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Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
RSC Advances
RSC Advances PAPER View Article Online View Journal | View Issue Experimental identification and computational characterization of a novel extracellular Cite this: RSC Adv.,2017,7,13928 metalloproteinase produced by Clostridium sordellii† Michael J. Aldape,*ab Aoxiang Tao,c Dustin D. Heeney,a Eric R. McIndoo,a John M. Frencha and Dong Xu*c Clostridium sordellii is a lethal pathogen for both animals and humans. Severe capillary leakage, toxic shock syndrome, and an extreme leukemoid reaction (LR), are hallmark features of C. sordellii infections and contribute to its high mortality rate. Here we report the discovery of a previously unknown and uncharacterized metalloproteinase of C. sordellii (referred as Mcs1) that cleaves human vascular cell adhesion molecule (VCAM)-1 in vitro, an adhesion molecule critical to hematopoietic precursor retention and leukocyte diapedesis. We successfully identified the open reading frame encoding Mcs1 within Creative Commons Attribution-NonCommercial 3.0 Unported Licence. the ATCC 9714 genome and developed an Dmcs1 mutant strain using the ClosTron mutagenesis technology. No VCAM-1 proteolysis was observed from exotoxins collected from mutant strain cultures. Using advanced protein structural modeling and molecular dynamics simulation techniques, the 3D molecular structure and conformational features of Mcs1 were also characterized. Our data demonstrates that Mcs1 proteolytic activity is controlled by the electrostatic interactions between Glu113 and Arg227 residues and the gating motions within its cleft region. This pilot interdisciplinary investigation provided crucial experimental evidence of the existence of Mcs1 in C. sordellii and Received 2nd December 2016 molecular insights into its 3D structure and proteolytic activity. These findings have the potential to help Accepted 22nd February 2017 This article is licensed under a advance new therapeutics and diagnostics against deadly C. -
Supplementary Materials
Supplementary materials Supplementary Table S1: MGNC compound library Ingredien Molecule Caco- Mol ID MW AlogP OB (%) BBB DL FASA- HL t Name Name 2 shengdi MOL012254 campesterol 400.8 7.63 37.58 1.34 0.98 0.7 0.21 20.2 shengdi MOL000519 coniferin 314.4 3.16 31.11 0.42 -0.2 0.3 0.27 74.6 beta- shengdi MOL000359 414.8 8.08 36.91 1.32 0.99 0.8 0.23 20.2 sitosterol pachymic shengdi MOL000289 528.9 6.54 33.63 0.1 -0.6 0.8 0 9.27 acid Poricoic acid shengdi MOL000291 484.7 5.64 30.52 -0.08 -0.9 0.8 0 8.67 B Chrysanthem shengdi MOL004492 585 8.24 38.72 0.51 -1 0.6 0.3 17.5 axanthin 20- shengdi MOL011455 Hexadecano 418.6 1.91 32.7 -0.24 -0.4 0.7 0.29 104 ylingenol huanglian MOL001454 berberine 336.4 3.45 36.86 1.24 0.57 0.8 0.19 6.57 huanglian MOL013352 Obacunone 454.6 2.68 43.29 0.01 -0.4 0.8 0.31 -13 huanglian MOL002894 berberrubine 322.4 3.2 35.74 1.07 0.17 0.7 0.24 6.46 huanglian MOL002897 epiberberine 336.4 3.45 43.09 1.17 0.4 0.8 0.19 6.1 huanglian MOL002903 (R)-Canadine 339.4 3.4 55.37 1.04 0.57 0.8 0.2 6.41 huanglian MOL002904 Berlambine 351.4 2.49 36.68 0.97 0.17 0.8 0.28 7.33 Corchorosid huanglian MOL002907 404.6 1.34 105 -0.91 -1.3 0.8 0.29 6.68 e A_qt Magnogrand huanglian MOL000622 266.4 1.18 63.71 0.02 -0.2 0.2 0.3 3.17 iolide huanglian MOL000762 Palmidin A 510.5 4.52 35.36 -0.38 -1.5 0.7 0.39 33.2 huanglian MOL000785 palmatine 352.4 3.65 64.6 1.33 0.37 0.7 0.13 2.25 huanglian MOL000098 quercetin 302.3 1.5 46.43 0.05 -0.8 0.3 0.38 14.4 huanglian MOL001458 coptisine 320.3 3.25 30.67 1.21 0.32 0.9 0.26 9.33 huanglian MOL002668 Worenine -
Collection of Information on Enzymes a Great Deal of Additional Information on the European Union Is Available on the Internet
