NUCLEOSIDE CATABOLIZING ACTIVITIES in SELECTED SEEDS by Nogood Almarwani a Thesis Submitted to the Faculty of the College Of

Total Page:16

File Type:pdf, Size:1020Kb

NUCLEOSIDE CATABOLIZING ACTIVITIES in SELECTED SEEDS by Nogood Almarwani a Thesis Submitted to the Faculty of the College Of NUCLEOSIDE CATABOLIZING ACTIVITIES IN SELECTED SEEDS By Nogood Almarwani A Thesis Submitted to the Faculty of the College of Graduate Studies at Middle Tennessee State University in Partial Fulfillment of the Requirements for the Degree of Master of Science in Chemistry Middle Tennessee State University December 2016 Thesis Committee: Dr. Paul C. Kline, Chair Dr. Andrew Burden Dr. Anthony Farone I dedicate this research work to my husband, parents, my sisters, and my brothers. ii ACKNOWLEDGMENTS This research work would not be possible without the support of a great people around me. In the beginning, I would like to thank my loving husband, Fahad Almarwani, for his endless encouragement and support me. I would also like to thank Dr. Paul C. Kline, my major professor. I cannot convey how much I appreciate him for his help and support me. Also, I would like to thank Dr. Anthony Farone and Dr. Andrew Burden as my committee members. I am grateful for their invaluable suggestions and for taking time to read my thesis. In addition, I would like to thank all the staff and faculty of the Department of Chemistry for their help and support throughout my stay at MTSU. Finally, special thanks to my parents, my sisters, my brothers, my little son, Sultan, and my friends. I would not have an opportunity to achieve this dream without their support and love. iii ABSTRACT The efficacy of pyrimidine and purine nucleotide metabolism plays a critical role in the progression of biological systems. The process of nucleotide degradation exists in all organisms. The nucleoside degradation and salvage of nucleotides, nucleosides, and nucleobases require several enzymes including deaminases and nucleosidases. Deaminases play a substantial role in the course of removing amino groups from selected nucleobases to convert one nucleoside to another. The cleavage of the N-glycosidic bond in nucleosides is catalyzed by the nucleoside hydrolases or nucleosidases. This process facilitates the recycling of nucleobases. Nucleoside degradation protein extracts were assessed in some seed sources including Alaska pea, okra, organic okra, peas (Cascadia Sugar Snap), yellow lupin, soybean, spinach, and cantaloupe. Extracts of un-germinated seeds were incubated with reaction mixtures containing 1 mM uridine, inosine, purine riboside, cytidine, adenosine, or 2'-deoxyadenosine in 10 Mm Tris pH 7.2 buffer. Using an HPLC with a Kinetex 5 μ, EVO C18 reverse phase column eluted with ammonium phosphate/ methanol, nucleosidase and deaminase activities were quantified. The results show the existence of active nucleosidases and deaminases in seeds tested. However, there were differences in the levels of activities based on the plant and substrate observed. Uridine, cytidine, and thymine exhibited the highest levels of activity among the nucleosides, while lower activities were observed with guanosine, purine riboside, inosine, and 2'-deoxyadenosine. Among the seeds, soybeans had the lowest activity levels, while okra had the highest activity levels. iv TABLE OF CONTENTS PAGE LIST OF TABLES ......................................................................................................... vii LIST OF FIGURES ........................................................................................................ viii CHAPTER I: INTRODUCTION......................................................................................1 Purines and Pyrimidines......................................................................................................2 Purine Metabolism .............................................................................................................5 Pyrimidine Metabolism ....................................................................................................10 Nucleoside Hydrolases......................................................................................................13 Uridine Nucleosidase.........................................................................................................15 Adenosine Nucleosidase…................................................................................................16 Guanosine Nucleosidase................................................................................................... 19 Inosine Nucleosidase….................................................................................................... 19 Cytidine Nucleosidase.......................................................................................................20 Nucleoside Deaminases ....................................................................................................21 Adenosine Deaminases (EC 3.5.4.4) .....................................................................21 Cytidine Deaminases (EC 3.5.4.1).........................................................................22 Guanosine Deaminases (EC 3.5.4.3).....................................................................22 Current Research ..............................................................................................................23 CHAPTER II: MATERIALS AND METHODS ...........................................................24 Equipment and Instrumentation .......................................................................................24 Materials and Reagents......................................................................................................24 