ß-Glucosidases. Biochemistry and Molecular Biology PDF
Preview ß-Glucosidases. Biochemistry and Molecular Biology
org 001 s.w 12 | http://pubs.ac1/bk-1993-0533.f ß-Glucosidases 02 20 uly 16, oi: 10.1 on J3 | d 90.30 7, 199 09.y 2 213.1e: Jul y at bD wnloaded blication Do Pu In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. org 001 s.w 12 | http://pubs.ac1/bk-1993-0533.f 02 20 uly 16, oi: 10.1 on J3 | d 90.30 7, 199 09.y 2 213.1e: Jul y at bD wnloaded blication Do Pu In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. ACS SYMPOSIUM SERIES 533 ß-Glucosidases Biochemistry and Molecular Biology org 001 s.w 12 | http://pubs.ac1/bk-1993-0533.f Asim Esen, 02 EDITOR 20 uly 16, oi: 10.1 Virginia Polytechnic Institute and State University on J3 | d 90.30 7, 199 09.y 2 213.1e: Jul Developed from a symposium sponsored by Dat by the Division of Agricultural and Food Chemistry wnloaded blication of atht eth Aem 20er4itcha nN Cathioenmailc aMl eSeoticniegt y, Do Pu Washington, D.C., August 23-28, 1992 American Chemical Society, Washington, DC 1993 In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. Library of Congress Cataloging-in-Publication Data ß-glucosidases: biochemistry and molecular biology / Asim Esen, editor p. cm.—(ACS symposium series, ISSN 0097-6156; 533) "Developed from a symposium sponsored by the Division of Agricultural and Food Chemistry at the 204th National Meeting of the American Chemical Society, Washington, D.C., August 23-28, 1992." Includes bibliographical references and indexes. org 001 ISBN 0-8412-2697-0 s.w 12 | http://pubs.ac1/bk-1993-0533.f AMsidgeI1rae..is tc eEiuGnsls.gtle uu nVrc(,ao.2 Als 0 Sids4eaiatmrnhsieed,:s s —1. 9F13Co98o9o-2dn : g rCe.sW hsIeeIams.s. hiAsitnmryget.ro incIa,I In.D CA.Chme.m)e riiccIaaVln .S ToCcitihleeet:ym . icBDaelit vaSi-sogicoluinect oyo-.f 02 uly 16, 2oi: 10.10 5Q7P46.0199.G'245B42—3 d1c92904 93-25191 CIP on J3 | d 90.30 7, 199 The paper used in this publication meets the minimum requirements of American National y 213.109.ate: July 2 SZCt3oa9pn.yd4ra8irg-1dh9 tf8 o©4r. I1n99fo3r mation Sciences—Permanence of Paper for Printed Library Materials, ANSI bD wnloaded blication AAchlmla peRrteiicgrah intns C tRhhieessm evriocvaleuldm S. oecT iinehtdeyi c aaptepse atrhaen cceo poyfr igthhet ocwodneer 'ast c othnese nbott tthoamt roefp rtohger afpirhsitc pcaogpeie os fo fe athche Do Pu chapter may be made for personal or internal use or for the personal or internal use of specific clients. This consent is given on the condition, however, that the copier pay the stated per-copy fee through the Copyright Clearance Center, Inc., 27 Congress Street, Salem, MA 01970, for copying beyond that permitted by Sections 107 or 108 of the U.S. Copyright Law. This consent does not extend to copying or transmission by any means—graphic or electronic—for any other purpose, such as for general distribution, for advertising or promotional purposes, for creating a new collective work, for resale, or for information storage and retrieval systems. The copying fee for each chapter is indicated in the code at the bottom of the first page of the chapter. The citation of trade names and/or names of manufacturers in this publication is not to be construed as an endorsement or as approval by ACS of the commercial products or services referenced herein; nor should the mere reference herein to any drawing, specification, chemical process, or other data be regarded as a license or as a conveyance of any righto r permission to the holder, reader, or any other person or corporation, to manufacture, reproduce, use, or sell any patented invention or copyrighted work that may in any way be related thereto. Registered names, trademarks, etc., used in this publication, even without specific indication thereof, are not to be considered unprotected by law. PRINTED IN THE UNITED STATES OF AMERICA American Chemical Society Library 1155 16th St. N. W. In ß-Glucosidases; Esen, A.; ACS Symposium SeriesW; Aamserhiciann gChteomnic aDl S.o Ccie.t y2: W0a0sh3in6gto n, DC, 1993. 