Cutinase Structure, Function and Biocatalytic Applications
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Kramers' Theory and the Dependence of Enzyme Dynamics on Trehalose
catalysts Review Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity José G. Sampedro 1,* , Miguel A. Rivera-Moran 1 and Salvador Uribe-Carvajal 2 1 Instituto de Física, Universidad Autónoma de San Luis Potosí, Manuel Nava 6, Zona Universitaria, San Luis Potosí C.P. 78290, Mexico; [email protected] 2 Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México C.P. 04510, Mexico; [email protected] * Correspondence: [email protected]fisica.uaslp.mx; Tel.: +52-(444)-8262-3200 (ext. 5715) Received: 29 April 2020; Accepted: 29 May 2020; Published: 11 June 2020 Abstract: The disaccharide trehalose is accumulated in the cytoplasm of some organisms in response to harsh environmental conditions. Trehalose biosynthesis and accumulation are important for the survival of such organisms by protecting the structure and function of proteins and membranes. Trehalose affects the dynamics of proteins and water molecules in the bulk and the protein hydration shell. Enzyme catalysis and other processes dependent on protein dynamics are affected by the viscosity generated by trehalose, as described by the Kramers’ theory of rate reactions. Enzyme/protein stabilization by trehalose against thermal inactivation/unfolding is also explained by the viscosity mediated hindering of the thermally generated structural dynamics, as described by Kramers’ theory. The analysis of the relationship of viscosity–protein dynamics, and its effects on enzyme/protein function and other processes (thermal inactivation and unfolding/folding), is the focus of the present work regarding the disaccharide trehalose as the viscosity generating solute. Finally, trehalose is widely used (alone or in combination with other compounds) in the stabilization of enzymes in the laboratory and in biotechnological applications; hence, considering the effect of viscosity on catalysis and stability of enzymes may help to improve the results of trehalose in its diverse uses/applications. -
Cutinases from Mycobacterium Tuberculosis
Identification of Residues Involved in Substrate Specificity and Cytotoxicity of Two Closely Related Cutinases from Mycobacterium tuberculosis Luc Dedieu, Carole Serveau-Avesque, Ste´phane Canaan* CNRS - Aix-Marseille Universite´ - Enzymologie Interfaciale et Physiologie de la Lipolyse - UMR 7282, Marseille, France Abstract The enzymes belonging to the cutinase family are serine enzymes active on a large panel of substrates such as cutin, triacylglycerols, and phospholipids. In the M. tuberculosis H37Rv genome, seven genes coding for cutinase-like proteins have been identified with strong immunogenic properties suggesting a potential role as vaccine candidates. Two of these enzymes which are secreted and highly homologous, possess distinct substrates specificities. Cfp21 is a lipase and Cut4 is a phospholipase A2, which has cytotoxic effects on macrophages. Structural overlay of their three-dimensional models allowed us to identify three areas involved in the substrate binding process and to shed light on this substrate specificity. By site-directed mutagenesis, residues present in these Cfp21 areas were replaced by residues occurring in Cut4 at the same location. Three mutants acquired phospholipase A1 and A2 activities and the lipase activities of two mutants were 3 and 15 fold greater than the Cfp21 wild type enzyme. In addition, contrary to mutants with enhanced lipase activity, mutants that acquired phospholipase B activities induced macrophage lysis as efficiently as Cut4 which emphasizes the relationship between apparent phospholipase A2 activity and cytotoxicity. Modification of areas involved in substrate specificity, generate recombinant enzymes with higher activity, which may be more immunogenic than the wild type enzymes and could therefore constitute promising candidates for antituberculous vaccine production. -
Purification and Characterization of Cutinase from Venturia Inaequalis