Methods..............................................................................................................................25 v Preparation of Crude Extract...............................................................................25 Enzymatic Activity Measurement..........................................................................25 Measurement of Protein Concentration ...............................................................26 CHAPTER III: RESULTS AND DISCUSSION............................................................28 Enzyme Activities in Okra, Organic Okra and Yellow Lupin..........................................32 Enzyme Activities in Spinach and Cantaloupe.................................................................45 Enzyme Activities in Alaska Peas and Sugar Snap Peas..................................................54 Enzyme Activities in Soybean...........................................................................................62 CHAPTER IV: CONCLUSIONS…...............................................................................67 REFERENCES ................................................................................................................70 vi LIST OF TABLES TABLE PAGE 1. Summary of retention times of nucleosides and nucleobase…………………….31 2. Rate of disappearance of nucleoside with okra seed extract……...……..…….....42 3. Rate of disappearance of nucleoside with organic okra seed extract …………....43 4. Rate of disappearance of nucleoside with yellow lupin seed extract ..…..……....44 5. Rate of disappearance of nucleoside with spinach seed extract……..…………...52 6. Rate of disappearance of nucleoside with cantaloupe seed extract.……………....53 7. Rate of disappearance of nucleoside with Alaska pea seed extract...……….........60 8. Rate of disappearance of nucleoside with sugar snap pea seed extract………......61 9. Rate of disappearance of nucleoside with soybean seed extract…………............66 vii LIST OF FIGURES FIGURE PAGE 1. Representative structure of a nucleoside and a nucleotide……………………………2 2. General structure of a purine …………………….………….......................................3 3. General structure of purine bases adenine, hypoxanthine and guanine………………3 4. General structure of a pyrimidine …………….…………............................................4 5. Common pyrimidine bases……………………………………………………………4 6. Schematic representation of the purine nucleotides de novo pathway….…….............6 7. Purine salvage reactions ………………………...........................................................9 8. Schematic representation of the pyrimidine de novo pathway in plants………..…….11 9. Pyrimidine salvage reactions in plants…………………….………………….............12 10. Reaction mechanism of hydrolases .…………………….…………..........................14 11. Hydrolysis of uridine by uridine nucleosidase to uracil and ribose catalyzed by uridine nucleosidase...………………………………..................15 12. Reaction catalyzed by adenosine nucleosidase between adenosine and water to yield adenine and ribose..………….………….....................16 13. Hydrolysis of guanosine by guanosine or inosine/guanosine nucleosidase to guanine and ribose………..............…………...…………..................19 14. Reaction between inosine and water catalyzed by inosine nucleosidase to yield hypoxanthine and ribose….….………….……………............20 15. Cytidine hydrolysis by cytidine nucleosidase to cytosine and ribose………………..20 16. Adenosine nucleosidase mediates conversion of adenosine to inosine and releases NH3………………………….………………………….……………….21 17. Cytidine deaminase converts cytidine to uridine…………………………………….22 viii 18. Bovine serum albumin (BSA) standard curve generated after plotting known amount of BSA against A595nm………………….…….……….27 19. 2'-Deoxyadenosine nucleosidase catalyzed hydrolysis of 2'-deoxyadenosine into adenine and 2’-deoxyribose….……………….…….……..……….....................29 20. Structure of xanthine and xanthosine…………………….…......................................29 21. Uridine to uracil conversion catalyzed by uridine nucleosidase in okra seed extract……………………………………………………………………………...…33
Recommended publications
  • Thesis Final
    CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS by Abdullah K. Shamsuddin A Thesis Submitted to the Faculty of the College of Graduate Studies at Middle Tennessee State University in Partial Fulfillment of the Requirements for the Degree of Master of Science in Chemistry Middle Tennessee State University August 2015 Thesis Committee: Dr. Paul C. Kline, Chair Dr. Donald A. Burden Dr. Kevin L. Bicker I dedicate this research to my parents, my sisters, and my brother. I love you all. ii" " ACKNOWLEDGEMENTS I would like to express my sincere gratitude to my advisor, Dr. Paul C. Kline, for his guidance, support, and ongoing encouragement throughout this project. I also wish to thank my committee members, Dr. Donald A. Burden and Dr. Kevin L. Bicker, for their advice and insightful comments. In addition, I would like to thank all the staff and faculty of the Department of Chemistry for their contribution to the success of this study. Lastly, I wish to thank my family and my friends, without whom none of my accomplishments would have been possible. Thank you for you endless support, concern, love, and prayer. iii" " ABSTRACT Adenosine nucleosidase was purified from Alaska pea seeds five days after germination. A 4-fold purification has been reached with a 1.3 % recovery. The subunit molecular weight of adenosine nucleosidase was determined by mass spectrometry to be 26,103 daltons. The number of subunits was 1. The Michaelis constant, Km, and the maximum velocity, V max, for adenosine were determined to be 137 ± 48 µM, and 0.34 ± 0.02 µM/min respectively.
