Springer Handbook of Enzymes

Total Page:16

File Type:pdf, Size:1020Kb

Springer Handbook of Enzymes Dietmar Schomburg Ida Schomburg (Eds.) Springer Handbook of Enzymes Alphabetical Name Index 1 23 © Springer-Verlag Berlin Heidelberg New York 2010 This work is subject to copyright. All rights reserved, whether in whole or part of the material con- cerned, specifically the right of translation, printing and reprinting, reproduction and storage in data- bases. The publisher cannot assume any legal responsibility for given data. Commercial distribution is only permitted with the publishers written consent. Springer Handbook of Enzymes, Vols. 1–39 + Supplements 1–7, Name Index 2.4.1.60 abequosyltransferase, Vol. 31, p. 468 2.7.1.157 N-acetylgalactosamine kinase, Vol. S2, p. 268 4.2.3.18 abietadiene synthase, Vol. S7,p.276 3.1.6.12 N-acetylgalactosamine-4-sulfatase, Vol. 11, p. 300 1.14.13.93 (+)-abscisic acid 8’-hydroxylase, Vol. S1, p. 602 3.1.6.4 N-acetylgalactosamine-6-sulfatase, Vol. 11, p. 267 1.2.3.14 abscisic-aldehyde oxidase, Vol. S1, p. 176 3.2.1.49 a-N-acetylgalactosaminidase, Vol. 13,p.10 1.2.1.10 acetaldehyde dehydrogenase (acetylating), Vol. 20, 3.2.1.53 b-N-acetylgalactosaminidase, Vol. 13,p.91 p. 115 2.4.99.3 a-N-acetylgalactosaminide a-2,6-sialyltransferase, 3.5.1.63 4-acetamidobutyrate deacetylase, Vol. 14,p.528 Vol. 33,p.335 3.5.1.51 4-acetamidobutyryl-CoA deacetylase, Vol. 14, 2.4.1.147 acetylgalactosaminyl-O-glycosyl-glycoprotein b- p. 482 1,3-N-acetylglucosaminyltransferase, Vol. 32, 3.5.1.29 2-(acetamidomethylene)succinate hydrolase, p. 287 Vol. 14,p.407 2.4.1.148 acetylgalactosaminyl-O-glycosyl-glycoprotein b- 2.8.3.8 acetate CoA-transferase, Vol. 39,p.497 1,6-N-acetylglucosaminyltransferase, Vol. 32, 2.7.2.1 acetate kinase, Vol. 37, p. 259 p. 293 2.7.2.12 acetate kinase (diphosphate), Vol. 37,p.358 2.4.1.226 N-acetylgalactosaminyl-proteoglycan 3-b-glucuro- 6.2.1.1 Acetate-CoA ligase, Vol. 2, p. 186 nosyltransferase, Vol. 32, p. 613 6.2.1.13 Acetate-CoA ligase (ADP-forming), Vol. 2, p. 267 1.2.1.38 N-acetyl-g-glutamyl-phosphate reductase, Vol. 20, 4.1.1.4 Acetoacetate decarboxylase, Vol. 3,p.23 p. 289 6.2.1.16 Acetoacetate-CoA ligase, Vol. 2,p.282 2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransfer- 3.1.2.11 acetoacetyl-CoA hydrolase, Vol. 9,p.505 ase, Vol. 33, p. 443 1.1.1.36 acetoacetyl-CoA reductase, Vol. 16, p. 328 3.5.1.33 N-acetylglucosamine deacetylase, Vol. 14, p. 422 3.1.2.9 S-acetoacetylhydrolipoate hydrolase, deleted entry, 2.7.1.59 N-acetylglucosamine kinase, Vol. 36, p. 135 Vol. 9,p.502 2.7.5.2 acetylglucosamine phosphomutase, transferred to 3.1.2.8 S-acetoacylglutathione hydrolase, deleted entry, in- EC 5.4.2.3, Vol. 37,p.618 cluded in EC 3.1.2.6, Vol. 9, p. 501 3.1.4.45 