European Commission Collection of information on enzymes A great deal of additional information on the European Union is available on the Internet. It can be accessed through the Europa server (http://europa.eu.int). Luxembourg: Office for Official Publications of the European Communities, 2002 ISBN 92-894-4218-2 © European Communities, 2002 Reproduction is authorised provided the source is acknowledged. Final Report „Collection of Information on Enzymes“ Contract No B4-3040/2000/278245/MAR/E2 in co-operation between the Federal Environment Agency Austria Spittelauer Lände 5, A-1090 Vienna, http://www.ubavie.gv.at and the Inter-University Research Center for Technology, Work and Culture (IFF/IFZ) Schlögelgasse 2, A-8010 Graz, http://www.ifz.tu-graz.ac.at PROJECT TEAM (VIENNA / GRAZ) Werner Aberer c Maria Hahn a Manfred Klade b Uli Seebacher b Armin Spök (Co-ordinator Graz) b Karoline Wallner a Helmut Witzani (Co-ordinator Vienna) a a Austrian Federal Environmental Agency (UBA), Vienna b Inter-University Research Center for Technology, Work, and Culture - IFF/IFZ, Graz c University of Graz, Department of Dermatology, Division of Environmental Dermatology, Graz Executive Summary 5 EXECUTIVE SUMMARY Technical Aspects of Enzymes (Chapter 3) Application of enzymes (Section 3.2) Enzymes are applied in various areas of application, the most important ones are technical use, manufacturing of food and feedstuff, cosmetics, medicinal products and as tools for re- search and development. Enzymatic processes - usually carried out under mild conditions - are often replacing steps in traditional chemical processes which were carried out under harsh industrial environments (temperature, pressures, pH, chemicals). Technical enzymes are applied in detergents, for pulp and paper applications, in textile manufacturing, leather industry, for fuel production and for the production of pharmaceuticals and chiral substances in the chemical industry. -
Airway Microbiota Signals Anabolic and Catabolic Remodeling in the Transplanted Lung
Airway microbiota signals anabolic and catabolic remodeling in the transplanted lung Stephane Mouraux, MD,a* Eric Bernasconi, PhD,a*Celine Pattaroni, MSc,a Angela Koutsokera, MD, PhD,a John-David Aubert, MD,a Johanna Claustre, MD,b,c,d Christophe Pison, MD, PhD,b,c,d Pierre-Joseph Royer, PhD,e Antoine Magnan, MD,e Romain Kessler, MD, PhD,f Christian Benden, MD, FCCP,g Paola M. Soccal, MD,h Benjamin J. Marsland, PhD,aà and Laurent P. Nicod, MD,aà on behalf of the SysCLAD Consortium§ Lausanne, Zurich, and Geneva, Switzerland; and Grenoble, Saint Martin d’Heres, Nantes, and Strasbourg, France GRAPHICAL ABSTRACT Microbiota Impact on Airway Remodeling Microbiota: Prevotella, Streptococcus Veillonella, Neisseria Lung Bacterial transplant communities Staphylococcus, Pseudomonas Haemophilus, Corynebacterium Broncho- alveolar Host: M2 macrophage Myofibroblast lavage Cell differential M1 macrophage Neutrophil Fibroblast Gene Platelet-derived growth factor Thrombospondin expression Matrix metalloproteinases Osteopontin Pulmonary alveolus Capillary Extracellular Matrix Collagen Anabolic Fibronectin Remodeling Homeostasis Catabolic Remodeling Type I cell Type II cell Background: Homeostatic turnover of the extracellular matrix for a heterogeneous entity ultimately associated with conditions the structure and function of the healthy lung. In pathological airway and/or parenchyma remodeling. lung transplantation, long-term management remains limited Objective: This study assessed whether the local cross-talk by chronic lung allograft dysfunction, an umbrella term used between the pulmonary microbiota and host cells is a key From athe Service de Pneumologie, Centre Hospitalier Universitaire Vaudois, Lausanne; Thoracic Society for this work. E. Bernasconi’s institution received grant no. 305457, bthe Clinique Universitaire de Pneumologie, Pole^ Thorax et Vaisseaux, Centre Hospi- SysCLAD Consortium from European Commission FP7; grant no. -
DNA-5-O- S Ot-On-O-8.As -O-On-Oh'ss Taxi & 8 8-1 Cataceoa-8 NA As S-PEG-38Agasksacrestsgescga-3 DNA As 8-Cacaccoagios CEO: C(-3 Patent Application Publication Jun
US 201201498.43A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2012/0149843 A1 Chien et al. (43) Pub. Date: Jun. 14, 2012 (54) NANOFIBERS AND MORPHOLOGY Publication Classification SHIFTING MICELLES (51) Int. Cl. (75) Inventors: Miao-Ping Chien, San Diego, CA C08F 29/2 (2006.01) (US); Nathan C. Gianneschi, San A 6LX 9/70 (2006.01) Diego, CA (US) CI2O I/68 (2006.01) CO8F 299/00 (2006.01) (73) Assignee: THE REGENTS OF THE BOSD 7/4 (2006.01) UNIVERSITY OF A6IR 8/02 (2006.01) CALIFORNLA, Oakland, CA (US) CI2P 19/34 (2006.01) B82Y 4O/OO (2011.01) (21) Appl. No.: 13/363,645 B82Y5/00 (2011.01) (22) Filed: Feb. 1, 2012 (52) U.S. Cl. ......... 525/54.1; 424/401; 424/443; 435/6.1: 435/91.1 : 525/54.2; 427/216:977/788; 977/915; Related U.S. Application Data 977/890; 977/906 (63) Continuation of application No. PCT/US2010/ 044321, filed on Aug. 3, 2010. (57) ABSTRACT (60) Provisional application No. 61/230.924, filed on Aug. The invention discloses novel morphology shifting micelles 3, 2009, provisional application No. 61/316,325, filed and amphiphilic coated metal nanofibers. Methods of using on Mar. 22, 2010. and making the same are also disclosed. Assetsy whe Yxxx x: wa toxia 8A: is:tex : ona ... 8:kyi-xxx8 tapex 88-se: PEG - DNA-5-o- s ot-on-o-8.as -o-on-oh'ss taxi & 8 8-1 cataceoA-8 NA as S-PEG-38AGASKSACrestsgescGA-3 DNA as 8-cacAccoAgios CEO: C(-3 Patent Application Publication Jun. -