    [Show full text]
  • Activation-Induced Deoxycytidine Deaminase (AID) Co-Transcriptional Scanning at Single-Molecule Resolution
    ARTICLE Received 19 Nov 2014 | Accepted 13 Nov 2015 | Published 18 Dec 2015 DOI: 10.1038/ncomms10209 OPEN Activation-induced deoxycytidine deaminase (AID) co-transcriptional scanning at single-molecule resolution Gayan Senavirathne1,*, Jeffrey G. Bertram2,*, Malgorzata Jaszczur2,*, Kathy R. Chaurasiya3,4,*, Phuong Pham2, Chi H. Mak5,6, Myron F. Goodman2,5 & David Rueda1,3,4 Activation-induced deoxycytidine deaminase (AID) generates antibody diversity in B cells by initiating somatic hypermutation (SHM) and class-switch recombination (CSR) during transcription of immunoglobulin variable (IgV) and switch region (IgS) DNA. Using single- molecule FRET, we show that AID binds to transcribed dsDNA and translocates unidirectionally in concert with RNA polymerase (RNAP) on moving transcription bubbles, while increasing the fraction of stalled bubbles. AID scans randomly when constrained in an 8 nt model bubble. When unconstrained on single-stranded (ss) DNA, AID moves in random bidirectional short slides/hops over the entire molecule while remaining bound for B5 min. Our analysis distinguishes dynamic scanning from static ssDNA creasing. That AID alone can track along with RNAP during transcription and scan within stalled transcription bubbles suggests a mechanism by which AID can initiate SHM and CSR when properly regulated, yet when unregulated can access non-Ig genes and cause cancer. 1 Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA. 2 Department of Biological Sciences, University of Southern California, Los Angeles, California 90089, USA. 3 Department of Medicine, Section of Virology, Imperial College London, Du Cane Road, London W12 0NN, UK. 4 Single Molecule Imaging Group, MRC Clinical Sciences Center, Imperial College London, Du Cane Road, London W12 0NN, UK.
    [Show full text]
  • METABOLIC EVOLUTION in GALDIERIA SULPHURARIA By
    METABOLIC EVOLUTION IN GALDIERIA SULPHURARIA By CHAD M. TERNES Bachelor of Science in Botany Oklahoma State University Stillwater, Oklahoma 2009 Submitted to the Faculty of the Graduate College of the Oklahoma State University in partial fulfillment of the requirements for the Degree of DOCTOR OF PHILOSOPHY May, 2015 METABOLIC EVOLUTION IN GALDIERIA SUPHURARIA Dissertation Approved: Dr. Gerald Schoenknecht Dissertation Adviser Dr. David Meinke Dr. Andrew Doust Dr. Patricia Canaan ii Name: CHAD M. TERNES Date of Degree: MAY, 2015 Title of Study: METABOLIC EVOLUTION IN GALDIERIA SULPHURARIA Major Field: PLANT SCIENCE Abstract: The thermoacidophilic, unicellular, red alga Galdieria sulphuraria possesses characteristics, including salt and heavy metal tolerance, unsurpassed by any other alga. Like most plastid bearing eukaryotes, G. sulphuraria can grow photoautotrophically. Additionally, it can also grow solely as a heterotroph, which results in the cessation of photosynthetic pigment biosynthesis. The ability to grow heterotrophically is likely correlated with G. sulphuraria ’s broad capacity for carbon metabolism, which rivals that of fungi. Annotation of the metabolic pathways encoded by the genome of G. sulphuraria revealed several pathways that are uncharacteristic for plants and algae, even red algae. Phylogenetic analyses of the enzymes underlying the metabolic pathways suggest multiple instances of horizontal gene transfer, in addition to endosymbiotic gene transfer and conservation through ancestry. Although some metabolic pathways as a whole appear to be retained through ancestry, genes encoding individual enzymes within a pathway were substituted by genes that were acquired horizontally from other domains of life. Thus, metabolic pathways in G. sulphuraria appear to be composed of a ‘metabolic patchwork’, underscored by a mosaic of genes resulting from multiple evolutionary processes.