N-acetylglucosamine-1-phosphodiester N-acetyl- 1.1.1.5 acetoin dehydrogenase, Vol. 16,p.97 glucosaminidase, Vol. 11,p.208 5.1.2.4 Acetoin racemase, Vol. 1,p.85 3.5.1.25 N-acetylglucosamine-6-phosphate deacetylase, 2.2.1.4 acetoin-ribose-5-phosphate transaldolase, Vol. 29, Vol. 14,p.379 p. 194 3.1.6.14 N-acetylglucosamine-6-sulfatase, Vol. 11,p.316 4.1.1.5 Acetolactate decarboxylase, Vol. 3,p.29 5.3.1.11 Acetylglucosaminephosphate isomerase, deleted en- 5.4.99.3 2-Acetolactate mutase, Vol. 1,p.597 try, Vol. 1, p. 321 4.1.3.18 acetolactate synthase, Vol. 4, p. 116 3.2.1.50 a-N-acetylglucosaminidase, Vol. 13,p.18 2.2.1.6 acetolactate synthase, Vol. 29, p. 202 3.2.1.30 b-d-acetylglucosaminidase, deleted, included in EC 6.4.1.6 acetone carboxylase, Vol. S7, p. 657 3.2.1.52, Vol. 12, p. 493 4.1.2.37 Acetone-cyanhydrin lyase, Vol. 3,p.569 3.5.1.26 N4-(b-N-acetylglucosaminyl)-l-asparaginase, 3.1.1.54 acetoxybutynylbithiophene deacetylase, Vol. 9, Vol. 14,p.385 p. 353 2.4.1.141 N-acetylglucosaminyldiphosphodolichol N-acetyl- 3.5.1.85 (S)-N-acetyl-1-phenylethylamine hydrolase, glucosaminyltransferase, Vol. 32,p.252 Vol. 14,p.620 1.13.11.50 acetylacetone-cleaving enzyme, Vol. 25, p. 673 2.4.1.188 N-acetylglucosaminyldiphosphoundecaprenol glu- cosyltransferase, Vol. 32,p.457 3.1.1.80 acetylajmaline esterase, Vol. S5,p.20 3.1.1.71 acetylalkylglycerol acetylhydrolase, Vol. 9, p. 404 2.4.1.187 N-acetylglucosaminyldiphosphoundecaprenol N- d Vol. 32 2.7.1.9 acetylaminodeoxyglucose kinase, deleted, Vol. 35, acetyl-b- -mannosaminyltransferase, , p. 165 p. 454 3.5.1.21 N-acetyl-b-alanine deacetylase, Vol. 14, p. 360 2.4.1.38 b-N-acetylglucosaminylglycopeptide b-1,4-galac- 2.4.1.244 N-acetyl-b-glucosaminyl-glycoprotein 4-b-N-acet- tosyltransferase, Vol. 31, p. 353 ylgalactosaminyltransferase, Vol. S2, p. 201 3.1.1.69 N-acetylglucosaminylphosphatidylinositol deace- 2.6.1.65 N6-acetyl-b-lysine transaminase, Vol. 35,p.32 tylase, Vol. 9,p.400 3.1.1.7 acetylcholinesterase, Vol. 9,p.104 3.5.1.89 N-acetylglucosaminylphosphatidylinositol deace- 2.3.1.9 acetyl-CoA C-acetyltransferase, Vol. 29, p. 305 tylase, Vol. 14, p. 647 2.3.1.16 acetyl-CoA C-acyltransferase, Vol. 29, p. 371 2.4.1.225 N-acetylglucosaminyl-proteoglycan 4-b-glucuro- 6.4.1.2 Acetyl-CoA carboxylase, Vol. 2, p. 721 nosyltransferase, Vol. 32, p. 610 2.7.1.128 [acetyl-CoA carboxylase] kinase, Protein kinases 3.1.1.33 6-acetylglucose deacetylase, Vol. 9,p.264 are in a state of review by the NC-IUBMB. This EC 2.7.2.8 acetylglutamate kinase, Vol. 37, p. 342 class will presumably be transferred to EC 2.7.11.4, 1.1.1.240 N-acetylhexosamine 1-dehydrogenase, Vol. 18, Vol. 37,p.123 p. 390 2.7.1.111 acetyl-CoA carboxylase] kinase, transferred to EC 3.2.1.52 b-N-acetylhexosaminidase, Vol. 13,p.50 