DOCSLIB.ORG

Information to Users

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Information to Users INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely afreet reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book. Photographs included in the original manuscript have been reproduced xerographically in this copy. Higher quality 6" x 9" black and white photographic prints are available for any photographs or illustrations appearing in this copy for an additional charge. Contact UMI directly to order. University Microfilms International A Bell & Howell Information Company 300 North Zeeb Road, Ann Arbor, Ml 48106-1346 USA 313/761-4700 800/521-0600 Order Number 9218983 Purification, characterization, and inhibition of S-adenosyl-X-methionine decarboxylase (E.C. 4.1.1.50) from Acanthamoeba castellanni N eff Hugo, Eric R., Ph.D. The Ohio State University, 1992 UMI 300 N. ZeebRd. Ann Arbor, MI 48106 Purification, Characterization, and Inhibition of S-Adenosyl-L-Methionine Decarboxylase (E.C. 4.1.1.50) from Acanthamoeba castellanii Neff DISSERTATION Presented in Partial Fulfillment of the Requirement for the Degree of Doctor of Philosophy in the Graduate School of the Ohio State University by Eric R. Hugo, B.S., M.S. * * * * * The Ohio State University 1992 Dissertation Committee Approved by Thomas J. Byers, Committee Chair Berl O. Oakley Donald H. Dean Adviser Roy H. Tassava Department of Molecular Genetics To Vickie ACKNOWLEGEMENTS I would like to thank Drs. Thomas and Sandra Byers for their gracious help during my tenure in Columbus. I would also like to thank Dr. Wayne Parrish for support during part of this study as well as for many helpful discussions. I am greatly appreciative of the all of the assistance Ms. Rebbecca Gast provided during my stay in Dr. Byers laboratory. Finally, I thank my wife Vickie for her love, kindness, and patience during the many long hours I spent working in the laboratory. VITA November 27,1961 ...................................................Born Ft. Thomas, Ky. May, 1983 ................................................................ B.S. Northern Kentucky University Highland Heights, Ky. 1983-1986 ................................................................ Graduate Teaching Associate Dept, of Microbiology The Ohio State University Columbus, OH December, 1986 .......................................................M.S. The Ohio State University Columbus, OH 1986-1990 ............................................................... Graduate Teaching and Research Associate, Dept, of Molecular Genetics, The Ohio State Univesity, Columbus, OH 1990-199 1................................................................. Instructor, Denison University Granville, OH 1991-presen t ............................................................. Research Associate, DepL of Biochemistry and Molecular Biophysics, Washington University School of Medicine St. Louis, MO PUBLICATIONS Abstracts: Byers, T.J. and E.R. Hugo. 1990. S-adenosylraethionine decarboxylase: a possible role in the encystment of Acanthamoeba castellanii. Invest. Opthal. Vis. Sci. Abstract 2066 31:420. Hugo, E.R. and T.J. Byers. 1989. Purification and characterization of S-adenosyl-L-methionine decarboxylase from Acanthamoeba castellanii. J. Ceh Biol. Abstract 1403 109:255a. Hugo, E.R. and T.J. Byers. 1989. S-adenosylmethionine decarboxylase of Acanthamoeba castellanii (Neff strain). J. Protozool Abstract 198 37(4) :42A Papers and Proceedings Byers, T.J., B.G. Kim, L.E. King, and E.R. Hugo. 1991. Molecular aspects of the cell cycle and encystment in Acanthamoeba. Rev. Infect. Dis.13(Suppl 5):S378-84. Hugo, E.R., W.R. McLaughlin, K. Oh, and O.H. Tuovinen. 1991. Quantitative enumeration of Acanthamoeba for evaluation of cyst inactivation in contact lens care solutions. Invest. Vis. Ophthalmol. Res.32(3):655-57. Byers, T.J., E.R. Hugo, and V. Stewart. 1990. Genes of Acanthamoeba: DNA, RNA and protein sequences (a review), J. Protozool. 