    [Show full text]
  • Structural Insights Into Histone Modifying Enzymes
    Wayne State University Wayne State University Theses January 2019 Structural Insights Into Histone Modifying Enzymes Shruti Amle Wayne State University, [email protected] Follow this and additional works at: https://digitalcommons.wayne.edu/oa_theses Part of the Biochemistry Commons, and the Molecular Biology Commons Recommended Citation Amle, Shruti, "Structural Insights Into Histone Modifying Enzymes" (2019). Wayne State University Theses. 693. https://digitalcommons.wayne.edu/oa_theses/693 This Open Access Embargo is brought to you for free and open access by DigitalCommons@WayneState. It has been accepted for inclusion in Wayne State University Theses by an authorized administrator of DigitalCommons@WayneState. STRUCTURAL INSIGHTS INTO HISTONE MODIFYING ENZYMES by SHRUTI AMLE THESIS Submitted to the Graduate School of Wayne State University, Detroit, Michigan in partial fulfillment of the requirements for the degree of MASTER OF SCIENCE 2019 MAJOR: BIOCHEMISTRY AND MOLECULAR BIOLOGY Approved By: _________________________________________ Advisor Date _________________________________________ _________________________________________ _________________________________________ i ACKNOWLEDGEMENTS Writing this thesis has been extremely captivating and gratifying. I take this opportunity to express my deep and sincere acknowledgements to the number of people for extending their generous support and unstinted help during my entire study. Firstly, I would like to express my respectful regards and deep sense of gratitude to my advisor, Dr. Zhe Yang. I am extremely honored to study and work under his guidance. His vision, ideals, timely motivation and immense knowledge had a deep influence on my entire journey of this career. Without his understanding and support, it would not have been possible to complete this research successfully. I also owe my special thanks to my committee members: Dr.
    [Show full text]
  • Difluorodeoxycytidine 5'-Triphosphate: a Mechanism of Self-Potentiation1
    ICANCER RESEARCH 52, 533-539, February 1, 1992] Cellular Elimination of 2',2'-Difluorodeoxycytidine 5'-Triphosphate: A Mechanism of Self-Potentiation1 Volker Heinemann,2 Y¡-ZhengXu, Sherri Chubb, Alina Sen, Larry W. Hertel, Gerald B. Grindey, and William Plunkett1 Department of Medical Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 [V. H., Y. X., S. C., A. S., W. P.], and Lilly Research Laboratories, Indianapolis, Indiana 46285 (L. W. H., G. B. G.] ABSTRACT less, clinical cellular pharmacology studies have demonstrated 2',2'-Difluorodeoxycytidine (dFdC, Gemcitabine) is a deoxycytidine that the dFdCTP:dCTP value reaches potentially inhibitory analogue which, after phosphorylation to the 5'-di- and 5'-triphosphate values during clinical trials (4, 10, 11). (b) dFdCTP is incor porated into DNA by DNA polymerases a and f, inhibiting (dFdCTP), induces inhibition of DNA synthesis and cell death. We examined the values for elimination kinetics of cellular dFdCTP and further elongation (9). (c) Once incorporated, dFdCMP resi found they were dependent on cellular concentration after incubation of dues in the terminal or penultimate positions of the DNA strand CCRF-CEM cells with dFdC and washing into drug-free medium. When inhibit the editing function of DNA polymerase <(9). This may the drug was washed out at low cellular dFdCTP levels (<50 n\\), fix damage caused by the incorporated analogue, (d) dFdCDP dFdCTP elimination was linear (t,: = 3.3 h), but it became biphasic at inhibits ribonucleotide reducíase,blocking DNA synthesis by intracellular dFdCTP levels >100 JIM. Although the initial elimination decreasing the cellular concentrations of deoxynucleoside tri rate was similar at all concentrations, at higher concentrations the phosphates (12-14).
