DOCSLIB.ORG

Structure and Biochemistry of Polyunsaturated Fatty Acid Double Bond Isomerase from Propionibacterium Acnes

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Structure and Biochemistry of Polyunsaturated Fatty Acid Double Bond Isomerase from Propionibacterium Acnes Structure and biochemistry of polyunsaturated fatty acid double bond isomerase from Propionibacterium acnes PhD Thesis In partial fulfillment of the requirements for the degree “Doctor of Philosophy (PhD)” in the Molecular Biology Program at the Georg August University Göttingen, Faculty of Biology Submitted by Alena Liavonchanka Born in Vysoki Borak, Belarus 2007 Affidavit Hereby I declare that my thesis entitled “Structure and biochemistry of polyunsaturated fatty acid double bond isomerase from Propionibacterium acnes” has been written independently and with no other sources and aids than quoted. Alena Liavonchanka Göttingen, 28.09.2007 2 To all my teachers 3 List of publications Liavonchanka, A., and Feussner, I. (2006) Lipoxygenases: occurrence, functions and catalysis. J Plant Physiol 163, 348-357. Liavonchanka, A., Hornung, E., Feussner, I., and Rudolph, M. (2006) In-house SIRAS phasing of the polyunsaturated fatty-acid isomerase from Propionibacterium acnes. Acta Crystallograph Sect F Struct Biol Cryst Commun 62, 153-156. Liavonchanka, A., Hornung, E., Feussner, I., and Rudolph, M. G. (2006) Structure and mechanism of the Propionibacterium acnes polyunsaturated fatty acid isomerase. Proc Natl Acad Sci U S A 103, 2576-2581. 4 Table of contents Acknowledgements............................................................................................................. 7 Abstract............................................................................................................................... 9 1. Introduction................................................................................................................... 10 1.1 Physiological action of CLA and possible mechanisms............................................. 11 1.2 Biosynthesis of CLA................................................................................................... 15 1.3 Comparative analysis of enzymatic mechanisms involved in carbon-carbon double bond isomerization and conjugated PUFA synthesis........................................................ 22 1.4 Aim of the work.......................................................................................................... 32 2. Materials and methods .................................................................................................. 33 2.1 Chemicals.................................................................................................................... 33 2.2 Recombinant DNA...................................................................................................... 33 2.3 PCR based mutagenesis .............................................................................................. 34 2.4 Bacterial growth.......................................................................................................... 34 2.5 Protein solubility analysis and activity test................................................................. 35 2.6 Protein purification ..................................................................................................... 35 2.6.1 Affinity chromatography on Glutathione Sepharose ............................................... 35 2.6.2 Ni2+ affinity chromatography................................................................................... 36 2.6.3 Ion exchange chromatography on Source 30Q Sepharose ...................................... 36 2.6.4 SDS-PAGE analysis of protein fractions................................................................. 36 2.7 Immunoblotting........................................................................................................... 37 2.8 Spectroscopic assays................................................................................................... 37 2.9 Crystallization............................................................................................................. 37 2.9.1 Preliminary screening .............................................................................................. 37 2.9.2 Optimized conditions for PAI crystallization .......................................................... 38 2.10 Data collection, structure determination and refinement.......................................... 38 2.11 GC and GC-MS analysis of lipids ............................................................................ 39 2.11.1 Extraction and derivatization of lipids................................................................... 39 2.11.2 GC and GC-MS analysis of lipids ......................................................................... 40 2.12 HPLC analysis of FA................................................................................................ 40 2.13 Kinetic measurements............................................................................................... 41 2.14 Cofactor exchange .................................................................................................... 41 2.15 Anaerobic photoreduction and redox potential measurement .................................. 42 5 2.17 MALDI TOF analysis............................................................................................... 42 3. Results........................................................................................................................... 45 3.1 PAI structure ............................................................................................................... 