2.7.1.128, Vol. 36,p.483 3.5.1.34 acetylhistidine deacetylase, deleted, same as EC 2.7.11.27 [acetyl-CoA carboxylase] kinase, Vol. S4,p.326 3.4.13.5, Vol. 14, p. 425 3.1.3.44 [acetyl-CoA carboxylase]-phosphatase, Vol. 10, 4.2.99.10 O-acetylhomoserine (thiol)-lyase, Vol. 5,p.120 p. 389 2.5.1.49 O-acetylhomoserine aminocarboxypropyltransfer- 2.3.1.155 acetyl-CoA C-myristoyltransferase, Vol. 30,p.414 ase, Vol. 34, p. 122 3.1.2.1 acetyl-CoA hydrolase, Vol. 9, p. 450 1.7.3.2 acetylindoxyl oxidase, Vol. 24, p. 344 3.5.1.47 N-acetyldiaminopimelate deacetylase, Vol. 14, 2.4.1.90 N-acetyllactosamine synthase, Vol. 32,p.1 p. 471 2.4.1.151 N-acetyllactosaminide a-1,3-galactosyltransferase, 4.2.1.112 acetylene hydratase, Vol. S7, p. 118 transferred to EC 2.4.1.87, Vol. 32,p.317 4.2.1.71 Acetylenecarboxylate hydratase, Vol. 4, p. 584 2.4.99.6 N-acetyllactosaminide a-2,3-sialyltransferase, 4.1.1.78 acetylenedicarboxylate decarboxylase, Vol. S7,p.1 Vol. 33,p.361 4.2.1.72 Acetylenedicarboxylate hydratase, Vol. 4,p.587 2.4.1.149 N-acetyllactosaminide b-1,3-N-acetylglucosami- 3.1.1.6 acetylesterase, Vol. 9,p.96 nyltransferase, Vol. 32, p. 297 2.8.2.33 N-acetylgalactosamine 4-sulfate 6-O-sulfotransfer- 2.4.1.150 N-acetyllactosaminide b-1,6-N-acetylglucosami- ase, Vol. S4, p. 489 nyl-transferase, Vol. 32,p.307 Springer Handbook of Enzymes # Springer Verlag Berlin Heidelberg 2001–2010 1 Springer Handbook of Enzymes, Vols. 1–39 + Supplements 1–7, Name Index 3.4.19.4 N-acetylmethionylpeptide peptidase, deleted entry, 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, Vol. 6,p.545 Vol. 29,p.566 3.5.1.28 N-acetylmuramoyl-l-alanine amidase, Vol. 14, 1.3.99.3 acyl-CoA dehydrogenase, Vol. 21,p.488 p. 396 1.3.2.2 acyl-CoA dehydrogenase, transferred to EC 1.3.99.3, 2.3.1.44 N-acetylneuraminate 4-O-acetyltransferase, Vol. 21,p.341 Vol. 29,p.622 1.3.1.8 acyl-CoA dehydrogenase (NADP+), Vol. 21,p.34 2.3.1.45 N-acetylneuraminate 7-O(or 9-O)-acetyltransfer- 3.1.2.20 acyl-CoA hydrolase, Vol. 9, p. 539 ase, Vol. 29, p. 625 1.3.3.6 acyl-CoA oxidase, Vol. 21, p. 401 2.4.99.8 a-N-acetylneuraminate a-2,8-sialyltransferase, 3.5.1.81 N-acyl-d-amino-acid deacylase, Vol. 14,p.603 Vol. 33,p.371 3.5.1.83 N-acyl-d-aspartate deacylase, Vol. 14, p. 614 4.1.3.3 N-acetylneuraminate lyase, Vol. 4,p.24 3.5.1.82 N-acyl-d-glutamate deacylase, Vol. 14,p.610 4.1.3.19 N-acetylneuraminate synthase, Vol. 4, p. 131 5.1.3.8 N-Acylglucosamine 2-epimerase, Vol. 1, p. 140 2.5.1.56 N-acetylneuraminate synthase, Vol. 34, p. 184 5.1.3.9 N-Acylglucosamine-6-phosphate 2-epimerase, 4.1.3.20 N-Acetylneuraminate-9-phosphate synthase, Vol. 1,p.144 Vol. 4,p.135 2.7.1.94 acylglycerol kinase, Vol. 36,p.368 2.4.99.7 a-N-acetylneuraminyl-2,3-b-galactosyl-1,3-N-acet- 3.1.1.23 acylglycerol lipase, Vol.