    [Show full text]
  • Native Microorganisms Nucleoside Phosphorylase Cat
    Native Microorganisms Nucleoside Phosphorylase Cat. No. NATE-0606 Lot. No. (See product label) Introduction Description In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction:purine nucleoside + phosphate↔ purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. This enzyme participates in 3 metabolic pathways:purine metabolism, pyrimidine metabolism, and nicotinate and nicotinamide metabolism. Applications Nucleoside phosphorylase is used in coupled enzyme systems to measure protein dephosphorylation. This enzyme is useful for enzymatic determination of inorganic phosphorus, 5′-nucleotidase and adenosine deaminase when coupled with xanthine oxidase (XTO-212) and uricase (UAO-201, UAO-211). Purine nucleoside phosophorylase has shown the ability to perform both phosphorylosis and synthesis of purine deoxy-and ribonucleosides. It has also been found that membrane-ass ociated nucleoside phosphorylases may have a transmembranal orientation with their base and ribose-1-P binding sites on opposite sides of the membrane. Synonyms purine-nucleoside phosphorylase; inosine phosphorylase; PNP; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase;
    [Show full text]
  • Structural Properties of the Nickel Ions in Urease: Novel Insights Into the Catalytic and Inhibition Mechanisms
    Coordination Chemistry Reviews 190–192 (1999) 331–355 www.elsevier.com/locate/ccr Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms Stefano Ciurli a,*, Stefano Benini b, Wojciech R. Rypniewski b, Keith S. Wilson c, Silvia Miletti a, Stefano Mangani d a Institute of Agricultural Chemistry, Uni6ersity of Bologna, Viale Berti Pichat 10, I-40127 Bologna, Italy b European Molecular Biology Laboratory, c/o DESY, Notkestraße 85, D-22603 Hamburg, Germany c Department of Chemistry, Uni6ersity of York, Heslington, York YO15DD, UK d Department of Chemistry, Uni6ersity of Siena, Pian dei Mantellini 44, I-53100 Siena, Italy Accepted 13 March 1999 Contents Abstract.................................................... 331 1. Biological background ......................................... 332 2. Spectroscopic investigations of the urease active site structure .................. 333 3. Crystallographic studies of the native enzyme ............................ 334 4. Crystallographic studies of urease mutants.............................. 341 5. Crystallographic studies of urease–inhibitor complexes ...................... 345 6. Crystallographic study of a transition state analogue bound to urease.............. 348 7. A novel proposal for the urease mechanism ............................. 350 References .................................................. 353 Abstract This work provides a comprehensive critical summary of urease spectroscopy, crystallogra- phy, inhibitor binding, and site-directed
    [Show full text]
  • The Polycomb Group Genebmi1regulates Antioxidant
    The Journal of Neuroscience, January 14, 2009 • 29(2):529–542 • 529 Neurobiology of Disease The Polycomb Group Gene Bmi1 Regulates Antioxidant Defenses in Neurons by Repressing p53 Pro-Oxidant Activity Wassim Chatoo,1* Mohamed Abdouh,1* Jocelyn David,1 Marie-Pier Champagne,1 Jose´ Ferreira,2 Francis Rodier,4 and Gilbert Bernier1,3 1Developmental Biology Laboratory and 2Department of Pathology, Maisonneuve-Rosemont Hospital, Montreal, Quebec, Canada H1T 2M4, 3Department of Ophthalmology, University of Montreal, Montreal, Quebec, Canada H3T 1J4, and 4Lawrence Berkeley National Laboratory, Berkeley, California 94720 Aging may be determined by a genetic program and/or by the accumulation rate of molecular damages. Reactive oxygen species (ROS) generated by the mitochondrial metabolism have been postulated to be the central source of molecular damages and imbalance between levels of intracellular ROS and antioxidant defenses is a characteristic of the aging brain. How aging modifies free radicals concentrations and increases the risk to develop most neurodegenerative diseases is poorly understood, however. Here we show that the Polycomb group and oncogene Bmi1 is required in neurons to suppress apoptosis and the induction of a premature aging-like program characterized by reduced antioxidant defenses. Before weaning, Bmi1 Ϫ/Ϫ mice display a progeroid-like ocular and brain phenotype, while Bmi1ϩ/ Ϫ mice, although apparently normal, have reduced lifespan. Bmi1 deficiency in neurons results in increased p19 Arf/p53 levels, abnormally high ROS concentrations, and hypersensitivity to neurotoxic agents. Most Bmi1 functions on neurons’ oxidative metabolism are genetically linked to repression of p53 pro-oxidant activity, which also operates in physiological conditions. In Bmi1 Ϫ/Ϫ neurons, p53 and corepres- sors accumulate at antioxidant gene promoters, correlating with a repressed chromatin state and antioxidant gene downregulation.
