Potential physiological role of plant glycosidase inhibitors

被引:60
作者
Bellincampi, D
Camardella, L
Delcour, JA
Desseaux, V
D'Ovidio, R
Durand, A
Elliot, G
Gebruers, K
Giovane, A
Juge, N
Sórensen, JF
Svensson, B
Vairo, D
机构
[1] Univ Roma La Sapienza, Dipartimento Biol Vegetale, I-00185 Rome, Italy
[2] CNR, Inst Prot Biochem, I-80125 Naples, Italy
[3] Katholieke Univ Leuven, Lab Food Chem, B-3001 Louvain, Belgium
[4] Fac Sci & Tech Marseille, Inst Mediterraneen Rech Nutr, UMR 1111, INRA, F-13397 Marseille 20, France
[5] Univ Tuscia, Dipartimento Agrobiol & Agrochim, I-01100 Viterbo, Italy
[6] Inst Food Res, Norwich NR4 7UA, Norfolk, England
[7] Univ Naples 2, Dept Biochem & Biophys, I-80138 Naples, Italy
[8] Fac Sci & Tech St Jerome, Inst Mediterraneen Rech Nutr, UMR 1111, INRA, F-13397 Marseille 20, France
[9] Danisco AS, DK-8220 Brabrand, Denmark
[10] Carlsberg Lab, Dept Chem, DK-2500 Copenhagen, Denmark
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2004年 / 1696卷 / 02期
关键词
glycosidase proteinaceous inhibitor; plant defense; plant development;
D O I
10.1016/j.bbapap.2003.10.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Carbohydrate-active enzymes including glycosidases, transglycosidases, glycosyltransferases, polysaccharide lyases and carbohydrate esterases are responsible for the enzymatic processing of carbohydrates in plants. A number of carbohydrate-active enzymes are produced by microbial pathogens and insects responsible of severe crop losses. Plants have evolved proteinaceous inhibitors to modulate the activity of several of these enzymes. The continuing discovery of new inhibitors indicates that this research area is still unexplored and may lead to new exciting developments. To date, the role of the inhibitors is not completely understood. Here we review recent results obtained on the best characterised inhibitors, pointing to their possible biological role in vivo. Results recently obtained with plant transformation technology indicate that this class of inhibitors has potential biotechnological applications. (C) 2003 Elsevier B.V All rights reserved.
引用
收藏
页码:265 / 274
页数:10
相关论文
共 103 条
[1]   ROLE OF PROTEINACEOUS ALPHA-AMYLASE ENZYME-INHIBITORS IN PREHARVEST SPROUTING OF WHEAT-GRAIN [J].
ABDULHUSSAIN, S ;
PAULSEN, GM .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1989, 37 (02) :295-299
[2]   ARGININE IS ESSENTIAL FOR THE ALPHA-AMYLASE INHIBITORY ACTIVITY OF THE ALPHA-AMYLASE/SUBTILISIN INHIBITOR (BASI) FROM BARLEY-SEEDS [J].
ABE, J ;
SIDENIUS, U ;
SVENSSON, B .
BIOCHEMICAL JOURNAL, 1993, 293 :151-155
[3]   DEVELOPMENT-RELATED CHANGES IN DECAY SUSCEPTIBILITY AND POLYGALACTURONASE INHIBITOR CONTENT OF BARTLETT PEAR FRUIT [J].
ABUGOUKH, AA ;
STRAND, LL ;
LABAVITCH, JM .
PHYSIOLOGICAL PLANT PATHOLOGY, 1983, 23 (01) :101-109
[4]   HOST-PATHOGEN INTERACTIONS .3. PROTEINS FROM PLANT CELL WALLS INHIBIT POLYGALACTURONASES SECRETED BY PLANT PATHOGENS [J].
ALBERSHEIM, P ;
ANDERSON, AJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1971, 68 (08) :1815-+
[5]  
Bailey J. A., 1992, Colletotrichum: biology, pathology and control., P88
[6]   A GLYCOPROTEIN INHIBITOR OF PECTIN METHYLESTERASE IN KIWI FRUIT (ACTINIDIA-CHINENSIS) [J].
BALESTRIERI, C ;
CASTALDO, D ;
GIOVANE, A ;
QUAGLIUOLO, L ;
SERVILLO, L .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1990, 193 (01) :183-187
[7]   Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution [J].
Bishop, JG ;
Dean, AM ;
Mitchell-Olds, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (10) :5322-5327
[8]   Substrate mimicry in the active center of a mammalian alpha-amylase: Structural analysis of an enzyme-inhibitor complex [J].
BompardGilles, C ;
Rousseau, P ;
Rouge, P ;
Payan, F .
STRUCTURE, 1996, 4 (12) :1441-1452
[9]   A PECTIN LYASE INHIBITOR PROTEIN FROM CELL-WALLS OF SUGAR-BEET [J].
BUGBEE, WM .
PHYTOPATHOLOGY, 1993, 83 (01) :63-68
[10]   Kiwi protein inhibitor of pectin methylesterase - Amino-acid sequence and structural importance of two disulfide bridges [J].
Camardella, L ;
Carratore, V ;
Ciardiello, MA ;
Servillo, L ;
Balestrieri, C ;
Giovane, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (14) :4561-4565