45 3.1.1 PAI purification and biochemical properties ........................................................... 45 3.1.2 Crystallization, data collection, structure determination, and refinement ............... 45 3.1.3 Structure of PAI and PAI-CLA complex................................................................. 50 3.1.3.1 Overall structure description of free PAI.............................................................. 50 3.1.3.2 FAD cofactor ........................................................................................................ 52 3.1.3.3 Structure of PAI-CLA and PAI-CLnA complexes ............................................... 53 3.1.3.4 Gating mechanism for substrate entry .................................................................. 56 3.2 PAI reaction mechanism............................................................................................. 58 3.2.1 Structure-based mechanism of FA isomerization.................................................... 58 3.2.2 Hydrogen transfer during LA isomerization............................................................ 61 3.2.3 Active site engineering by site-directed mutagenesis.............................................. 64 3.2.4 Enzyme-substrate complex formation, anaerobic reduction, cofactor exchange .... 66 3.3 FA hydratase from Streptococcus pyogenes (SPH).................................................... 70 3.3.1 Cloning, purification and spectral properties........................................................... 70 3.3.2 SPH produces hydroxy FA species.......................................................................... 73 3.4 (9Z,11E)-CLA producing FA isomerases................................................................... 78 3.4.1 Bifidobacterium breve isomerase (BBI) .................................................................. 78 4. Discussion..................................................................................................................... 81 4.1. PAI structure and reaction mechanism ...................................................................... 81 4.2. Putative bifunctional FA hydratases-isomerases ....................................................... 90 5. Summary and conclusions ............................................................................................ 94 6. Supplementary material. ............................................................................................... 96 7. References................................................................................................................... 107 8. Abbreviations.............................................................................................................. 118 9. Curriculum vitae ......................................................................................................... 120 6 List of figures Fig. 1 Structures of LA, (9Z,11E)-CLA and (10E,12Z)-CLA. ......................................... 11 Fig. 2 Possible mechanisms of CLA action...................................................................... 14 Fig. 3 Structures of EPA and conjugated triene product produced by PFI....................... 18 Fig. 4 Scheme of LA conversion to hydroxy FAs by Lactobacillus sp............................ 19 Fig.5 The routes of LA metabolism in anaerobic bacteria of human gut. ........................ 21 Fig. 6 Schematic overview of enzymatic mechanisms for carbon-carbon double bond isomerization............................................................................................................. 23 Fig. 7 Reaction mechanism of IDI type 1......................................................................... 24 Fig. 8 Scheme of proposed CTI reaction mechanism....................................................... 25 Fig. 9 Reaction mechanism of ECI................................................................................... 26 Fig. 10 The reaction mechanism of KSI. .......................................................................... 27 Fig. 11 Analysis of active
Load more

Recommended publications
  • (12) United States Patent (10) Patent No.: US 8,530,724 B2 Whitelaw Et Al
    US008530724B2 (12) United States Patent (10) Patent No.: US 8,530,724 B2 Whitelaw et al. (45) Date of Patent: Sep. 10, 2013 (54) ALTERING THE FATTY ACID COMPOSITION 2011/0054198 A1 3/2011 Singh et al. OF RICE 2011/O190521 A1 8/2011 Damcevski et al. 2011/02O1065 A1 8/2011 Singh et al. 2011/02233.11 A1 9, 2011 Liu et al. (75) Inventors: Ella Whitelaw, Albury (AU); Sadequr 2011/0229623 A1 9, 2011 Liu et al. Rahman, Nicholls (AU); Zhongyi Li, 2012/0041218 A1 2/2012 Singh et al. Kaleen (AU); Qing Liu, Girralang (AU); Surinder Pal Singh, Downer (AU): FOREIGN PATENT DOCUMENTS WO WO99,049050 9, 1999 Robert Charles de Feyter, Monash WO WOO3,080802 10, 2003 (AU) WO WO 2003/080802 A2 10/2003 WO WO 2004/001001 12/2003 (73) Assignee: Commonwealth Scientific and WO WO 2004/001001 A2 12/2003 Industrial Research Organisation, WO WO 2008/O25068 6, 2008 Campbell (AU) WO WO 2009/12958 10/2009 WO WO 2010/009:500 1, 2010 (*) Notice: Subject to any disclaimer, the term of this WO WO 2010/057246 5, 2010 patent is extended or adjusted under 35 OTHER PUBLICATIONS U.S.C. 154(b) by 772 days. Supplementary European Search Report issued Feb. 23, 2010 in connection with corresponding European Patent Application No. (21) Appl. No.: 12/309.276 0776.37759. Taira et al. (1989) “Fatty Acid Composition of Indica-Types and (22) PCT Filed: Jul. 13, 2007 Japonica-Types of Rice Bran and Milled Rice' Journal of the Ameri can Oil Chemists’ Society; vol.
