scholar Commons. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of Scholar Commons. For more information, please contact [email protected]. THE ROLE OF INTERMEMBRANE SPACE REDOX FACTORS IN GLUTATHIONE METABOLISM AND INTRACELLULAR REDOX EQUILIBRIUM by Hatice Kubra Ozer Bachelor of Science Uludag University, 2004 Master of Food Science and Nutrition Clemson University, 2010 Submitted in Partial Fulfillment of the Requirements For the Degree of Doctor of Philosophy in Chemistry College of Arts and Sciences University of South Carolina 2015 Accepted by: Caryn E. Outten, Major Professor F. Wayne Outten, Committee Chair Erin Connolly, Committee Member Andrew B. Greytak, Committee Member Lacy K. Ford, Senior Vice Provost and Dean of Graduate Studies © Copyright by Hatice Kubra Ozer, 2015 All Rights Reserved. ii ACKNOWLEDGEMENTS First, I would like to thank my advisor, Dr. Caryn E. Outten for her patience, guidance, expertise, and confidence in me to complete the work contained herein. She has been an excellent mentor during my graduate program. She is also the only person beside myself who is guaranteed to have read every word of this manuscript and to review every presentations in the past and her insight was irreplaceable.
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Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review
molecules Review Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review 1, 1, 1 1 Trnka Daniel y , Hossain Md Faruq y , Jordt Laura Magdalena , Gellert Manuela and Lillig Christopher Horst 2,* 1 Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, 17475 Greifswald, Germany; [email protected] (T.D.); [email protected] (H.M.F.); [email protected] (J.L.M.); [email protected] (G.M.) 2 Christopher Horst Lillig, Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Ferdinand-Sauerbruch-Straße, 17475 Greifswald, Germany * Correspondence: [email protected]; Tel.: +49-3834-865407; Fax: +49-3834-865402 These authors contributed equally to this work. y Academic Editor: Pál Perjési Received: 29 July 2020; Accepted: 22 August 2020; Published: 25 August 2020 Abstract: Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have come more and more into focus. GSH is indispensable in mitochondrial iron-sulfur (FeS) cluster biosynthesis, primarily by co-ligating FeS clusters as a cofactor of the CGFS-type (class II) glutaredoxins (Grxs). GSH is required for the export of the yet to be defined FeS precursor from the mitochondria to the cytosol. In the cytosol, it is an essential cofactor, again of the multi-domain CGFS-type Grxs, master players in cellular iron and FeS trafficking. In this review, we summarize the recent advances and progress in this field. The most urgent open questions are discussed, such as the role of GSH in the export of FeS precursors from mitochondria, the physiological roles of the CGFS-type Grx interactions with BolA-like proteins and the cluster transfer between Grxs and recipient proteins.
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BARNES-DISSERTATION-2016.Pdf (1.557Mb)
ABSORPTION AND METABOLISM OF MANGO (MANGIFERA INDICA L.) GALLIC ACID AND GALLOYL GLYCOSIDES A Dissertation by RYAN CRISPEN BARNES Submitted to the Office of Graduate and Professional Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Chair of Committee, Stephen Talcott Co-Chair of Committee, Susanne Talcott Committee Members, Nancy Turner Arul Jayaraman Head of Department, Boon Chew December 2016 Major Subject: Food Science and Technology Copyright 2016 Ryan Barnes ABSTRACT The composition, absorption, metabolism, and excretion of gallic acid, monogalloyl glucose, and gallotannins in mango (Mangifera indica L.) pulp were investigated. Each galloyl derivative was hypothesized to have a different rate of absorption, and their concentrations were compared in the pulp of five mango varieties. The cultivar Ataulfo was found to have the highest concentration of monogalloyl glucose and gallotannins while the cultivar Kent had the lowest. Enzymatic hydrolysis of gallotannins with tannase led to the characterization of six digalloyl glucoses and five trigalloyl glucoses that have the potential to be formed in the colon following gallotannin consumption. The bioaccessibility of galloyl derivatives was evaluated in both homogenized mango pulp and 0.65 mm3 cubes following in vitro digestion conditions. Monogalloyl glucose was found to be bioaccessible in both homogenized and cubed mango pulp. However, cubed mango pulp had a significantly higher amount of gallotannins still bound to the fruit following digestion. Gallic acid bioaccessibility significantly increased following digestion in both homogenized and cubed mango pulp, likely from hydrolysis of gallotannins. Additionally, for the first time, the absorption of monogalloyl glucose and gallic acid was investigated in both Caco-2 monolayer transport models and a porcine pharmacokinetic model with no significant differences found in their absorption or ability to produce phase II metabolites.