EUROPEAN COMMISSION Brussels, 28 April 2020 REGISTER of FOOD
EUROPEAN COMMISSION DIRECTORATE-GENERAL FOR HEALTH AND FOOD SAFETY Food and feed safety, innovation Food processing technologies and novel foods Brussels, 28 April 2020 REGISTER OF FOOD ENZYMES TO BE CONSIDERED FOR INCLUSION IN THE UNION LIST Article 17 of Regulation (EC) No 1332/20081 provides for the establishment of a Register of all food enzymes to be considered for inclusion in the Union list. In accordance with that Article, the Register includes all applications which were submitted within the initial period fixed by that Regulation and which comply with the validity criteria laid down in accordance with Article 9(1) of (EC) No 1331/2008 establishing a common authorisation procedure for food additives, food enzymes and food flavourings2. The Register therefore lists all valid food enzyme applications submitted until 11 March 2015 except those withdrawn by the applicant before that date. Applications submitted after that date are not included in the Register but will be processed in accordance with the Common Authorisation Procedure. The entry of a food enzyme in the Register specifies the identification, the name, the source of the food enzyme as provided by the applicant and the EFSA question number under which the status of the Authority’s assessment can be followed3. As defined by Article 3 of Regulation (EC) No 1332/2008, ‘food enzyme’ subject to an entry in the Register, refers to a product that may contain more than one enzyme capable of catalysing a specific biochemical reaction. In the assessment process, such a food enzyme may be linked with several EFSA question numbers. -
Enzymes in Fish and Seafood Processing
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Frontiers - Publisher Connector REVIEW published: 07 July 2016 doi: 10.3389/fbioe.2016.00059 Enzymes in Fish and Seafood Processing Pedro Fernandes1,2* 1 Department of Bioengineering, Institute for Biotechnology and Bioengineering, Instituto Superior Técnico, Universidade de Lisboa, Lisbon, Portugal, 2 Faculdade de Engenharia, Universidade Lusófona de Humanidades e Tecnologias, Lisbon, Portugal Enzymes have been used for the production and processing of fish and seafood for several centuries in an empirical manner. In recent decades, a growing trend toward a rational and controlled application of enzymes for such goals has emerged. Underlying such pattern are, among others, the increasingly wider array of enzyme activities and enzyme sources, improved enzyme formulations, and enhanced requirements for cost-effective and environmentally friendly processes. The better use of enzyme action in fish- and seafood-related application has had a significant impact on fish-related indus- Edited by: Antonio Trincone, try. Thus, new products have surfaced, product quality has improved, more sustainable Istituto di Chimica Biomolecolare, processes have been developed, and innovative and reliable analytical techniques have Consiglio Nazionale delle Ricerche, been implemented. Recent development in these fields are presented and discussed, Italy and prospective developments are suggested. Reviewed by: Tania Primavera Pozzo Mendoza, Keywords: biocatalysis, biosensors, proteases, transglutaminases, lipases, oxidases University of California Davis, USA Helena M. Moreno Conde, Institute of Food Science, INTRODUCTION Technology and Nutrition (ICTAN), Spain Enzymes are key tools in biotechnology and related areas because of their catalytic nature (Fraatz *Correspondence: et al., 2014; Jemli et al., 2016). -
Thermophiles and Thermozymes