    [Show full text]
  • Supplementary Table 9. Functional Annotation Clustering Results for the Union (GS3) of the Top Genes from the SNP-Level and Gene-Based Analyses (See ST4)
    Supplementary Table 9. Functional Annotation Clustering Results for the union (GS3) of the top genes from the SNP-level and Gene-based analyses (see ST4) Column Header Key Annotation Cluster Name of cluster, sorted by descending Enrichment score Enrichment Score EASE enrichment score for functional annotation cluster Category Pathway Database Term Pathway name/Identifier Count Number of genes in the submitted list in the specified term % Percentage of identified genes in the submitted list associated with the specified term PValue Significance level associated with the EASE enrichment score for the term Genes List of genes present in the term List Total Number of genes from the submitted list present in the category Pop Hits Number of genes involved in the specified term (category-specific) Pop Total Number of genes in the human genome background (category-specific) Fold Enrichment Ratio of the proportion of count to list total and population hits to population total Bonferroni Bonferroni adjustment of p-value Benjamini Benjamini adjustment of p-value FDR False Discovery Rate of p-value (percent form) Annotation Cluster 1 Enrichment Score: 3.8978262119731335 Category Term Count % PValue Genes List Total Pop Hits Pop Total Fold Enrichment Bonferroni Benjamini FDR GOTERM_CC_DIRECT GO:0005886~plasma membrane 383 24.33290978 5.74E-05 SLC9A9, XRCC5, HRAS, CHMP3, ATP1B2, EFNA1, OSMR, SLC9A3, EFNA3, UTRN, SYT6, ZNRF2, APP, AT1425 4121 18224 1.18857065 0.038655922 0.038655922 0.086284383 UP_KEYWORDS Membrane 626 39.77128335 1.53E-04 SLC9A9, HRAS,
    [Show full text]
  • SI Appendix Index 1
    SI Appendix Index Calculating chemical attributes using EC-BLAST ................................................................................ 2 Chemical attributes in isomerase reactions ............................................................................................ 3 Bond changes …..................................................................................................................................... 3 Reaction centres …................................................................................................................................. 5 Substrates and products …..................................................................................................................... 6 Comparative analysis …........................................................................................................................ 7 Racemases and epimerases (EC 5.1) ….................................................................................................. 7 Intramolecular oxidoreductases (EC 5.3) …........................................................................................... 8 Intramolecular transferases (EC 5.4) ….................................................................................................. 9 Supporting references …....................................................................................................................... 10 Fig. S1. Overview …............................................................................................................................
