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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_002334685Cyc: Desulfovibrio sp. G11 Cellular Overview Connections between pathways are omitted for legibility.

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Ferric Reductase Activity of the Arsh Protein from Acidithiobacillus Ferrooxidans
J. Microbiol. Biotechnol. (2011), 21(5), 464–469 doi: 10.4014/jmb.1101.01020 First published online 13 April 2011 Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans Mo, Hongyu1,2, Qian Chen1,2, Juan Du1, Lin Tang1, Fang Qin1, Bo Miao2, Xueling Wu2, and Jia Zeng1,2* 1College of Biology, Hunan University, Changsha, Hunan 410082, P. R. China 2Department of Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China Received: January 14, 2011 / Revised: March 10, 2011 / Accepted: March 11, 2011 The arsH gene is one of the arsenic resistance system in iron (free or chelated) into ferrous iron before its incorporation bacteria and eukaryotes. The ArsH protein was annotated into heme and nonheme iron-containing proteins. Ferric as a NADPH-dependent flavin mononucleotide (FMN) reductase catalyzes the reduction of complexed Fe3+ to reductase with unknown biological function. Here we complexed Fe2+ using NAD(P)H as the electron donor. The report for the first time that the ArsH protein showed resulting Fe2+ is subsequently released and incorporated high ferric reductase activity. Glu104 was an essential into iron-containing proteins [17]. residue for maintaining the stability of the FMN cofactor. Here we report for the first time that the ArsH protein The ArsH protein may perform an important role for showed high ferric reduction activity. The ArsH from A. cytosolic ferric iron assimilation in vivo. ferrooxidans may perform an important role as a NADPH- Keywords: Acidithiobacillus ferrooxidans, ArsH, flavoprotein, dependent ferric reductase for cytosolic ferric iron assimilation ferric reductase in vivo. MATERIALS AND METHODS Arsenic resistance genes are widespread in nature.
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Copyright by Jeremy Daniel O'connell 2012
Copyright by Jeremy Daniel O’Connell 2012 The Dissertation Committee for Jeremy Daniel O’Connell Certifies that this is the approved version of the following dissertation: Systemic Protein Aggregation in Stress and Aging Restructures Cytoplasmic Architecture Committee: Edward Marcotte, Supervisor Dean Appling Andrew Ellington Makkuni Jayaram Scott Stevens Systemic Protein Aggregation in Stress and Aging Restructures Cytoplasmic Architecture by Jeremy Daniel O’Connell, B.S. Dissertation Presented to the Faculty of the Graduate School of The University of Texas at Austin in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy The University of Texas at Austin September 2012 Dedication Cytisus laburnum, simul vincet omnem To my dad and mom who encouraged and enabled my education with countless sacrifices, I promised this graduation would be the one we would attend, and I am truly sorry I was not swift enough to make that possible. Acknowledgements Foremost, I thank my advisor Edward Marcotte, for not just a second lease on a life in science but one in an amazing lab environment. His intellectual rigor, enduring patience, amazing work ethic, and enthusiasm for discovery were an inspiration. I thank my collaborators in this project: Gwen Stovall, Alice Zhao, Gabe Wu, and Mark Tsechansky for their comradery and support on this great adventure. I thank the talented undergraduates: Maguerite West-Driga, Ariel Royall, and Tyler McDonald who stuck with me. Each of you will soon be a better scientist than I ever will, and I hope you enjoyed and learned from our research together nearly as much as I did.
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The Regulation of Carbamoyl Phosphate Synthetase-Aspartate Transcarbamoylase-Dihydroorotase (Cad) by Phosphorylation and Protein-Protein Interactions
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Uva-DARE (Digital Academic Repository)
UvA-DARE (Digital Academic Repository) The pivotal role of CTP synthetase in the metabolism of (deoxy)nucleosides in neuroblastoma Bierau, J. Publication date 2003 Link to publication Citation for published version (APA): Bierau, J. (2003). The pivotal role of CTP synthetase in the metabolism of (deoxy)nucleosides in neuroblastoma. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulations If you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: https://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. UvA-DARE is a service provided by the library of the University of Amsterdam (https://dare.uva.nl) Download date:27 Sep 2021 1 1 Introduction n "Nucleotidess are water-soluble components which naturally occur, inn larger or smaller portions, in both animal and vegetable foods. Combinedd with other components, theyy are the elements to bring the flavor in food." fromm the Ajinomoto Europe website ChapterChapter 1 Introduction n 1.11 General introduction to neuroblastoma Incidence Incidence Neuroblastomaa is the most common extra cranial solid cancer of childhood.
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1611 REGULATION of PYRIMIDINE METABOLISM in PLANTS Chris
[Frontiers in Bioscience 9, 1611-1625, May 1, 2004] REGULATION OF PYRIMIDINE METABOLISM IN PLANTS 1, 2 1, 3 1, 4 1, 5 1, 6 1, 7 Chris Kafer , Lan Zhou , Djoko Santoso , Adel Guirgis , Brock Weers , Sanggyu Park and Robert Thornburg 1 1 Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, 2 BASF Plant Science LLC, 2901 South Loop Drive, Ste 3800, Ames, Iowa 50014, 3 Lan Zhou, Pioneer Hi-Bred International, Inc. 7300 NW 62nd Avenue, PO Box 1004, Johnston, Iowa 50131-1004, 4 Indonesian Biotechnology Research Institute for Estate Crops, Jl, Taman Kencana No 1, Bogor 16151 Indonesia, 5 Institute of Genetic Engineering and Biotechnology, Menofiya University, PO Box 79/22857, Sadat City, Egypt, 6 Department of Biochemistry, University of Iowa, 4/511 Bowen Science Building, Iowa City, Iowa 52242-1109, 7 Division of Life and Environment, College of Natural Resources, Daegu University, Gyongsan City, Gyongbuk, Korea 712-714 TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Pyrimidine metabolic pathways 3.1. De novo pyrimidine biosynthesis 3.1.1. CPSase 3.1.2. ATCase 3.1.3. DHOase 3.1.4. DHODH 3.1.5. UMPS 3.1.6. Intracellular Organization of the de novo Pathway 3.2. Pyrimidine Salvage and Recycling 3.2.1. Cytosine deaminase 3.2.2. Cytidine deaminase 3.2.3. UPRTase 3.3. Pyrimidine Modification 3.3.1. UMP/CMP kinase 3.3.2. NDP kinase 3.3.3. CTP synthase, NDP reductase, dUTPase 3.3.4. Thymidylate synthase/Dihydrofolate reductase 3.4. Pyrimidine Catabolism 4. Regulation of pyrimidine metabolism 4.1.
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