    [Show full text]
  • DOI: 10.2478/V10129-011-0033-Y
    PLANT BREEDING AND SEED SCIENCE Volume 64 2011 DOI: 10.2478/v10129-011-0033-y Wolfgang Schweiger 1,* , Barbara Steiner 2, Apinun Limmongkon 2, Kurt Brunner 3, Marc Lemmens 2, Franz Berthiller 4, Hermann Bürstmayr 2, Gerhard Adam 1 1Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria; 2Institute of Biotechnology in Plant Production, Department of Agrobiotechnology, University of Natural Resources and Applied Life Sciences, A-3430 Tulln, Austria; 3Institute of Chemical Engineering, Vienna University of Technology, A-1060 Vienna, Austria; 4Center for Analytical Chemistry, Depart- ment of Agrobiotechnology, University of Natural Resources and Applied Life Sciences, A-3430 Tulln, Austria; * Author to whom correspondence should be addressed. e-mail: [email protected] ; CLONING AND HETEROLOGOUS EXPRESSION OF CANDIDATE DON-INACTIVATING UDP-GLUCOSYLTRANFERASES FROM RICE AND WHEAT IN YEAST ABSTRACT Fusarium graminearum and related species causing Fusarium head blight of cereals and ear rot of maize produce the trichothecene toxin and virulence factor deoxynivalenol (DON). Plants can detoxify DON to a variable extent into deoxynivalenol-3-O-glucoside (D3G). We have previously reported the DON inactivat- ing glucosyltransferase (UGT) AtUGT73C5 from Arabidopsis thaliana (Poppenberger et al , 2003). Our goal was to identify UGT genes from monocotyledonous crop plants with this enzymatic activity. The two selected rice candidate genes with the highest sequence similarity with AtUGT73C5 were expressed in a toxin sensitive yeast strain but failed to protect against DON. A full length cDNA clone corresponding to a transcript derived fragment (TDF108) from wheat, which was reported to be specifically expressed in wheat genotypes contain- ing the quantitative trait locus Qfhs.ndsu-3BS for Fusarium spreading resistance (Steiner et al , 2009) was reconstructed.
    [Show full text]
  • Ijms-20-05263-V2
    Delft University of Technology Leloir Glycosyltransferases in Applied Biocatalysis A Multidisciplinary Approach Mestrom, Luuk; Przypis, Marta; Kowalczykiewicz, Daria; Pollender, André; Kumpf, Antje; Marsden, Stefan R.; Szymańska, Katarzyna; Hanefeld, Ulf; Hagedoorn, Peter Leon; More Authors DOI 10.3390/ijms20215263 Publication date 2019 Document Version Final published version Published in International Journal of Molecular Sciences Citation (APA) Mestrom, L., Przypis, M., Kowalczykiewicz, D., Pollender, A., Kumpf, A., Marsden, S. R., Szymańska, K., Hanefeld, U., Hagedoorn, P. L., & More Authors (2019). Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach. International Journal of Molecular Sciences, 20(21), [5263]. https://doi.org/10.3390/ijms20215263 Important note To cite this publication, please use the final published version (if applicable). Please check the document version above. Copyright Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons. Takedown policy Please contact us and provide details if you believe this document breaches copyrights. We will remove access to the work immediately and investigate your claim. This work is downloaded from Delft University of Technology. For technical reasons the number of authors shown on this cover page is limited to a maximum of 10. International Journal of Molecular Sciences Review Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach Luuk Mestrom 1, Marta Przypis 2,3 , Daria Kowalczykiewicz 2,3, André Pollender 4 , Antje Kumpf 4,5, Stefan R. Marsden 1, Isabel Bento 6, Andrzej B.
