A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana

被引:192
作者
Henrissat, B
Coutinho, PM
Davies, GJ
机构
[1] CNRS, UMR 6098, F-13402 Marseille 20, France
[2] Univ Aix Marseille I & II, F-13402 Marseille 20, France
[3] Inst Super Tecn, Ctr Biol & Chem Engn, P-1049001 Lisbon, Portugal
[4] Univ York, Dept Chem, Struct Biol Lab, York Y010 5DD, N Yorkshire, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
Arabidopsis; genome; glycoside hydrolases; glycosyltransferases;
D O I
10.1023/A:1010667012056
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
The synthesis, modification, and breakdown of carbohydrates is one of the most fundamentally important reactions in nature. The structural and functional diversity of glycosides is mirrored by a vast array of enzymes involved in their synthesis (glycosyltransferases), modification (carbohydrate esterases) and breakdown (glycoside hydrolases and polysaccharide lyases). The importance of these processes is reflected in the dedication of 1-2% of an organism's genes to glycoside hydrolases and glycosyltransferases alone. In plants, these processes are of particular importance for cell-wall synthesis and expansion, starch metabolism, defence against pathogens, symbiosis and signalling. Here we present an analysis of over 730 open reading frames representing the two main classes of carbohydrate-active enzymes, glycoside hydrolases and glycosyltransferases, in the genome of Arabidopsis thaliana. The vast importance of these enzymes in cell-wall formation and degradation is revealed along with the unexpected dominance of pectin degradation in Arabidopsis, with at least 170 open-reading frames dedicated solely to this task.
引用
收藏
页码:55 / 72
页数:18
相关论文
共 63 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   Horizontal gene transfer and mutation:: Ngrol genes in the genome of Nicotiana glauca [J].
Aoki, S ;
Syono, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (23) :13229-13234
[3]   IMMUNOCYTOCHEMISTRY OF PLANT DEFENSE-MECHANISMS INDUCED UPON MICROBIAL ATTACK [J].
BENHAMOU, N .
MICROSCOPY RESEARCH AND TECHNIQUE, 1995, 31 (01) :63-78
[4]   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
[5]   High resolution x-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base [J].
Burmeister, WP ;
Cottaz, S ;
Rollin, P ;
Vasella, A ;
Henrissat, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (50) :39385-39393
[6]   Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives [J].
Callebaut, I ;
Labesse, G ;
Durand, P ;
Poupon, A ;
Canard, L ;
Chomilier, J ;
Henrissat, B ;
Mornon, JP .
CELLULAR AND MOLECULAR LIFE SCIENCES, 1997, 53 (08) :621-645
[7]   A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities [J].
Campbell, JA ;
Davies, GJ ;
Bulone, V ;
Henrissat, B .
BIOCHEMICAL JOURNAL, 1997, 326 :929-939
[8]   In vitro activities of four xyloglucan endotransglycosylases from Arabidopsis [J].
Campbell, P ;
Braam, J .
PLANT JOURNAL, 1999, 18 (04) :371-382
[9]   Three-dimensional structures of UDP-sugar glycosyltransferases illuminate the biosynthesis of plant polysaccharides [J].
Charnock, SJ ;
Henrissat, B ;
Davies, GJ .
PLANT PHYSIOLOGY, 2001, 125 (02) :527-531
[10]   The X6 "thermostabilizing" domains of xylanases are carbohydrate-binding modules:: Structure and biochemistry of the Clostridium thermocellum X6b domain [J].
Charnock, SJ ;
Bolam, DN ;
Turkenburg, JP ;
Gilbert, HJ ;
Ferreira, LMA ;
Davies, GJ ;
Fontes, CMGA .
BIOCHEMISTRY, 2000, 39 (17) :5013-5021