Recommended publications
  • METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
    Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0.
    [Show full text]
  • Thesis, Dissertation
    THE COENZYME M BIOSYNTHETIC PATHWAY IN PROTEOBACTERIUM XANTHOBACTER AUTOTROPHICUS PY2 by Sarah Eve Partovi A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry MONTANA STATE UNIVERSITY Bozeman, Montana January 2018 ©COPYRIGHT by Sarah Eve Partovi 2018 All Rights Reserved ii DEDICATION I dedicate this dissertation to my family, without whom none of this would have been possible. My husband Ky has been a part of the graduate school experience since day one, and I am forever grateful for his support. My wonderful family; Iraj, Homa, Cameron, Shireen, Kevin, Lin, Felix, Toby, Molly, Noise, Dooda, and Baby have all been constant sources of encouragement. iii ACKNOWLEDGEMENTS First, I would like to acknowledge Dr. John Peters for his mentorship, scientific insight, and for helping me gain confidence as a scientist even during the most challenging aspects of this work. I also thank Dr. Jennifer DuBois for her insightful discussions and excellent scientific advice, and my other committee members Dr. Brian Bothner and Dr. Matthew Fields for their intellectual contributions throughout the course of the project. Drs. George Gauss and Florence Mus have contributed greatly to my laboratory technique and growth as a scientist, and have always been wonderful resources during my time in the lab. Members of the Peters Lab past and present have all played an important role during my time, including Dr. Oleg Zadvornyy, Dr. Jacob Artz, and future Drs. Gregory Prussia, Natasha Pence, and Alex Alleman. Undergraduate researchers/REU students including Hunter Martinez, Andrew Gutknecht and Leah Connor have worked under my guidance, and I thank them for their dedication to performing laboratory assistance.
    [Show full text]
  • Review: Microbial Transformations of Human Bile Acids Douglas V
    Guzior and Quinn Microbiome (2021) 9:140 https://doi.org/10.1186/s40168-021-01101-1 REVIEW Open Access Review: microbial transformations of human bile acids Douglas V. Guzior1,2 and Robert A. Quinn2* Abstract Bile acids play key roles in gut metabolism, cell signaling, and microbiome composition. While the liver is responsible for the production of primary bile acids, microbes in the gut modify these compounds into myriad forms that greatly increase their diversity and biological function. Since the early 1960s, microbes have been known to transform human bile acids in four distinct ways: deconjugation of the amino acids glycine or taurine, and dehydroxylation, dehydrogenation, and epimerization of the cholesterol core. Alterations in the chemistry of these secondary bile acids have been linked to several diseases, such as cirrhosis, inflammatory bowel disease, and cancer. In addition to the previously known transformations, a recent study has shown that members of our gut microbiota are also able to conjugate amino acids to bile acids, representing a new set of “microbially conjugated bile acids.” This new finding greatly influences the diversity of bile acids in the mammalian gut, but the effects on host physiology and microbial dynamics are mostly unknown. This review focuses on recent discoveries investigating microbial mechanisms of human bile acids and explores the chemical diversity that may exist in bile acid structures in light of the new discovery of microbial conjugations. Keywords: Bile acid, Cholic acid, Conjugation, Microbiome, Metabolism, Microbiology, Gut health, Clostridium scindens, Enterocloster bolteae Introduction the development of healthy or diseased states. For The history of bile example, abnormally high levels of the microbially modi- Bile has been implicated in human health for millennia.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2013/0089535 A1 Yamashiro Et Al