    [Show full text]
  • Chronic Pancreatitis.Pdf
    CHRONIC PANCREATITIS: ELECTROPHILIC STRESS TEMPLATE Joan M Braganza DSc FRCP FRCPath DEVELOPMENT RATIONALISING GEOGRAPHY PETROCHEMICAL CONNECTION ACCOMMODATING GENE MUTATIONS MICRONUTRIENT THERAPY MAST CELL PATHOLOGY DISEASE PREVENTION CHRONIC PANCREATITIS: ELECTROPHILIC STRESS TEMPLATE By: Joan M Braganza DSc FRCP FRCPath University of Manchester Manchester, UK Published by: Pancreapedia: Exocrine Pancreas Knowledge Base In partnership with the University of Michigan Library Ann Arbor, MI 48109 and The American Pancreatic Association ISBN 978-1-60785-412-8 (e-book) This work is licensed under the Creative Commons Attribution-NonCommercial 4.0 International License. To view a copy of this license, visit https://creativecommons.org/licenses/by- nc/4.0/ or send a letter to Creative Commons, PO Box 1866, Mountain View, California, 94042, USA. Publishers Preface This monograph presents a comprehensive review of the work of Professor Joan Braganza into the pathogenesis and treatment of chronic pancreatitis as a disease caused by oxidative and particularly electrophilic stress with an emphasis on environmental toxicants as one factor which is part of the balance of damaging and protective cellular forces in the pancreas, liver and other participating organs. This is the second monograph of this type and follows “The Hamster Pancreas” written by Parviz Pour. Both books are published in open access eBook form under a Creative Commons license and are available on the Pancreapedia site. Pancreapedia will from time to time publish eBooks that are more substantive than a review article and where the author prepares the text and secures copyright approval for figures or tables published previously. Publishing can be done at no or low cost to the author.
    [Show full text]
  • Under the Direction of Dr. David J. Dix, Dr
    ABSTRACT GOETZ, AMBER KRISTINA. Toxicogenomic Study of Triazole Antifungal Modes of Action. (Under the direction of Dr. David J. Dix, Dr. Ernest Hodgson.) Common modes and mechanisms of hepatic and reproductive toxicity were characterized for a set of triazole antifungals. Wistar Han rats were fed myclobutanil, propiconazole, or triadimefon from gestation day 6 to postnatal day (PND) 120. Anogenital distance, body and organ weights, serum hormone levels, age at preputial separation, sperm morphology and motility, fertility and fecundity assays were selected to evaluate effects on development and adult reproductive function. All three triazoles increased anogenital distance, increased relative liver weights, induced hepatomegaly, increased absolute testis weights and serum testosterone levels. Myclobutanil and triadimefon impaired insemination and fertility, myclobutanil decreased pituitary weights, and triadimefon delayed puberty and decreased total serum thyroxine levels. The reproductive effects are consistent with disruption of testosterone homeostasis as a key event for triazole reproductive toxicity. To investigate common mechanisms of triazole toxicity, a toxicogenomic study was performed using liver and testis samples from PND92. Pathway and gene-level analysis of the liver highlighted biological processes affected by all three triazoles, including phase I-III; fatty acid, steroid, and xenobiotic metabolism; and lipid homeostasis. Triadimefon had a distinctive impact on sterol biosynthesis related genes in the liver. No common pathways were affected in the testis. To explore common mechanisms of action between in vivo and in vitro model systems, a series of comparative toxicogenomic studies were conducted on rat liver at multiple time points, rat and human primary hepatocytes, H295R cells, and PND92 liver and testis. Comparison between liver and rat hepatocytes showed consistent effect on fatty acid catabolism, sterol metabolism, and phase III transporters.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 6,706,501 B1 Ross0n Et Al