37(4):17S-25S. FIELDS OF STUDY Major Field: Molecular Biology v ABBREVIATIONS apparent Km ab: antibody agm: agmatine MTA: methylthioadenosine Ber: berenil NEM: Neffs Encystment medium BLOTTO Bovine-lacto transfer Norspd: norspermidine optimizer CBB: Coumassie Brilliant Blue OGMA: optimal growth medium A Dap: 1,3-diaminopropane Ora: ornithine dcSAM: decarboxylated SAM ODC: ornithine decarboxylase DFMO: a-difluoromethylomithine Pi: inorganic phosphate DGM-11: defined growth medium PA: polyamine DTT: dithiothreatol Pent: pentamidine EB: ethidium bromide Put: putrescine EEA: encystment enhancing act. Pro: propamidine HPLC: high performance liquid SAMDC: S-adenosylmethionine chromatography decarboxylase HS: hydroxystilbamidine SAM: S-adenosylmethionine kDa: kilodalton TPCK: tosylphenylalanyl chloromethyl ketone Kl: inhibition constant velocity TABLE OF CONTENTS ACKNOWLEGEMENTS ............................................................................................. iii VTTA .................................................................. ............................................................iv LIST OF FIGURES___________________________________________________ xi LIST OF TABLES_____________________________________________________xiv Introduction. ---------------------------------------------------------------------------------------- 1 1. Literature Review-------------------- --------------------------------------------------------- 3 l.L Polyamines _________________________________________________ 3 1.1.1 Polyamine function ___________________________________ 3 1.1.2 Polyamine synthesis ...................................................................... 7 1.1.3 Regulation of polyamine biosynthesis ............................................12 1.1.4 Polyamine function and synthesis as targets of chemotherapy -------- --------------------------------------------14 1.2 Acanthamoeba ______________________________________________ 19 1.2.1 General characteristics..................................................................19 1.2.2 Developmental biology .. ......................................................... 21 1.2.3 Polyamine metabolism ................................................................-2 4 1.2.4 Molecular biology ............................................................ 25 1.2.5 Pathogenicity ..................................................................................26 2. Materials and Methods ...............................................................................................31 2.1 Cell culture and growth ................................................................................31 2.1.1 Cell lines ........................................................................................ 31 2.1.2 Media..............................................................................................32 2.1.3 Cell growth ..................................................................................... 32 2.1.4 Effect of diamidines on growth ......................................................33 2.2 Enzyme purification ...................................................................................... 34 2.2.1 Homogenization and extract preparation .......................................34 2.2.2 Precipitation ................................................................................... 35 2.2.3 Hydrophobic interaction chromatography .....................................35 2.2.4 DEAE anion exchange chromatography .......................................36 2.2.5 Gel filtration chromatography ........................................................37 2.3 Electrophoresis ..............................................................................................37 2.3.1 Sodium dodecyl sulfate polyacrylamide gel electrophoresis 37 2.3.1 Agarose isoelectric focusing gel electrophoresis .......................... 38 2.4 SAMDC assay...............................................................................................40 2.4.1 Quantitative microassay .................................................................40 2.4.2 Qualitative microtiter plate assay .................................................. 43 2.4.3 Determination of pH optima ..........................................................44 2.4.4 Kinetic analysis ..............................................................................44 2.5 Physical structure analysis .............................................................................44 2.5.1 Determination of a-subunit size ..................................................... 44 2.5.2 N-terminal amino acid sequence determination ............................ 46 2.5.3 Tryptic peptide