Physiology and Biochemistry Purification and Characterization of Cutinase from Venturia inaequalis Wolfram K611er and Diana M. Parker Assistant professor and research assistant, Department of Plant Pathology, Cornell University, New York State Agricultural Experiment Station, Geneva 14456. We thank Professor A. L. Jones for the isolates of Venturia inaequalis, Mr. Robert W. Ennis, Jr. for his help in cutin preparation, and Comstock Foods, Alton, NY, for the apple peels. Accepted for publication 16 August 1988. ABSTRACT K61ler, W., and Parker, D. M. 1989. Purification and characterization of cutinase from Venturia inaequalis. Phytopathology 79:278-283. Venturia inaequalis was grown in a culture medium containing purified cutinase from V. inaequalisis optimal at a pH of 6 and thus different from apple cutin as the sole carbon source. After 8 wk of growth an esterase was the alkaline pH-optimum reported for other purified cutinases. The isolated from the culture fluid and purified to apparent homogeneity. The hydrolysis of the model esterp-nitrophenyl butyrate was less affected by the enzyme hydrolyzed tritiated cutin and thus was identified as cutinase. The pH. The esterase activity was strongly inhibited by diisopropyl purified cutinase is a glycoprotein with a molecular mass of 21-23 kg/ mol, fluorophosphate, and the phosphorylation of one serine was sufficient for as determined by various procedures. Remarkable structural features are a complete inhibition. Thus, cutinase from V. inaequalis belongs to the class high content of glycine, a high content of nonpolar amino acids, two of serine hydrolases, a characterisitic shared with other fungal cutinases. disulfide bridges, and a high degree of hydrophobicity. -
Letters to Nature
letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997). -
Mycobacterial Lipolytic Enzymes: a Gold Mine for Tuberculosis Research Luc Dedieu, C
Mycobacterial lipolytic enzymes: A gold mine for tuberculosis research Luc Dedieu, C. Serveau-Avesque, L. Kremer, Stéphane Canaan To cite this version: Luc Dedieu, C. Serveau-Avesque, L. Kremer, Stéphane Canaan. Mycobacterial lipolytic en- zymes: A gold mine for tuberculosis research. Biochimie, Elsevier, 2013, 95 (1), pp.66-73. 10.1016/j.biochi.2012.07.008. hal-02646757 HAL Id: hal-02646757 https://hal.inrae.fr/hal-02646757 Submitted on 29 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives| 4.0 International License Version définitive du manuscrit publiée dans / Final version of the manuscript published in : Biochimie (2013), Vol. 95, p. 66-73, DOI: 10.1016/j.biochi.2012.07.008 Journal homepage : www.elsevier.com/locate/biochi ipt cr nus a Review m Mycobacterial lipolytic enzymes: A gold mine for tuberculosis research a a b,c a,* / Author L. Dedieu , C. Serveau-Avesque , L. Kremer , S. Canaan r a u CNRS UMR7282-Aix-Marseille Université e Enzymologie Interfaciale -
WO 2013/016115 Al 31 January 2013 (31.01.2013) 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 2013/016115 Al 31 January 2013 (31.01.2013) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every CUP 19/14 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, (21) International Application Number: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, PCT/US20 12/047326 DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, (22) International Filing Date: HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, 19 July 2012 (19.07.2012) KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (25) Filing Language: English OM, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, SD, (26) Publication Language: English SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (30) Priority Data: 61/5 10,637 22 July 201 1 (22.07.201 1) US (84) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (71) Applicant (for all designated States except US) : NO- GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, VOZYMES NORTH AMERICA, INC. -
Investigations of the Mechanism for Activation of Bacillus Thuringiensis Phosphatidylinositol-Specific Phospholipase C
Investigations of the Mechanism for Activation of Bacillus Thuringiensis Phosphatidylinositol-specific Phospholipase C Author: Mingming Pu Persistent link: http://hdl.handle.net/2345/1179 This work is posted on eScholarship@BC, Boston College University Libraries. Boston College Electronic Thesis or Dissertation, 2009 Copyright is held by the author, with all rights reserved, unless otherwise noted. Boston College The Graduate School of Arts and Sciences Department of Chemistry INVESTIGATIONS OF THE MECHANISM FOR ACTIVATION OF BACILLUS THURINGIENSIS PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C a dissertation by MINGMING PU submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy August 2009 © copyright by