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Nummer 18/17 03 Mei 2017 Nummer 18/17 2 03 Mei 2017
Nummer 18/17 03 mei 2017 Nummer 18/17 2 03 mei 2017 Inleiding Introduction Hoofdblad Patent Bulletin Het Blad de Industriële Eigendom verschijnt The Patent Bulletin appears on the 3rd working op de derde werkdag van een week. Indien day of each week. If the Netherlands Patent Office Octrooicentrum Nederland op deze dag is is closed to the public on the above mentioned gesloten, wordt de verschijningsdag van het blad day, the date of issue of the Bulletin is the first verschoven naar de eerstvolgende werkdag, working day thereafter, on which the Office is waarop Octrooicentrum Nederland is geopend. Het open. Each issue of the Bulletin consists of 14 blad verschijnt alleen in elektronische vorm. Elk headings. nummer van het blad bestaat uit 14 rubrieken. Bijblad Official Journal Verschijnt vier keer per jaar (januari, april, juli, Appears four times a year (January, April, July, oktober) in elektronische vorm via www.rvo.nl/ October) in electronic form on the www.rvo.nl/ octrooien. Het Bijblad bevat officiële mededelingen octrooien. The Official Journal contains en andere wetenswaardigheden waarmee announcements and other things worth knowing Octrooicentrum Nederland en zijn klanten te for the benefit of the Netherlands Patent Office and maken hebben. its customers. Abonnementsprijzen per (kalender)jaar: Subscription rates per calendar year: Hoofdblad en Bijblad: verschijnt gratis Patent Bulletin and Official Journal: free of in elektronische vorm op de website van charge in electronic form on the website of the Octrooicentrum Nederland.
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Biochemical and Biophysical Characterization of a Mycoredoxin
International Journal of Biological Macromolecules 107 (2018) 1999–2007 Contents lists available at ScienceDirect International Journal of Biological Macromolecules j ournal homepage: www.elsevier.com/locate/ijbiomac Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis a a a b a Raphael J. Eberle , Liege A. Kawai , Fabio R. de Moraes , Ljubica Tasic , Raghuvir K. Arni , a,∗ Monika A. Coronado a Multiuser Center for Biomolecular Innovation, Departament of Physics, Instituto de Biociências Letras e Ciências Exatas (Ibilce), Universidade Estadual Paulista (UNESP), São Jose do Rio Preto, SP, 15054-000, Brazil b Institute of Chemistry, University of Campinas (UNICAMP), Campinas, SP, 13083-970, Brazil a r t i c l e i n f o a b s t r a c t Article history: Glutaredoxin A1 from Corynebacterium pseudotuberculosis was shown to be a mycoredoxin protein. In Received 25 July 2017 this study, we established a process to overexpress and purify glutaredoxin A1. The aim of this study Received in revised form 6 October 2017 was the investigation of the Glutaredoxin A1 from C. pseudotuberculosis behavior under different redox Accepted 11 October 2017 environments and the identiﬁcation of lead molecules, which can be used for speciﬁc inhibitor develop- Available online 16 October 2017 ment for this protein family. A quantitative assay was performed measuring the rate of insulin reduction spectrophotometrically at 640 nm through turbidity formation from the precipitation of the free insulin. Keywords: Glutaredoxin A1, at 5 ␮M concentration, accelerated the reduction process of 0.2 mM insulin and 1 mM Corynebacterium pseudotuberculosis Glutaredoxin DTT.