1993 Advisory Board ACS Symposium Series M. Joan Comstock, Series Editor V. Dean Adams Bonnie Lawlor University of Nevada— Institute for Scientific Information Reno Douglas R. Lloyd Robert J. Alaimo The University of Texas at Austin Procter & Gamble Pharmaceuticals, Inc. Robert McGorrin org 001 Kraft General Foods 12 | http://pubs.acs.1/bk-1993-0533.fw MUDUnnaaiivvvrieekdrr ss ABiittyyra nkoooffe lrITdo ew nan essee JPulalnUiut. SsS. c JiDe. neMcpeaser tnImnnes tnittu otef ,A griculture 2002 Vincent Pecoraro uly 16, oi: 10.1 APfrizinerd Camen tBraol sRee search University of Michigan on J3 | d Marshall Phillips 90.30 7, 199 NRaovbael rRte sFe.a rBchra Ldayb,o Jrarto. ry Delmont Laboratories 213.109.e: July 2 Margaret A. Cavanaugh NGoerothr gCea rWoli.n Ra oSbtaetret Us niversity by Dat National Science Foundation Downloaded Publication DLeehnignhi sU nWiv.e rHsiteys s AJMo.a hcTnarl auRsmt.e raS Cnho aSlplcelhegwey artz Hiroshi Ito University of Illinois IBM Almaden Research Center at Urbana—Champaign Madeleine M. Joullie L. Somasundaram University of Pennsylvania Ε. I. du Pont de Nemours and Company Gretchen S. Kohl Peter Willett Dow-Corning Corporation University of Sheffield (England) In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. Foreword IHE ACS SYMPOSIUM SERIES was first published in 1974 to provide a mechanism for publishing symposia quickly in book form. The purpose of this series is to publish comprehensive books developed from symposia, which are usually "snapshots in time" of the current research being done on a topic, plus org 001 some review material on the topic. For this reason, it is neces s.w 12 | http://pubs.ac1/bk-1993-0533.f tsppharaeropy pe totroBhssp aeeitfdac o rterhate aen bdeapl x easfc pyolourmef dr pcsec oodobms nei atupeptmr nuet-thbshb eliainssis sshe ipdevr doeeb ivnanoiesteo s,w ksq uaeiidnosc dfkp f lotuyhort etah uas enpcprpdosorel oslre aspcircrbetoi ilanoetat.en rdn.a decesSt,ds o mthttoeoe 02 20 round out the scope of the volume. In addition, a draft of each uly 16, oi: 10.1 Tpahpise r aniso npyemero-ures vireewvieedw pprrioocr etsos ifsin aslu paecrcveipsetadn cbey othr e reojregcatnioizn. on J3 | d er^) of the symposium, who become the editor(s) of the book. 09.90.30 y 27, 199 Tmheen daautitohnosr s othf enb orthe vitshee threeivr iepwaepresr s aancdc otrhdei nged tioto rtsh,e prreecpoamre 213.1e: Jul wcahmo ecrah-erceka dtyh atc oaplly n, eacneds ssauryb mreitv itshieo nsfi nhaal vep abpeeerns mtoa dthe.e editors, y at bD As a rule, only original research papers and original re wnloaded blication vtiioenws poaf pperresv iaorues liyn pcluubdliesdh iend tphaep evrosl uamre ens.o t Vaecrcbeapttiemd . reproduc Do Pu M. Joan Comstock Series Editor In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. Preface iHE ENZYME /?-GLUCOSIDASE (/?-D-glucoside glucohydrolase, EC 3.2.1.21) occurs widely in prokaryotes and eukaryotes. It catalyzes the hydrolysis of aryl- and alkyl-/?-D-glucosides as well as glucosides with only a carbohydrate moiety (e.g., cellobiose). This book reviews and discusses the state-of-the-art knowledge about /?-glucosidases of a wide spectrum of organisms (mammal, plant, insect, fungus, and bacterium). It also sets the tone for and points out the direction of future research and applications g 1 relative to this ubiquitous enzyme. s.acs.or33.pr00 and Ceucrorneonmt irce siemarpclhi caotni o/n?s-g. luHcousmidaans esa chida s /?s-igglnuicfoicsaidnat ses ci(egnltuifciocc, emreebdriocsail-, b5 p://pu993-0 cdeadseu)r ehsa st hpaott ewnitlila l bien tuhsee fdule vienl opthme enttr eoaft mtheenrta poefu tGica uacnhde rd'sia gdniosesatisce , praon 012 | htt21/bk-1 iton hethriet edly dsoissoormdeer. cCauysteods oblyic thnee udterafil ci/e?n-cgylu ocfo saicdiads e/ ?-igs luicmopsildicasaet eldo cianl izthede 20 uly 16, oi: 10.1 mgleutcaobsoidliessm i nogf epstyerdid oaxloinneg- 5w'-i/t?h- Dfo-goldusc oosfi dpel,a nats awnedll aans imthael hsoyudrrcoelys.s is Polfa nj3t- on J3 | d /?-glucosidases have been implicated in a variety of growth, productivity, 90.30 7, 199 Idne faednsdei,t ioann,d rfeocoedn t adnadt af eiendd itcoaxtiec itthya-tr etlhaet epd lraenat cetinoznysm seu cmha ya s bec yiannvooglevneeds iins . 