MINGMING PU 2009 Investigations of the Mechanism for Activation of Bacillus thuringiensis Phosphatidylinositol-specific Phospholipase C Mingming Pu Under the direction of Dr. Mary F. Roberts ABSTRACT The bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus thuringiensis is specifically activated by low concentrations of a non-substrate lipid, phosphatidylcholine (PC), presented as an interface. However, if the PC concentration in the interface is too high relative to substrate, the enzyme exhibits surface dilution inhibition. Understanding this bacterial enzyme, which shares many kinetic features with the larger and more complex mammalian PI-PLC enzymes, requires elucidating the mechanism for PC activation and inhibition. Various techniques were applied to study the interaction of the protein with vesicles composed of both the activator lipid PC and the substrate lipid (or a nonhydrolyzable analogue). Fluorescence correlation spectroscopy (FCS), used to monitor bulk partitioning of the enzyme on vesicles, revealed that both the PC and the substrate analogue are required for the tightest binding of the PI-PLC to vesicles. -
A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases
catalysts Review A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases Efstratios Nikolaivits 1,† , Maria Kanelli 1,†, Maria Dimarogona 2 and Evangelos Topakas 1,* 1 IndBioCat Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 9 Heroon Polytechniou Str., Zographou Campus, 15780 Athens, Greece; [email protected] (E.N.); [email protected] (M.K.) 2 Department of Chemical Engineering, University of Patras, 26504 Patras, Greece; [email protected] * Correspondence: [email protected]; Tel.: +30-210-772-3264 † These authors have contributed equally in this work. Received: 7 November 2018; Accepted: 27 November 2018; Published: 3 December 2018 Abstract: Cutinases are α/β hydrolases, and their role in nature is the degradation of cutin. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. The first focused studies on cutinases started around 50 years ago. Since then, numerous cutinases have been isolated and characterized, aiming at the elucidation of their structure–function relations. Our deeper understanding of cutinases determines the applications by which they could be utilized; from food processing and detergents, to ester synthesis and polymerizations. However, cutinases are mainly efficient in the degradation of polyesters, a natural function. Therefore, these enzymes have been successfully applied for the biodegradation of plastics, as well as for the delicate superficial hydrolysis of polymeric materials prior to their functionalization. Even though research on this family of enzymes essentially began five decades ago, they are still involved in many reports; novel enzymes are being discovered, and new fields of applications arise, leading to numerous related publications per year. -
Widespread Impact of Horizontal Gene Transfer on Plant Colonization of Land
ARTICLE Received 10 Jun 2012 | Accepted 20 Sep 2012 | Published 23 Oct 2012 DOI: 10.1038/ncomms2148 Widespread impact of horizontal gene transfer on plant colonization of land Jipei Yue1,2, Xiangyang Hu1,3, Hang Sun1, Yongping Yang1,3 & Jinling Huang2 In complex multicellular eukaryotes such as animals and plants, horizontal gene transfer is commonly considered rare with very limited evolutionary significance. Here we show that horizontal gene transfer is a dynamic process occurring frequently in the early evolution of land plants. Our genome analyses of the moss Physcomitrella patens identified 57 families of nuclear genes that were acquired from prokaryotes, fungi or viruses. Many of these gene families were transferred to the ancestors of green or land plants. Available experimental evidence shows that these anciently acquired genes are involved in some essential or plant- specific activities such as xylem formation, plant defence, nitrogen recycling as well as the biosynthesis of starch, polyamines, hormones and glutathione. These findings suggest that horizontal gene transfer had a critical role in the transition of plants from aquatic to terrestrial environments. On the basis of these findings, we propose a model of horizontal gene transfer mechanism in nonvascular and seedless vascular plants. 1 Key Laboratory of Biodiversity and Biogeography, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China. 2 Department of Biology, East Carolina University, Greenville, North Carolina 27858, USA. 3 Institute of Tibet Plateau Research, Chinese Academy of Sciences, Kunming 650201, China. Correspondence and requests for materials should be addressed to J.H. (email: [email protected]). NATURE COMMUNICATIONS | 3:1152 | DOI: 10.1038/ncomms2148 | www.nature.com/naturecommunications © 2012 Macmillan Publishers Limited. -