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Supplementary Information
Supplementary information (a) (b) Figure S1. Resistant (a) and sensitive (b) gene scores plotted against subsystems involved in cell regulation. The small circles represent the individual hits and the large circles represent the mean of each subsystem. Each individual score signifies the mean of 12 trials – three biological and four technical. The p-value was calculated as a two-tailed t-test and significance was determined using the Benjamini-Hochberg procedure; false discovery rate was selected to be 0.1. Plots constructed using Pathway Tools, Omics Dashboard. Figure S2. Connectivity map displaying the predicted functional associations between the silver-resistant gene hits; disconnected gene hits not shown. The thicknesses of the lines indicate the degree of confidence prediction for the given interaction, based on fusion, co-occurrence, experimental and co-expression data. Figure produced using STRING (version 10.5) and a medium confidence score (approximate probability) of 0.4. Figure S3. Connectivity map displaying the predicted functional associations between the silver-sensitive gene hits; disconnected gene hits not shown. The thicknesses of the lines indicate the degree of confidence prediction for the given interaction, based on fusion, co-occurrence, experimental and co-expression data. Figure produced using STRING (version 10.5) and a medium confidence score (approximate probability) of 0.4. Figure S4. Metabolic overview of the pathways in Escherichia coli. The pathways involved in silver-resistance are coloured according to respective normalized score. Each individual score represents the mean of 12 trials – three biological and four technical. Amino acid – upward pointing triangle, carbohydrate – square, proteins – diamond, purines – vertical ellipse, cofactor – downward pointing triangle, tRNA – tee, and other – circle.
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Generate Metabolic Map Poster
Authors: Pallavi Subhraveti Ron Caspi Quang Ong Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_900114035Cyc: Amycolatopsis sacchari DSM 44468 Cellular Overview Connections between pathways are omitted for legibility.
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TRACE: Tennessee Research and Creative Exchange
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 8-2009 Structure-Function Studies of the Large Subunit of Ribonucleotide Reductase from Homo sapiens and Saccharomyces cerevisiae James Wesley Fairman University of Tennessee - Knoxville Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Fairman, James Wesley, "Structure-Function Studies of the Large Subunit of Ribonucleotide Reductase from Homo sapiens and Saccharomyces cerevisiae. " PhD diss., University of Tennessee, 2009. https://trace.tennessee.edu/utk_graddiss/49 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by James Wesley Fairman entitled "Structure- Function Studies of the Large Subunit of Ribonucleotide Reductase from Homo sapiens and Saccharomyces cerevisiae." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the equirr ements for the degree of Doctor of Philosophy, with a major in Biochemistry and Cellular and Molecular Biology. Chris G. Dealwis,
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Enzymatic PET Degradation
GREEN AND SUSTAINABLE CHEMISTRY CHIMIA 2019, 73, No. 9 743 doi:10.2533/chimia.2019.743 Chimia 73 (2019) 743–749 © Swiss Chemical Society Enzymatic PET Degradation Athena Papadopoulou§, Katrin Hecht§, and Rebecca Buller* Abstract: Plastic, in the form of packaging material, disposables, clothing and other articles with a short lifespan, has become an indispensable part of our everyday life. The increased production and use of plastic, however, accelerates the accumulation of plastic waste and poses an increasing burden on the environment with negative effects on biodiversity and human health. PET, a common thermoplastic, is recycled in many countries via ther- mal, mechanical and chemical means. Recently, several enzymes have been identified capable of degrading this recalcitrant plastic, opening possibilities for the biological recycling of the omnipresent material. In this review, we analyze the current knowledge of enzymatic PET degradation and discuss advances in improving the involved enzymes via protein engineering. Looking forward, the use of plastic degrading enzymes may facilitate sustain- able plastic waste management and become an important tool for the realization of a circular plastic economy. Keywords: Biocatalysis · Biodegradation · Enzyme engineering · Plastic recycling · PET Dr. Athena Papadopoulou studied Biology 1. Introduction and received her BSc from the University Plastic has become an omnipresent material in our daily life of Ioannina. She completed her MSc in and, as a consequence, the plastic industry has become the seventh Chemistry with a focus on Chemical and most important industry in Europe, employing more than 1.5 mil- Biochemical Technologies. In 2013 she lion people with a turnover of 355 billion Euros in 2017.[1] Plastic moved to Biotechnology group at the production is cheap and the generated plastic items are durable University of Ioannina to pursue her PhD and versatile.
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