Thermophiles and Thermozymes Edited by María-Isabel González-Siso Printed Edition of the Special Issue Published in Microorganisms www.mdpi.com/journal/microorganisms Thermophiles and Thermozymes Thermophiles and Thermozymes Special Issue Editor Mar´ıa-Isabel Gonz´alez-Siso MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editor Mar´ıa-Isabel Gonzalez-Siso´ Universidade da Coruna˜ Spain 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 Microorganisms (ISSN 2076-2607) from 2018 to 2019 (available at: https://www.mdpi.com/journal/ microorganisms/special issues/thermophiles) 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 978-3-03897-816-9 (Pbk) ISBN 978-3-03897-817-6 (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 Editor ...................................... vii Mar´ıa-Isabel Gonz´alez-Siso Editorial for the Special Issue: Thermophiles and Thermozymes Reprinted from: Microorganisms 2019, 7, 62, doi:10.3390/microorganisms7030062 ........ -
(12) Patent Application Publication (10) Pub. No.: US 2004/0081648A1 Afeyan Et Al
US 2004.008 1648A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2004/0081648A1 Afeyan et al. (43) Pub. Date: Apr. 29, 2004 (54) ADZYMES AND USES THEREOF Publication Classification (76) Inventors: Noubar B. Afeyan, Lexington, MA (51) Int. Cl." ............................. A61K 38/48; C12N 9/64 (US); Frank D. Lee, Chestnut Hill, MA (52) U.S. Cl. ......................................... 424/94.63; 435/226 (US); Gordon G. Wong, Brookline, MA (US); Ruchira Das Gupta, Auburndale, MA (US); Brian Baynes, (57) ABSTRACT Somerville, MA (US) Disclosed is a family of novel protein constructs, useful as Correspondence Address: drugs and for other purposes, termed “adzymes, comprising ROPES & GRAY LLP an address moiety and a catalytic domain. In Some types of disclosed adzymes, the address binds with a binding site on ONE INTERNATIONAL PLACE or in functional proximity to a targeted biomolecule, e.g., an BOSTON, MA 02110-2624 (US) extracellular targeted biomolecule, and is disposed adjacent (21) Appl. No.: 10/650,592 the catalytic domain So that its affinity Serves to confer a new Specificity to the catalytic domain by increasing the effective (22) Filed: Aug. 27, 2003 local concentration of the target in the vicinity of the catalytic domain. The present invention also provides phar Related U.S. Application Data maceutical compositions comprising these adzymes, meth ods of making adzymes, DNA's encoding adzymes or parts (60) Provisional application No. 60/406,517, filed on Aug. thereof, and methods of using adzymes, Such as for treating 27, 2002. Provisional application No. 60/423,754, human Subjects Suffering from a disease, Such as a disease filed on Nov. -
Ext 43867.Pdf
ISSN (Online) 2456 -1304 International Journal of Science, Engineering and Management (IJSEM) Vol 2, Issue 9, September 2017 A Comprehensive Review – Anatomical, Functional and Molecular profiling of honey bee wax moth Galleria mellonella [1] S. Pooja Sri , [2] S. Sribal Department of Genetic Engineering, Bharath University, Chennai - 600073, Tamil Nadu, India [email protected], [email protected] Abstract:-- The greater wax moth Galleria mellonella attracts the view of many researchers by their anatomical, functional and molecular profiling patterns. Mostly the larvae feeds on honey bee hive and Larvae of the greater wax moth Galleria mellonella have been shown to provide a useful insight into the pathogenesis model of a wide range of microbial infections including mammalian fungal (Fusarium oxysporum, Aspergillus fumigatus, Candida albicans) and bacterial pathogens, such as Staphylococcus aureus, Proteus vulgaris, Serratia marcescens, Pseudomonas aeruginosa, Listeria monocytogenes or Enterococcus faecalis [1]. Like mammals, insects possess a complex innate immune system. In addition, analogies are found between the epithelial cells of insect larval midguts and intestinal cells of mammalian digestive systems. Finally, several basic components essential for the bacterial infection process such as cell adhesion, resistance to antimicrobial peptides, tissue degradation and adaptation to oxidative stress are likely to be important in both insects and mammals [2]. Thus, insects are polyvalent tools for the identification and characterization of microbial virulence factors involved in mammalian infections [1]. In 1934, many researchers focused on studying the larval body fluids to understand the biochemical mechanism of the honey bee moth. The larva of Galleria mellonella is available as in commercial for feeding the predatory insects. -
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.