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. -
Cutinase: Characteristics, Preparation, and Application
Biotechnology Advances 31 (2013) 1754–1767 Contents lists available at ScienceDirect Biotechnology Advances journal homepage: www.elsevier.com/locate/biotechadv Research review paper Cutinase: Characteristics, preparation, and application Sheng Chen, Lingqia Su, Jian Chen, Jing Wu ⁎ State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Ave., Wuxi, Jiangsu 214122, China School of Biotechnology and Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Ave., Wuxi, Jiangsu 214122, China article info abstract Article history: Cutinases (E.C. 3.1.1.74) belong to the α/β-hydrolase superfamily. They were initially discovered because they Received 15 May 2013 are secreted by fungi to hydrolyze the ester bonds of the plant polymer cutin. Since then, they have been Received in revised form 4 August 2013 shown to catalyze the hydrolysis of a variety of polymers, insoluble triacylglycerols, and low-molecular-weight Accepted 11 September 2013 soluble esters. Cutinases are also capable of catalyzing esterification and transesterification reactions. These Available online 19 September 2013 relatively small, versatile, secreted catalysts have shown promise in a number of industrial applications. This re- view begins by describing the characteristics of cutinases, pointing out key differences among cutinases, esterases Keywords: Cutinase and lipases, and reviewing recent progress in engineering improved cutinases. It continues with a review of the Identification methods used to produce cutinases, with the goal of obtaining sufficient quantities of material for use in indus- Crystal structure trial processes. Finally, the uses of cutinases in the textile industry are described. The studies presented here dem- Molecular modification onstrate that the cutinases are poised to become important industrial catalysts, replacing older technologies with Preparation more environmentally friendly processes. -
NAPRALERT Classification Codes
NAPRALERT Classification Codes June 1993 STN International® Copyright © 1993 American Chemical Society Quoting or copying of material from this publication for educational purposes is encouraged, providing acknowledgement is made of the source of such material. Classification Codes in NAPRALERT The NAPRALERT File contains classification codes that designate pharmacological activities. The code and a corresponding textual description are searchable in the /CC field. To be comprehensive, both the code and the text should be searched. Either may be posted, but not both. The following tables list the code and the text for the various categories. The first two digits of the code describe the categories. Each table lists the category described by codes. The last table (starting on page 56) lists the Classification Codes alphabetically. The text is followed by the code that also describes the category. General types of pharmacological activities may encompass several different categories of effect. You may want to search several classification codes, depending upon how general or specific you want the retrievals to be. By reading through the list, you may find several categories related to the information of interest to you. For example, if you are looking for information on diabetes, you might want to included both HYPOGLYCEMIC ACTIVITY/CC and ANTIHYPERGLYCEMIC ACTIVITY/CC and their codes in the search profile. Use the EXPAND command to verify search terms. => S HYPOGLYCEMIC ACTIVITY/CC OR 17006/CC OR ANTIHYPERGLYCEMIC ACTIVITY/CC OR 17007/CC 490 “HYPOGLYCEMIC”/CC 26131 “ACTIVITY”/CC 490 HYPOGLYCEMIC ACTIVITY/CC ((“HYPOGLYCEMIC”(S)”ACTIVITY”)/CC) 6 17006/CC 776 “ANTIHYPERGLYCEMIC”/CC 26131 “ACTIVITY”/CC 776 ANTIHYPERGLYCEMIC ACTIVITY/CC ((“ANTIHYPERGLYCEMIC”(S)”ACTIVITY”)/CC) 3 17007/CC L1 1038 HYPOGLYCEMIC ACTIVITY/CC OR 17006/CC OR ANTIHYPERGLYCEMIC ACTIVITY/CC OR 17007/CC 2 This search retrieves records with the searched classification codes such as the ones shown here.