Load more

Recommended publications
  • Histamine Degradation by Halophilic Archaea Wanaporn Tapingkae A
    Histamine Degradation by Halophilic Archaea Wanaporn Tapingkae A Thesis Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy in Food Technology Prince of Songkla University 2009 Copyright of Prince of Songkla University i Thesis Title Histamine Degradation by Halophilic Archaea Author Miss Wanaporn Tapingkae Major Program Food Technology Major Advisor Examining Committee : ……..…………………………………. ……..…………..…………….Chairperson (Dr. Wonnop Visessanguan) (Asst. Prof. Dr. Tipparat Hongpattarakere) ……..…………………..……………….… Co-advisors (Dr. Wonnop Visessanguan) ……..…………………………………. ……..…………………..……………….… (Prof. Dr. Soottawat Benjakul) (Prof. Dr. Soottawat Benjakul) ……..…………………………………. ……..…………………..……………….… (Prof. Dr. Kirk L. Parkin) (Assoc. Prof. Dr. Somboon Tanasupawat) ……..…………………..……………….… (Assoc. Prof. Dr. Borwonsak Leenanon) The Graduate School, Prince of Songkla University, has approved this thesis as partial fulfillment of the requirements for the Doctor of Philosophy Degree in Food Technology ………………………………………… (Assoc. Prof. Dr. Krerkchai Thongnoo) Dean of Graduate School ii ชือวทยานิ ิพนธ์ การยอยสลายฮ่ ีสตามีนโดยอาเคียที่ชอบเกลือ ผู้เขียน นางสาววรรณพร ทะพิงคแก์ สาขาวชาิ เทคโนโลยอาหารี ปี การศึกษา 2551 บทคดยั ่อ ปริมาณฮีสตามีนที่สูงก่อใหเก้ ิดผลเสียหายต่อทงคั ุณภาพและความปลอดภยของั นาปลาํ ดงนั นการทดลองนั ีจึงมีวตถั ุประสงคเพ์ ื่อคดแยกเชั ืออาเคียที่ชอบเกลือที่มีความสามารถยอย่ ฮีสตามีนในสภาวะที่มีเกลือสูง ศึกษาเอนไซมท์ ี่เกี่ยวของ้ และศึกษาความเป็นไปไดในการประย้ กตุ ์ ใชในกระบวนการผล้ ิตนาปลาํ จากเชืออาเคียที่ชอบเกลือ
    [Show full text]
  • Functional Characterization of Seven Γ-Glutamylpolyamine Synthetase
    JOURNAL OF BACTERIOLOGY, Aug. 2011, p. 3923–3930 Vol. 193, No. 15 0021-9193/11/$12.00 doi:10.1128/JB.05105-11 Copyright © 2011, American Society for Microbiology. All Rights Reserved. Functional Characterization of Seven ␥-Glutamylpolyamine Synthetase Genes and the bauRABCD Locus for Polyamine and ␤-Alanine Utilization in Pseudomonas aeruginosa PAO1ᰔ Xiangyu Yao,1† Weiqing He,1,2† and Chung-Dar Lu1,3* Department of Biology, Georgia State University, Atlanta, Georgia 303031; Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China2; and Department of Medical Laboratory Sciences and Biotechnology, China Medical University, Taichung, Taiwan 404023 Received 16 April 2011/Accepted 13 May 2011 Pseudomonas aeruginosa and many other bacteria can utilize biogenic polyamines, including diaminopropane (DAP), putrescine (Put), cadaverine (Cad), and spermidine (Spd), as carbon and/or nitrogen sources. Tran- scriptome analysis in response to exogenous Put and Spd led to the identification of a list of genes encoding putative enzymes for the catabolism of polyamines. Among them, pauA1 to pauA6, pauB1 to pauB4, pauC, and pauD1 and pauD2 (polyamine utilization) encode enzymes homologous to Escherichia coli PuuABCD of the ␥-glutamylation pathway in converting Put into GABA. A series of unmarked pauA mutants was constructed for growth phenotype analysis. The results revealed that it requires specific combinations of pauA knockouts to abolish utilization of different polyamines and support the importance of ␥-glutamylation for polyamine catabolism in P. aeruginosa. Another finding was that the list of Spd-inducible genes overlaps almost completely with that of Put-inducible ones except the pauA3B2 operon and the bauABCD operon (␤-alanine utilization).