    [Show full text]
  • B Number Gene Name Mrna Intensity Mrna Present # of Tryptic
    list list sample) short list predicted B number Gene name assignment mRNA present mRNA intensity Gene description Protein detected - Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0003 thrB 6781 P 9 P 3 3 P 3 0 homoserine kinase Metabolism of small molecules b0004 thrC 15039 P 18 P 10 P 11 P 10 0 threonine synthase Metabolism of small molecules b0008 talB 20561 P 20 P 13 P 16 P 13 0 transaldolase B Metabolism of small molecules b0009 mog 1296 P 7 0 0 0 0 required for the efficient incorporation of molybdate into molybdoproteins Metabolism of small molecules b0014 dnaK 13283 P 32 P 23 P 24 P 23 0 chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins Cell processes b0031 dapB 2348 P 16 P 3 3 P 3 0 dihydrodipicolinate reductase Metabolism of small molecules b0032 carA 9312 P 14 P 8 P 8 P 8 0 carbamoyl-phosphate synthetase, glutamine (small) subunit Metabolism of small molecules b0048 folA 1588 P 7 P 1 2 P 1 0 dihydrofolate reductase type I; trimethoprim resistance Metabolism of small molecules peptidyl-prolyl cis-trans isomerase (PPIase), involved in maturation of outer b0053 surA 3825 P 19 P 4 P 5 P 4 P(m) 1 GenProt membrane proteins (1st module) Cell processes b0054 imp 2737 P 42 P 5 0 0 P(m) 5 GenProt organic solvent tolerance Cell processes b0071 leuD 4770
    [Show full text]
  • Discovery of Novel Bacterial Queuine Salvage Enzymes and Pathways in Human Pathogens
    Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens a,1 b,1 c,1 b d a Yifeng Yuan , Rémi Zallot , Tyler L. Grove , Daniel J. Payan , Isabelle Martin-Verstraete , Sara Sepic´ , Seetharamsingh Balamkundue, Ramesh Neelakandane, Vinod K. Gadie, Chuan-Fa Liue, Manal A. Swairjof,g, Peter C. Dedone,h,i, Steven C. Almoc, John A. Gerltb,j,k, and Valérie de Crécy-Lagarda,l,2 aDepartment of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611; bInstitute for Genomic Biology, University of Illinois at Urbana–Champaign, Urbana, IL 61801; cDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461; dLaboratoire de Pathogénèse des Bactéries Anaérobies, Institut Pasteur et Université de Paris, F-75015 Paris, France; eSingapore-MIT Alliance for Research and Technology, Infectious Disease Interdisciplinary Research Group, 138602 Singapore, Singapore; fDepartment of Chemistry and Biochemistry, San Diego State University, San Diego, CA 92182; gThe Viral Information Institute, San Diego State University, San Diego, CA 92182; hDepartment of Biological Engineering and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; iCenter for Environmental Health Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139; jDepartment of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; kDepartment of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; and lUniversity of Florida Genetics Institute, Gainesville, FL 32610 Edited by Tina M. Henkin, The Ohio State University, Columbus, OH, and approved August 1, 2019 (received for review June 16, 2019) Queuosine (Q) is a complex tRNA modification widespread in 1A. The TGT enzyme, which is responsible for the base ex- eukaryotes and bacteria that contributes to the efficiency and accuracy change, is the signature enzyme in the Q biosynthesis pathway.
    [Show full text]