09.y 2 the metabolism of plant hormones such as auxin, gibberellin, and cytoki- 3.1Jul nin, whose storage forms occur as /?-glucosides and are activated upon 21e: by Dat cleavage by /?-glucosidase. d n Cellulose, our most abundant renewable resource on this planet, wnloadeblicatio foothrmers pthaep ehr igphroesdtu cptrso).p oIrnt iofnu ngoif amnudn ibcaicptaelr igaa, rbthaeg ee n(ze.ygm., e neisw isnpvaoplevr eda nind Do Pu cellulose and cellobiose catabolism as part of the cellulase complex. Cel- lulases break down cellulose to cellobiose, and /?-glucosidases hydrolyze cellobiose to two glucose molecules. /?-Glucosidase is inhibited by its end product, glucose; the substrate cellobiose accumulates and in turn inhibits the cellulase complex in organisms that rely on cellulose as their carbon source. If the rate-limiting step catalyzed by /?-glucosidase in cellulose hydrolysis can be overcome, glucose production from cellulose by enzy matic means should become economically feasible. Thus, fungal and bac terial /?-glucosidases appear as ideal candidates for engineering a 0- glucosidase to be used as part of the cellulase complex in the industrial- scale conversion of cellulose to glucose. In the past decade, considerable progress has been made on the ix In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. molecular biology and biochemistry of /?-glucosidases, but much more remains to be done and known. It is hoped that the data, ideas, and insights presented in this book by leading researchers in the field will serve as a launching pad for future research, discoveries, and applications. I would like to take this opportunity to express my gratitude to the contributing authors, the ACS Division of Agricultural and Food Chemis try, the ACS Books Department, and the National Science Foundation Biochemistry Program for making possible the symposium and the publi cation of the book. ASIM ESEN Department of Biology Virginia Polytechnic and State University g 1 Blacksburg, VA 24061 s.acs.or33.pr00 January 12, 1993 b5 u0 p://p993- 12 | htt1/bk-1 02 20 uly 16, oi: 10.1 Jd on 3 | 90.30 7, 199 09.y 2 3.1Jul 21e: by Dat d n wnloadeblicatio Do Pu x In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. Chapter 1 ß-Glucosidases Overview Asim Esen Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061 g 1 or00 In the past decade, considerable progress has been made on the cs.ch molecular biology and biochemistry of ß-glucosidases. Some of bs.a533. these data have been analyzed and discussed in the context of p://pu993-0 srepsepceifcitc toor gsapnecisimfics p(rpolabnletsm, sf u(nbgiio, mbaascst ecroian, vaenrsdi ohnu,m caynasn) oagnedn ewsiitsh, 12 | htt1/bk-1 thoogset-tphaerra suitned eirn tethraec tsioamnse, Guamubcrheelrla's tdhiese alesea)d. inTg his bßo-golku cobsriidnagses 02 20 researchers with widely different but complementary research uly 16, oi: 10.1 irnevteireews,t sa. ndI nd itshceu snse xtth e1 5b icohcahpetmeriss,t ryt haensed mreosleeacruclhare rbs ioplroegsye notf, Jd on 3 | ß-glucosidases from bacteria, fungi, plants, insects, and humans. 90.30 7, 199 Tß-hgeluyc osiadlassoes promvaidye bei nsaipgphltise d intoto prhobolwem sk nroawnlgeidngge froomn 09.y 2 biomass production and conversion to the diagnosis and 3.1Jul treatment of Gaucher's disease. 21e: y at bD wnloaded blication /ipn?l -aGanrtlysul,c oasfniuddna gasile, ksy l(a En/C?im- 3ga.l2ul.sc1, o.2s1iad)n edcs a taabnlaydcz tece ertilhaloe. bhiyodsBer oealcynasdui ss oeo cfc gu/?lr-y gculobusicqiodusiiictd oleiusn sklyaa gnineds Do Pu /f-glucosidases are ubiquitous in the living world, one expects to find structural and catalytic properties shared by all /?-glucosidases. In fact, a review of the literature indicates that almost all /?-glucosidases have subunit molecular weights of 55 to 65 kD, acidic pH optima (pH 5-6), and an absolute requirement for a /^-glycoside (i.e., glucoside, and to a much lesser extent fucoside and galactoside) as substrate. /J-Glucosidases from widely different sources show remarkable similarity in substrate specificity for glycone (glucose) and some nonphysiological aglycones (e.g., nitrophenols and umbelliferone), although they may have widely different physiological glucosidic substrates with different aglycone moieties. In general, /?