    [Show full text]
  • Appl. Microbiol. Biotechnol. 78: 293-307
    Appl Microbiol Biotechnol (2008) 78:293–307 DOI 10.1007/s00253-007-1308-y APPLIED GENETICS AND MOLECULAR BIOTECHNOLOGY PA2663 (PpyR) increases biofilm formation in Pseudomonas aeruginosa PAO1 through the psl operon and stimulates virulence and quorum-sensing phenotypes Can Attila & Akihiro Ueda & Thomas K. Wood Received: 19 October 2007 /Revised: 26 November 2007 /Accepted: 28 November 2007 / Published online: 22 December 2007 # Springer-Verlag 2007 Abstract Previously, we identified the uncharacterized PA2130, and PA4549) and for small molecule transport predicted membrane protein PA2663 of Pseudomonas (PA0326, PA1541, PA1632, PA1971, PA2214, PA2215, aeruginosa PAO1 as a virulence factor using a poplar tree PA2678, and PA3407). Phenotype arrays also showed that model; PA2663 was induced in the poplar rhizosphere and, PA2663 represses growth on D-gluconic acid, D-mannitol, upon inactivation, it caused 20-fold lower biofilm forma- and N-phthaloyl-L-glutamic acid. Hence, the PA2663 gene tion (Attila et al., Microb Biotechnol, 2008). Here, we product increases biofilm formation by increasing the psl- confirmed that PA2663 is related to biofilm formation by operon-derived exopolysaccharides and increases pyover- restoring the wild-type phenotype by complementing the dine synthesis, PQS production, and elastase activity while PA2663 mutation in trans and investigated the genetic basis reducing swarming and swimming motility. We speculate of its influence on biofilm formation through whole- that PA2663 performs these myriad functions as a novel transcriptome and -phenotype studies. Upon inactivating membrane sensor. PA2663 by transposon insertion, the psl operon that encodes a galactose- and mannose-rich exopolysaccharide Keywords Biofilm . Pseudomonas aeruginosa . was highly repressed (verified by RT-PCR).
    [Show full text]
  • A Plant Spermine Oxidase/Dehydrogenase Regulated
    Journal of Experimental Botany, Vol. 65, No. 6, pp. 1585–1603, 2014 doi:10.1093/jxb/eru016 Advance Access publication 18 February, 2014 RESEARCH PAPER A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines Downloaded from https://academic.oup.com/jxb/article-abstract/65/6/1585/588180 by Divisione Coordinamento Biblioteche MI user on 10 June 2020 Abdellah Ahou1, Damiano Martignago1, Osama Alabdallah1, Raffaela Tavazza2, Pasquale Stano1, Alberto Macone3, Micaela Pivato4,5, Antonio Masi4, Jose L. Rambla6, Francisco Vera-Sirera6, Riccardo Angelini1, Rodolfo Federico1 and Paraskevi Tavladoraki1,* 1 Department of Science, University ‘ROMA TRE’, Rome, Italy 2 Italian National Agency for New Technologies, Energy and Sustainable Economic Development (ENEA), UTAGRI-INN C.R. Casaccia, Rome, Italy 3 Department of Biochemical Sciences ‘A. Rossi Fanelli’, University ‘La Sapienza’, Rome, Italy 4 DAFNAE, University of Padova, Legnaro, Italy 5 Proteomics Center of Padova University, Padova, Italy 6 Instituto de Biología Molecular y Celular de Plantas, UPV-CSIC, Valencia, Spain * To whom correspondence should be addressed. E-mail: [email protected] Received 31 October 2013; Revised 20 December 2013; Accepted 7 January 2014 Abstract Polyamine oxidases (PAOs) are flavin-dependent enzymes involved in polyamine catabolism. In Arabidopsis five PAO genes (AtPAO1–AtPAO5) have been identified which present some common characteristics, but also important dif- ferences in primary structure, substrate specificity, subcellular localization, and tissue-specific expression pattern, differences which may suggest distinct physiological roles. In the present work, AtPAO5, the only so far uncharac- terized AtPAO which is specifically expressed in the vascular system, was partially purified from 35S::AtPAO5-6His Arabidopsis transgenic plants and biochemically characterized.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • Homospermidine, Spermidine, and Putrescine: The