    USOO6706501B1 (12) United States Patent (10) Patent No.: US 6,706,501 B1 ROSS0n et al. (45) Date of Patent: Mar. 16, 2004 (54) POLYNUCLEOTIDE ENCODING A Hamberg, Biochem. and BiophyS. Res. Comm., 188(3): PROPIONIBACTERIUM LINOLEATE 1220–1227 (1992). SOMERASE AND USES THEREOF Hart et al., J. Virol.., 70.3606–3616 (1996) Sequence Search. Hughes et al., J. Biological Chemistry, 257(7):3643-3649 (75) Inventors: Reinhardt A. Rosson, Manitowoc, WI (1982). (US); Ming-De Deng, Manitowoc, WI Hunter et al., J. Biological Chemistry, 251 (8):2241-2247 (US); Alan D. Grund, Manitowoc, WI (1976). (US) Jack et al., Clinica Chimica Acta, 224:139-146 (1994). Jiang et al., J. Applied Microbiology, 85:95-102 (1998). (73) Assignee: Arkion Life Sciences LLC, Kemp et al., J. General Microbiology, 130:527–533 (1984). Wilmington, DE (US) Kemp et al., British J. Nutrition, 52:165–170 (1984). (*) Notice: Subject to any disclaimer, the term of this Kemp et al., British J. Nutrition, 52:171-177 (1984). patent is extended or adjusted under 35 Kemp et al., J. General Microbiology, 90:100-114 (1975). U.S.C. 154(b) by 0 days. Kepler et al., J. Biological Chemistry, 242(24):5686-5692 (1967). Kepler et al., Methods in Enzymology, 14:105-110 (1969). (21) Appl. No.: 09/561,077 Kepler et al., J. Biological Chemistry, 241(6):1350-1354 (22) Filed: Apr. 28, 2000 (1966). Kepler et al., J. Biological Chemistry, 245(14):3612-3620 Related U.S. Application Data (1970). (60) Provisional application No. 60/141,798, filed on Jun. 30, Kepler et al., J.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 6,743,609 B1 Ross0n Et Al
    USOO6743609B1 (12) United States Patent (10) Patent No.: US 6,743,609 B1 ROSS0n et al. (45) Date of Patent: Jun. 1, 2004 (54) LINOLEATE ISOMERASE Hunter et al., J. Biological Chemistry, 251 (8):2241-2247 (1976). (75) Inventors: Reinhardt A. Rosson, Manitowoc, WI Jack et al., Clinica Chimica Acta, 224:139-146 (1994). (US); Alan D. Grund, Manitowoc, WI Jiang et al., J. Applied Microbiology, 85:95-102 (1998). (US); Ming-De Deng, Manitowoc, WI Kemp et al., J. General Microbiology, 130:527–533 (1984). (US); Fernando Sanchez-Riera, Kemp et al., British J. Nutrition, 52:165–170 (1984). Manitowoc, WI (US) Kemp et al., British J. Nutrition, 52:171-177 (1984). Kemp et al., J. General Microbiology, 90:100-114 (1975). (73) Assignee: Arkion Life Sciences LLC, Kepler et al., J. Biological Chemistry, 242(24):5686-5692 Wilmington, DE (US) (1967). Kepler et al., Methods in Enzymology, 14:105-110 (1969). (*) Notice: Subject to any disclaimer, the term of this Kepler et al., J. Biological Chemistry, 241(6):1350-1354 patent is extended or adjusted under 35 (1966). U.S.C. 154(b) by 0 days. Kepler et al., J. Biological Chemistry, 245(14):3612-3620 (1970). (21) Appl. No.: 09/221,014 Kepler et al., J. Biological Chemistry, 246(9):2765-2771 (22) Filed: Dec. 23, 1998 (1971). Kil et al., Infect. Immun., 62:2440-2449 (sequence search) Related U.S. Application Data (1994). (60) Provisional application No. 60/068,617, filed on Dec. 23, Klein et al., 1983, Immobilized Microbial Cells, vol. 4, pp. 1997, and provisional application No.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2005/0003383 A1 Ross0n Et Al