-glucosidases from different orders and kingdoms appear to differ in their specificities for the aglycone (an aryl or alkyl group) linked to the glucosyl group by a /?-glycosidic bond. /?-Glucosidases of fungi, bacteria, humans, and dicotylodenous plants have been shown to be 0097-6156/93/0533-0001$06.00/0 © 1993 American Chemical Society In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. 2 /3-GLUCOSIDASES: BIOCHEMISTRY AND MOLECULAR BIOLOGY glycosylated, while those of monocots (maize and sorghum) are not. In plants, the /?-glucosidases of dicots are localized to the cell wall (1, 2) or protein bodies (3; Chapter 11) while the /?-glucosidases of monocots are localized to the plastid (4, 5, 6, Esen and Stetler, in press). In mammals (e.g., humans and mice), acid /?-glucosidase is localized to the lysosome while its neutral counterpart is a soluble protein (cytosolic) (Chapter 7). One would also expect that an enzyme such as /J-glucosidase that is not involved in a mainstream metabolic pathway would differ considerably in its structure and specificity from organism to organism due to divergent or convergent evolution. This would be especially true among members of different kingdoms as well as among members of the higher taxonomic groups in the same kingdom. Current research on /7-glucosidases has significant scientific and economic implications. Plant /?-glucosidases have been implicated in a variety of key metabolic events: growth, productivity, and food and feed g 1 or00 toxicity-related reactions. In humans, one /?-glucosidase, commonly cs.ch known as glucocerebrosidase (/?-D-glucosyl-N-acylsphingosine bs.a533. glucohydrolase) or human acid /?-glucosidase, catalyzes the degradation p://pu993-0 toof agnlu icnohseyrlicteedr admiisdeea sien, thGea ulycshoesro'sm dei.s eTashee, dienf iwchieicnhc yt hoef gthley ceonszpyhmineg olleipaidds 12 | htt1/bk-1 gcelullcs,o spyrlocdeuracminigd eo naec coufm thuel atthesr ewe iftohrinm sth eo f ltyhsiso sdoimseeass eo f( 7re, tCichualpoteenrd 6o)t.h eTlihael 02 20 molecular biology of the gene encoding this human /?-glucosidase and the uly 16, oi: 10.1 wpheylls-iucnodcheresmtoicoadl. proHpeurmtiaens oafc idth e /?e-ngzluycmoes idhaasvee hbaese n psotutedniteida l anind athree on J3 | d development of therapeutic and diagnostic procedures, particularly for the 90.30 7, 199 t(rseoamtme efunnt goi f aGnda ubcahcetre'rsi ad) isheaavsee .b e/e?n- Gthleu csousbidjeacste so fo mf cueclhlu ploalsytt iacn do rognagnoisimngs 09.y 2 research. These enzymes are expected to be targets for genetic 3.1Jul engineering to design and select /?-glucosidases for specific applications 21e: such as biomass conversion. y at bD wnloaded blication OSunbe sotrf atthee Scpoenctrifoicvietrys aianl di sNsuaetus rarel lSautebds ttroa t/eJ-sg lucosidases is their substrate Do Pu specificity. Are /?-glucosidases a sort of "jack of all trades" enzymes catalyzing the hydrolysis of /?-glycosidic linkages in all mono and diglycosides? Are they specialists catalyzing only the hydrolysis of /?-glycosidic linkages between glucose and specific aryl and alkyl aglycones? Another way of asking the question is: is the enzyme specific for the glycone or the aglycone or both? For example, maize /?-glucosidase purified to homogeneity show 5 times greater activity towards p-nitrophenyl (pNP) /J-D-fucoside than pNP /?-D-glucoside (the difference is due to higher V x; the Ks are the same). Similarly, its ma m relative activity towards pNP /?-D-galactoside is about 10% of that towards pNP /?-D-glucoside. Is the maize enzyme a /J-fucosidase, a /J-glucosidase or a /?-glycosidase? The questions of substrate specificity and the importance of using natural substrates during enzyme purification and characterization have In ß-Glucosidases; Esen, A.; ACS Symposium Series; American Chemical Society: Washington, DC, 1993.
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