    AN ABSTRACT OF THE THESIS OF Paula Allene Tower for the degree of Doctor of Philosophy in Microbiology presented on July 28, 1987. Title: Homospermidine, Spermidine, and Putrescine: The Biosynthesis and Metabolism of Polyamines in Rhizobium meliloti Redacted for privacy Abstract approved: Dr.4dolph J. Ferro Rhizobium, in symbiotic association with leguminous plants, is able to fix atmospheric nitrogen after first forming root nodules. Since polyamines are associated with and found in high concentration in rapidly growing cells and are thought to be important foroptimal cell growth, it is possible that these polycations are involved in the extensive cell proliferation characteristic of the nodulation process. As a first step towards elucidating the role(s) of poly- amines in the rhizobial-legume interaction, I have characterized polyamine biosynthesis and metabolism in free-living Rhizobium meliloti. In addition to the detection of putrescine and spermidine, the presence of a less common polyamine, homospermidine, wasconfirmed in Rhizobium meliloti, with homospermidine comprising 79 percent of the free polyamines in this procaryote. The presence of an exogenous polyamine both affected the intra- cellular levels of each polyamine pool and inhibited the accumula- tion of a second amine. DL-a-Difluoromethylornithine (DFMO), an irreversible inhibitor of ornithine decarboxylase, wasfound to: (1) inhibit the rhizobial enzyme both in vitro and in vivo; (2) increase the final optical density; and (3) create ashift in the dominant polyamine from homospermidine to spermidine. A series of radiolabeled amino acids and polyamines were studied as polyamine precursors. Ornithine, arginine, aspartic acid, putrescine, and spermidine, but not methionine, resulted in the isolation of labeled putrescine, spermidine, andhomospermidine.
    [Show full text]
  • Ferritin and Iron Metabolism in Phycomyces
    MICROBIAL IRON METABOLISM A COMPREHENSIVE TREATISE Edited by J.B. Neilands DEPARTMENT OF BIOCHEMISTRY UNIVERSITY OF CALIFORNIA BERKELEY, CALIFORNIA ACADEMIC PRESS New York and London 1974 A Subsidiary of Harcourt Brace Jovanovich, Publishers CONTENTS List of Contributors xi Preface xv PART I INTRODUCTION Chapter 1. Iron and Its Role in Microbial Physiology /. B. Neüands I. Introduction 4 II. Historical Background 4 III. Biogeochemistry of Iron 5 IV. Some Physical and Chemical Properties of Iron 7 V. Iron Content of Microorganisms 16 VI. Iron Ligand Atoms in Microorganisms and Their Function 18 VII. Life without Iron and Functional Replacements for Iron 25 VIII. Aspects of the Comparative Biochemistry of Iron Metabolism 27 References 31 Chapter 2. Metabolism in Iron-Limited Growth P. Ann Light and Roger A. Clegg I. Introduction 35 II. Iron-Limited Growth 36 III. Practical Aspects of Iron Limitation 40 IV. Effects of Iron Deficiency and Iron Limitation 42 V. Summary 60 References 61 PART II TRANSPORT, BIOSYNTHESIS, AND STORAGE Chapter 3. Iron Transport in the Enteric Bacteria H. Rosenberg and I. G, Young I. Introduction 67 II. Iron Transport Systems in Eschenchia Colt 68 υ vi CONTENTS III. Iron Transport Systems in Aerobacter aerogenes 78 IV. Iron Transport Systems in Salmonella typhimurium 79 V. Discussion 80 References 81 Chapter 4. Iron Transport in Gram-Positive and Acid-Fast Bacilli B. R. Byers I. Introduction 83 II. Production of Iron-Chelating Agents by Bacillus Species 85 III. Iron Transport in Bacillus megaterium 87 IV. Iron Transport in Bacillus subtilis 98 V. Iron Transport in Mycobacterium smegmatis 100 VI.