    US 2013 0089535A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2013/0089535 A1 Yamashiro et al. (43) Pub. Date: Apr. 11, 2013 (54) AGENT FOR REDUCING ACETALDEHYDE Publication Classification NORAL CAVITY (51) Int. Cl. (75) Inventors: Kan Yamashiro, Kakamigahara-shi (JP); A68/66 (2006.01) Takahumi Koyama, Kakamigahara-shi A638/51 (2006.01) (JP) A61O 11/00 (2006.01) A638/44 (2006.01) Assignee: AMANOENZYME INC., Nagoya-shi (52) U.S. Cl. (73) CPC. A61K 8/66 (2013.01); A61K 38/44 (2013.01); (JP) A61 K38/51 (2013.01); A61O II/00 (2013.01) (21) Appl. No.: 13/703,451 USPC .......... 424/94.4; 424/94.5; 435/191: 435/232 (22) PCT Fled: Jun. 7, 2011 (57) ABSTRACT Disclosed herein is a novel enzymatic agent effective in (86) PCT NO.: PCT/UP2011/062991 reducing acetaldehyde in the oral cavity. It has been found S371 (c)(1), that an aldehyde dehydrogenase derived from a microorgan (2), (4) Date: Dec. 11, 2012 ism belonging to the genus Saccharomyces and a threonine aldolase derived from Escherichia coli are effective in reduc (30) Foreign Application Priority Data ing low concentrations of acetaldehyde. Therefore, an agent for reducing acetaldehyde in the oral cavity is provided, Jun. 19, 2010 (JP) ................................. 2010-140O26 which contains these enzymes as active ingredients. Patent Application Publication Apr. 11, 2013 Sheet 1 of 2 US 2013/0089535 A1 FIG 1) 10.5 1 0 9.9.5 8. 5 CONTROL TA AD (BSA) ENZYME Patent Application Publication Apr. 11, 2013 Sheet 2 of 2 US 2013/0089535 A1 FIG 2) 110 the CONTROL (BSA) 100 354.
    [Show full text]
  • Katalog 2015 Cover Paul Lin *Hinweis Förderung.Indd
    Product List 2015 WE LIVE SERVICE Certificates quartett owns two productions sites that are certified according to EN ISO 9001:2008 Quality management systems - Requirements EN ISO 13485:2012 + AC:2012 Medical devices - Quality management systems - Requirements for regulatory purposes GMP Conformity Our quality management guarantees products of highest quality! 2 Foreword to the quartett product list 2015 quartett Immunodiagnostika, Biotechnologie + Kosmetik Vertriebs GmbH welcomes you as one of our new business partners as well as all of our previous loyal clients. You are now member of quartett´s worldwide customers. First of all we would like to introduce ourselves to you. Founded as a family-run company in 1986, quartett ensures for more than a quarter of a century consistent quality of products. Service and support of our valued customers are our daily businesses. And we will continue! In the end 80´s quartett offered radioimmunoassay and enzyme immunoassay kits from different manufacturers in the USA. In the beginning 90´s the company changed its strategy from offering products for routine diagnostic to the increasing field of research and development. Setting up a production plant in 1997 and a second one in 2011 supported this decision. The company specialized its product profile in the field of manufacturing synthetic peptides for antibody production, peptides such as protease inhibitors, biochemical reagents and products for histology, cytology and immunohistology. All products are exclusively manufactured in Germany without outsourcing any production step. Nowadays, we expand into all other diagnostic and research fields and supply our customers in universities, government institutes, pharmaceutical and biotechnological companies, hospitals, and private doctor offices.