    US 20050003383A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2005/0003383 A1 ROSS0n et al. (43) Pub. Date: Jan. 6, 2005 (54) LINOLEATE ISOMERASE (60) Provisional application No. 60/141,798, filed on Jun. 30, 1999. (75) Inventors: Reinhardt A. Rosson, Manitowoc, WI (US); Ming-De Deng, Manitowoc, WI Publication Classification (US); Alan D. Grund, Manitowoc, WI (US) (51) Int. Cl. ............................ C12O 1/68; CO7H 21/04; C12P 7/64; C12N 9/90 Correspondence Address: (52) U.S. Cl. ............................. 435/6; 435/69.1; 435/134; SHERIDAN ROSS PC 435/233; 435/252.3; 536/23.2 1560 BROADWAY SUTE 1200 (57) ABSTRACT DENVER, CO 80202 The present invention provides an isolated (trans,cis)-10,12 (73) Assignee: Arkion Life Sciences LLC d/b/a Bio linoleate isomerase and its nucleic acid and amino acid Technical Resources Division Sequences. The present invention also provides a method for (21) Appl. No.: 10/755,087 producing conjugated linoleic acid or conjugated linolenic acid (CLA), or derivatives thereof, from an oil using an (22) Filed: Jan. 9, 2004 immobilized cell and/or an isolated linoleate isomerase. The present invention also provides an isolated lipase-like pro Related U.S. Application Data tein and its nucleic acid and amino acid Sequences. The present invention also provides an isolated acetyltrans (63) Continuation of application No. 09/561,077, filed on ferase-like enzyme and its nucleic acid and amino acid Apr. 28, 2000, now Pat. No. 6,706,501. Sequences. Patent Application Publication Jan. 6, 2005 Sheet 1 of 59 OZZ 00Z 09|| VI(olqoree)z92.gz–Ж VTO(o?qolae)z92.gz–o– WTOsuel](O?qoJee)z92.gz–o– Patent Application Publication Jan.
    [Show full text]
  • W O 2019/079360 a L 25 April 2019 (25.04.2019) W 1P O PCT
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date W O 2019/079360 A l 25 April 2019 (25.04.2019) W 1P O PCT (51) International Patent Classification: (72) Inventors; and G01N 33/48 (2006.01) G01N 33/53 (2006.01) (71) Applicants: KEAN, Leslie [US/US]; c/o 818 Stewart St, Suite 603, Seattle, Washington 98101 (US). COLONNA, (21) International Application Number: Lucrezia [US/US]; c/o 818 Stewart St, Suite 603, Seattle, PCT/US2018/056166 Washington 98101 (US). CARROLL, Shaina [US/US]; (22) International Filing Date: c/o 77 Massachusetts Avenue, Cambridge, Massachusetts 16 October 2018 (16. 10.2018) 02139 (US). (25) Filing Language: English (72) Inventors: SHALEK, Alexander K.; c/o 77 Massachu¬ setts Avenue, Cambridge, Massachusetts 02139 (US). ZIE- (26) Publication Language: English GLER, Carly; c/o 77 Massachusetts Avenue, Cambridge, (30) Priority Data: Massachusetts 02139 (US). 62/573,015 16 October 2017 (16. 10.2017) US (74) Agent: SCHER, Michael B. et al.; Johnson, Marcou & (71) Applicants: MASSACHUSETTS INSTITUTE OF Isaacs, LLC, P.O. Bo 691, Hoschton, Georgia 30548 (US). TECHNOLOGY [US/US]; 77 Massachusetts Av¬ (81) Designated States (unless otherwise indicated, for every enue, Cambridge, Massachusetts 02139 (US). SEAT¬ kind of national protection available): AE, AG, AL, AM, TLE CHILDREN'S HOSPITAL DBA SEATTLE AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CHILDREN'S RESEARCH INSTITUTE [US/US]; 818 CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, Stewart St, Suite 603, Seattle, Washington 98101 (US).