    [Show full text]
  • Alternative Metabolic Routes in Channeling Xylose to Cordycepin Production of Cordyceps Militaris Identified by Comparative Transcriptome Analysis
    Genomics xxx (xxxx) xxx–xxx Contents lists available at ScienceDirect Genomics journal homepage: www.elsevier.com/locate/ygeno Alternative metabolic routes in channeling xylose to cordycepin production of Cordyceps militaris identified by comparative transcriptome analysis Boontariga Wongsaa, Nachon Raethongb, Pramote Chumnanpuena,c, Jirasak Wong-ekkabutc,d, ⁎ ⁎⁎ Kobkul Laotenge, , Wanwipa Vongsangnaka,f, a Department of Zoology, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand b Interdisciplinary Graduate Program in Bioscience, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand c Computational Biomodelling Laboratory for Agricultural Science and Technology (CBLAST), Faculty of Science, Kasetsart University, Bangkok 10900, Thailand d Department of Physics, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand e Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), Pathum Thani 12120, Thailand f Omics Center for Agriculture, Bioresources, Food, and Health, Faculty of Science, Kasetsart University (OmiKU), Bangkok 10900, Thailand ARTICLE INFO ABSTRACT Keywords: The responsive mechanism of C. militaris TBRC7358 on xylose utilization was investigated by comparative Cordyceps militaris analysis of transcriptomes, growth kinetics and cordycepin productions. The result showed that the culture Cordycepin grown on xylose exhibited high production yield of cordycepin on dry
    [Show full text]
  • Microbially Mediated Transformation of Dissolved Nitrogen in Aquatic Environments a Dissertation Submitted to Kent State Univers
    Microbially Mediated Transformation of Dissolved Nitrogen in Aquatic Environments A dissertation submitted to Kent State University in partial fulfillment of the requirements for the degree of Doctor of Philosophy by Xinxin Lu (Lucy) May 2015 © Copyright All rights reserved Except for previously published material Dissertation written by Xinxin Lu (Lucy) B.S., Jimei University, 2005 M.S., Ocean University of China, 2008 Ph.D., Kent State University, 2015 Approved by _______________________________________________________________ Xiaozhen Mou, Associate Professor, Ph.D., Department of Biological Sciences _______________________________________________________________ Laura G. Leff, Professor, Ph.D., Department of Biological Sciences _______________________________________________________________ Darren L. Bade, Assistant Professor, Ph.D., Department of Biological Sciences _______________________________________________________________ Joseph D. Ortiz, Professor, Ph.D., Department of Geology _______________________________________________________________ Scott Sheridan, Professor, Ph.D., Department of Geography Accepted by _______________________________________________________________ Laura G. Leff, Professor, Ph.D., Chair, Department of Biological Sciences _______________________________________________________________ James L. Blank, Professor, Ph.D., Dean, College of Arts and Sciences TABLE OF CONTENTS TABLE OF CONTENTS………………………………………………………………………...iii LIST OF FIGURES……………………………………………………………………………....vi LIST OF TABLES………………………………………………………………………………..xi
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur Et Al
    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
    [Show full text]
  • WO 2015/017866 Al 5 February 2015 (05.02.2015) P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2015/017866 Al 5 February 2015 (05.02.2015) P O P C T (51) International Patent Classification: Gregory, B. [US/US]; C/o 83 Cambridge Parkway, Cam C12N 15/63 (2006.01) C40B 40/06 (2006.01) bridge, MA 02142 (US). C12N 15/87 (2006.01) (74) Agents: ALTIERI, Stephen, L. et al; Bingham Mc- (21) International Application Number: cutchen LLP, 2020 K Street, NW, Washington, DC 20006- PCT/US20 14/049649 1806 (US). (22) International Filing Date: (81) Designated States (unless otherwise indicated, for every 4 August 2014 (04.08.2014) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (25) Filing Language: English BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, (26) Publication Language: English DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, (30) Priority Data: KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, 61/861,805 2 August 2013 (02.08.2013) US MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, 61/883,13 1 26 September 2013 (26.09.2013) US OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, 61/935,265 3 February 2014 (03.02.2014) US SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, 61/938,933 12 February 2014 (12.02.2014) US TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (71) Applicant: ENEVOLV, INC.
    [Show full text]