    [Show full text]
  • Mapping Active Site Residues in Glutamate-5-Kinase. the Substrate Glutamate and the Feed-Back Inhibitor Proline Bind at Overlapping Sites
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 580 (2006) 6247–6253 Mapping active site residues in glutamate-5-kinase. The substrate glutamate and the feed-back inhibitor proline bind at overlapping sites Isabel Pe´rez-Arellanoa, Vicente Rubiob, Javier Cerveraa,* a Centro de Investigacio´n Prı´ncipe Felipe, Avda. Autopista del Saler, 16, Valencia 46013, Spain b Instituto de Biomedicina de Valencia (IBV-CSIC), Jaime Roig 11, Valencia 46010, Spain Received 22 August 2006; revised 10 October 2006; accepted 12 October 2006 Available online 20 October 2006 Edited by Stuart Ferguson (a domain named after pseudo uridine synthases and archaeo- Abstract Glutamate-5-kinase (G5K) catalyzes the controlling first step of proline biosynthesis. Substrate binding, catalysis sine-specific transglycosylases) domain [10]. AAK domains and feed-back inhibition by proline are functions of the N-termi- bind ATP and a phosphorylatable acidic substrate, and make nal 260-residue domain of G5K. We study here the impact on a phosphoric anhydride [11]. The function of the PUA domain these functions of 14 site-directed mutations affecting 9 residues (a domain characteristically found in some RNA-modifying of Escherichia coli G5K, chosen on the basis of the structure of enzymes) [12] is not known. By deleting the PUA domain of the bisubstrate complex of the homologous enzyme acetylgluta- E. coli G5K we showed [10] that the isolated AAK domain, mate kinase (NAGK). The results support the predicted roles as the complete enzyme, forms tetramers, catalyzes the reac- of K10, K217 and T169 in catalysis and ATP binding and of tion and is feed-back inhibited by proline.
    [Show full text]
  • Advances in Chitin/Chitosan Characterization and Applications
    Advances in Chitin/Chitosan Characterization and Applications Edited by Marguerite Rinaudo and Francisco M. Goycoolea Printed Edition of the Special Issue Published in Polymers www.mdpi.com/journal/polymers Advances in Chitin/Chitosan Characterization and Applications Advances in Chitin/Chitosan Characterization and Applications Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea University of Grenoble Alpes University of Leeds France UK Editorial Office MDPI St. Alban-Anlage 66 4052 Basel, Switzerland This is a reprint of articles from the Special Issue published online in the open access journal Polymers (ISSN 2073-4360) from 2017 to 2018 (available at: https://www.mdpi.com/journal/polymers/ special issues/chitin chitosan) For citation purposes, cite each article independently as indicated on the article page online and as indicated below: LastName, A.A.; LastName, B.B.; LastName, C.C. Article Title. Journal Name Year, Article Number, Page Range. ISBN 978-3-03897-802-2 (Pbk) ISBN 978-3-03897-803-9 (PDF) c 2019 by the authors. Articles in this book are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book as a whole is distributed by MDPI under the terms and conditions of the Creative Commons license CC BY-NC-ND. Contents About the Special Issue Editors ..................................... ix Preface to ”Advances in Chitin/Chitosan Characterization and Applications” .........
    [Show full text]
  • Recombinant Escheichia Coli-Catalyzed Production of Cytidine 5′-Triphosphate from Cytidine 5′-Monophosphate
    J. Ind. Eng. Chem., Vol. 12, No. 5, (2006) 757-761 Recombinant Escheichia coli-Catalyzed Production of Cytidine 5′-Triphosphate from Cytidine 5′-Monophosphate Sun-Gu Lee† and Byung-Gee Kim* Department of Chemical and Biochemical Engineering, Pusan National University, Busan 609-735, Korea *School of Chemical Engineering, and Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea Received April 24, 2006; Accepted May 22, 2006 Abstract: A recombinant Escherichia coli overexpressing CMP-kinase was constructed and employed as a whole cell biocatalyst for the conversion of cytidine 5′-monophosphate to cytidine 5′-triphosphate. In the whole cell biocatalysis, recombinant CMP kinase catalyzed the conversion of CMP to CDP, and endogenous acetate kinase of the E. coli was utilized for the ATP regeneration as well as for the conversion of CDP to CTP. A conversion yield of ca. 88 % CTP was obtained when starting with 20 mM CMP, 1 mM ATP, and 80 mM acetyl phosphate based on the initial CMP concentration. Endogenous pyruvate kinase and poly- phosphate kinase were inefficient in the process. The CTP production system was applied to the production of CMP-NeuAc by additionally introducing the CMP-NeuAc synthetase gene into the recombinant E. coli. Keywords: CMP-kinase, whole cell biocatalysis, ATP regeneration, cytidine 5′-monophosphate Introduction employing enzymes [4]. They applied various enzymatic 1) methods and chemical methods and concluded that the As glycosyltransferase-catalyzed synthetic techniques enzymatic method based on adenylate kinase/pyruvate are becoming recognized as powerful methods for the kinase provided the most convenient route to CTP. In the preparation of biologically important oligosaccharides, process, CTP was generated efficiently from an inexpen- the development of cost-efficient production methods for sive substrate, CMP.