    [Show full text]
  • The Chemistry and Evolution of Enzyme Function
    The Chemistry and Evolution of Enzyme Function: Isomerases as a Case Study Sergio Mart´ınez Cuesta EMBL - European Bioinformatics Institute Gonville and Caius College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 31st July 2014 This dissertation is the result of my own work and contains nothing which is the outcome of work done in collaboration except where specifically indicated in the text. No part of this dissertation has been submitted or is currently being submitted for any other degree or diploma or other qualification. This thesis does not exceed the specified length limit of 60.000 words as defined by the Biology Degree Committee. This thesis has been typeset in 12pt font using LATEX according to the specifications de- fined by the Board of Graduate Studies and the Biology Degree Committee. Cambridge, 31st July 2014 Sergio Mart´ınezCuesta To my parents and my sister Contents Abstract ix Acknowledgements xi List of Figures xiii List of Tables xv List of Publications xvi 1 Introduction 1 1.1 Chemistry of enzymes . .2 1.1.1 Catalytic sites, mechanisms and cofactors . .3 1.1.2 Enzyme classification . .5 1.2 Evolution of enzyme function . .6 1.3 Similarity between enzymes . .8 1.3.1 Comparing sequences and structures . .8 1.3.2 Comparing genomic context . .9 1.3.3 Comparing biochemical reactions and mechanisms . 10 1.4 Isomerases . 12 1.4.1 Metabolism . 13 1.4.2 Genome . 14 1.4.3 EC classification . 15 1.4.4 Applications . 18 1.5 Structure of the thesis . 20 2 Data Resources and Methods 21 2.1 Introduction .
    [Show full text]
  • MOL #82305 TITLE PAGE Title: Induced CYP3A4 Expression In
    Downloaded from molpharm.aspetjournals.org at ASPET Journals on September 28, 2021 1 This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted.
    [Show full text]
  • Prof. Dr. Uwe Bornscheuer Publication and Patent List
    Prof. Dr. Uwe Bornscheuer Publication and Patent List Prof. Dr. Uwe Bornscheuer Researcher ID: C-4612-2012; ORCID: 0000-0003-0685-2696; Scopus-ID: 7006947469 Institute of Biochemistry, Dept. of Biotechnol. & Enzyme Catalysis, University Greifswald, Greifswald, Germany Publications, Books, Reviews and Patents List 2020 [578] Müller, H., Godehard, S.P., Palm, G.J., Berndt, L., Badenhorst, C.P.S., Becker, A.K., Lammers, M., Bornscheuer, U.T. (2020), Discovery and design of family VIII carboxylesterases as highly efficient acyltransferases, Angew. Chem. Int. Ed., DOI: 10.1002/anie.202014169; Entdeckung und Design promiskuitiver Acyltransferase-Aktivität in Carboxylesterasen der Familie VIII, Angew. Chem., DOI: 10.1002/ange.202014169. [577] Tang, Q., Grathwol, C.W., Aslan-Üzel, A.S., Wu, S., Link, A., Pavlidis, I.V., Badenhorst, C.P.S., Bornscheuer, U.T., (2020), Directed evolution of a halide methyltransferase enables biocatalytic synthesis of diverse SAM analogues, Angew. Chem. Int. Ed., DOI: 10.1002/anie.202013871; Die gerichtete Evolution einer Halogenid-Methyltransferase erlaubt die biokatalytische Synthese diverser SAM-Analoga, Angew. Chem., DOI: 10.1002/ange.202013871. [576] Grobe, S., Bayer, T., Hamnevik, E., Wu, S., Grathwol. C.W., Link, A., Koban, S., Brundiek, H., Großjohann, B., Bornscheuer, U.T. (2020), Engineering regioselectivity of a P450 monooxygenase enables the synthesis of ursodeoxycholic acid via 7β-hydroxylation of lithocholic acid, Angew. Chem. Int. Ed., online; Modifikation der Regioselektivität einer P450-Monooxygenase ermöglicht die Synthese von Ursodeoxycholsäure durch die 7β-Hydroxylierung von Lithocholsäure, Angew. Chem., online. (V.I.P., top 5%). [575] Schweder, T., Bornscheuer, U., Hehemann, J.H., Amann, R. (2020), The sweet ocean – Bakterielle Mechanismen der marinen Polysaccharidverwertung, Biospektrum, accepted.
    [Show full text]