    [Show full text]
  • A Genetic and Developmental Analysis of Dnase-1, an Acid Deoxyribonuclease in Droso~Hila Melano~Aster
    A GENETIC AND DEVELOPMENTAL ANALYSIS OF DNASE-1, AN ACID DEOXYRIBONUCLEASE IN DROSOPHILA MEL~NOGASTER A Thesis Presented to the Faculty of the Graduate School in Partial Fulfillment for the Degree of Doctor of Philosophy by Charles Roger Detwiler Hay, 1979 BIOGRAPHICAL SKETCH Charles R. Detwiler was born on December 15, 1950 in Norristown, Pennsylvania. He attended Collegeville-Trappe High School in Trappe, Pennsylvania from 1964 to 1968; Houghton College in Houghton, New York from 1968 to 1972 (B.S., Zoology); Buc~~ell University in Lewisburg, Pennsylvania from 1972 to 1974 (M.S., Biology); and Cornell University in Ithaca, New York from 1974 to 1979 (Ph.D., 1979). At Cornell he was a National Institutes of Health Genetics Trainee. He is a member of the Genetics Society of America, the American Scientific Afffiliation, and of Phi Sigma, the National Honorary Biology Society. ii - To the Designer of the fly iii ACKNOWLEDGMENTS I would like to thank all my friends 1-rho by their moral support or careful critical attention contributed to the completion of this work. First, I would like to thank my major professor, Dr. Ross MacIntyre, for his patience, generosity, and valuable ideas. I would like to thank Dr. Richard Halberg and Dr. Bruce "\{allace for their helpful comments and criticisms 1-li th regard to the thesis project. I would like to thank Margaret Dean for tireless reassurances and valuable tecrillical assistance especially at the begLnning. Lastly, Beverly my wife is aCYil101-Iledged. It would be absurd to "thank" her. Her patience and devotion have served both in brlllging these pages together, and in keeping hw people together in one beautiful relationship.
    [Show full text]
  • 1471-2164-15-164.Pdf
    Meinhardt et al. BMC Genomics 2014, 15:164 http://www.biomedcentral.com/1471-2164/15/164 RESEARCH ARTICLE Open Access Genome and secretome analysis of the hemibiotrophic fungal pathogen, Moniliophthora roreri, which causes frosty pod rot disease of cacao: mechanisms of the biotrophic and necrotrophic phases Lyndel W Meinhardt1*, Gustavo Gilson Lacerda Costa2, Daniela PT Thomazella3, Paulo José PL Teixeira3, Marcelo Falsarella Carazzolle2, Stephan C Schuster4, John E Carlson5, Mark J Guiltinan6, Piotr Mieczkowski7, Andrew Farmer8, Thiruvarangan Ramaraj8, Jayne Crozier9, Robert E Davis10, Jonathan Shao10, Rachel L Melnick1, Gonçalo AG Pereira3 and Bryan A Bailey1 Abstract Background: The basidiomycete Moniliophthora roreri is the causal agent of Frosty pod rot (FPR) disease of cacao (Theobroma cacao), the source of chocolate, and FPR is one of the most destructive diseases of this important perennial crop in the Americas. This hemibiotroph infects only cacao pods and has an extended biotrophic phase lasting up to sixty days, culminating in plant necrosis and sporulation of the fungus without the formation of a basidiocarp. Results: We sequenced and assembled 52.3 Mb into 3,298 contigs that represent the M. roreri genome. Of the 17,920 predicted open reading frames (OFRs), 13,760 were validated by RNA-Seq. Using read count data from RNA sequencing of cacao pods at 30 and 60 days post infection, differential gene expression was estimated for the biotrophic and necrotrophic phases of this plant-pathogen interaction. The sequencing data were used to develop a genome based secretome for the infected pods. Of the 1,535 genes encoding putative secreted proteins, 1,355 were expressed in the biotrophic and necrotrophic phases.
    [Show full text]
  • Transcriptional Regulation of the Acetone Carboxylase Operon Via Two-Component Signal Transduction in Helicobacter Pylori
    W&M ScholarWorks Undergraduate Honors Theses Theses, Dissertations, & Master Projects 7-2012 Transcriptional Regulation of the Acetone Carboxylase Operon via Two-Component Signal Transduction in Helicobacter pylori Samuel Emerson Harvey College of William and Mary Follow this and additional works at: https://scholarworks.wm.edu/honorstheses Part of the Biology Commons Recommended Citation Harvey, Samuel Emerson, "Transcriptional Regulation of the Acetone Carboxylase Operon via Two- Component Signal Transduction in Helicobacter pylori" (2012). Undergraduate Honors Theses. Paper 471. https://scholarworks.wm.edu/honorstheses/471 This Honors Thesis is brought to you for free and open access by the Theses, Dissertations, & Master Projects at W&M ScholarWorks. It has been accepted for inclusion in Undergraduate Honors Theses by an authorized administrator of W&M ScholarWorks. For more information, please contact [email protected]. Transcriptional Regulation of the Acetone Carboxylase Operon via Two- Component Signal Transduction in Helicobacter pylori A thesis submitted in partial fulfillment of the requirement for the degree of Bachelor of Science in Biology from The College of William & Mary By Samuel Emerson Harvey Accepted for ____________________________ (Honors) _______________________________________ Dr. Mark Forsyth, Chair _______________________________________ Dr. Oliver Kerscher _______________________________________ Dr. Kurt Williamson _______________________________________ Dr. Randolph Coleman Williamsburg, VA April 30, 2012 Abstract Helicobacter pylori is a gram negative gastric pathogen that infects the mucosal lining of the human stomach and is present is nearly half of the human population. H. pylori is the etiologic agent of peptic ulcer disease, and infection is highly associated with the development of gastric cancer. The H. pylori genome encodes three complete two- component signal transduction systems (TCSTs): ArsRS, CrdRS, and FlgRS.
    [Show full text]
  • Quantum Chemical Cluster Modeling of Enzymatic Reactions Rong-Zhen
    Quantum Chemical Cluster Modeling of Enzymatic Reactions Rong-Zhen Liao 1 Rong-Zhen Liao, Stockholm, 2010 ISBN 978-91-7447-129-8 Printed in Sweden by US-AB, Stockholm 2010 Distributor: Department of Organic Chemistry, Stockholm University 2 3 4 Abstract The Quantum chemical cluster approach has been shown to be quite powerful and efficient in the modeling of enzyme active sites and reaction mechanisms. In this thesis, the reaction mechanisms of several enzymes have been investigated using the hybrid density functional B3LYP. The enzymes studied include four dinuclear zinc enzymes, namely dihydroorotase, N-acyl-homoserine lactone hydrolase, RNase Z, and human renal dipeptidase, two trinuclear zinc enzymes, namely phospholipase C and nuclease P1, two tungstoenzymes, namely formaldehyde ferredoxin oxidoreductase and acetylene hydratase, aspartate α-decarboxylase, and mycolic acid cyclopropane synthase. The potential energy profiles for various mechanistic scenarios have been calculated and analyzed. The role of the metal ions as well as important active site residues has been discussed. In the cluster approach, the effects of the parts of the enzyme that are not explicitly included in the model are taken into account using implicit solvation methods. With aspartate α-decarboxylase as an example, systematic evaluation of the solvation effects with the increase of the model size has been performed. At a model size of 150-200 atoms, the solvation effects almost vanish and the choice of the dielectric constant becomes rather insignificant. For all six zinc-dependent enzymes studied, the di-zinc bridging hydroxide has been shown to be capable of performing nucleophilic attack on the substrate. In addition, one, two, or even all three zinc ions participate in the stabilization of the negative charge in the transition states and intermediates, thereby lowering the barriers.
    [Show full text]