β-Glucosidases

被引:515
作者
Cairns, James R. Ketudat [1 ,2 ]
Esen, Asim [3 ]
机构
[1] Suranaree Univ Technol, Sch Biochem, Inst Sci, Nakhon Ratchasima 30000, Thailand
[2] Suranaree Univ Technol, Sch Chem, Inst Sci, Nakhon Ratchasima 30000, Thailand
[3] Virginia Polytech Inst & State Univ, Dept Biol Sci, Blacksburg, VA 24061 USA
关键词
Biological function; Structure; Substrate-specificity; Glycoside hydrolase; Glycosides; Structure-function relationships; SUBSTRATE AGLYCONE SPECIFICITY; MOUSE KLOTHO GENE; CRYSTAL-STRUCTURE; ARABIDOPSIS-THALIANA; MOLECULAR-CLONING; AGGREGATING FACTOR; ACTIVE-SITE; ER-BODY; ISOFLAVONOID GLYCOSIDES; MAIZE;
D O I
10.1007/s00018-010-0399-2
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
beta-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. beta-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall beta-glucan turnover, phytohormone activation, and release of aromatic compounds in plants, and biomass conversion in microorganisms. These functions lead to many agricultural and industrial applications. beta-Glucosidases have been classified into glycoside hydrolase (GH) families GH1, GH3, GH5, GH9, and GH30, based on their amino acid sequences, while other beta-glucosidases remain to be classified. The GH1, GH5, and GH30 beta-glucosidases fall in GH Clan A, which consists of proteins with (beta/alpha)(8)-barrel structures. In contrast, the active site of GH3 enzymes comprises two domains, while GH9 enzymes have (alpha/alpha)(6) barrel structures. The mechanism by which GH1 enzymes recognize and hydrolyze substrates with different specificities remains an area of intense study.
引用
收藏
页码:3389 / 3405
页数:17
相关论文
共 138 条
[1]   Scopolin-hydrolyzing β-glucosidases in roots of Arabidopsis [J].
Ahn, Young Ock ;
Shimizu, Bun-ichi ;
Sakata, Kanzo ;
Gantulga, Dashzeveg ;
Zhou, Zhanghe ;
Bevan, David R. ;
Esen, Asim .
PLANT AND CELL PHYSIOLOGY, 2010, 51 (01) :132-143
[2]   A cell wall-bound β-glucosidase from germinated rice:: Purification and properties [J].
Akiyama, T ;
Kaku, H ;
Shibuya, N .
PHYTOCHEMISTRY, 1998, 48 (01) :49-54
[3]   Differential mechanism-based labeling and unequivocal activity assignment of the two active sites of intestinal lactase/phlorizin hydrolase [J].
Arribas, JCD ;
Herrero, AG ;
Martín-Lomas, M ;
Cañada, FJ ;
He, SM ;
Withers, SG .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (24) :6996-7005
[4]   Furostanol glycoside leaves of 26-O-β-glucosidase from the Solanum torvum [J].
Arthan, D ;
Kittakoop, P ;
Esen, A ;
Svasti, J .
PHYTOCHEMISTRY, 2006, 67 (01) :27-33
[5]   SUBSTRATE-SPECIFICITY OF MAIZE BETA-GLUCOSIDASE [J].
BABCOCK, GD ;
ESEN, A .
PLANT SCIENCE, 1994, 101 (01) :31-39
[6]   Molecular architecture of strictosidine glucosidase:: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family [J].
Barleben, Leif ;
Panjikar, Santosh ;
Ruppert, Martin ;
Koepke, Juergen ;
Stoeckigt, Joachim .
PLANT CELL, 2007, 19 (09) :2886-2897
[7]   A Glucosinolate Metabolism Pathway in Living Plant Cells Mediates Broad-Spectrum Antifungal Defense [J].
Bednarek, Pawel ;
Pislewska-Bednarek, Mariola ;
Svatos, Ales ;
Schneider, Bernd ;
Doubsky, Jan ;
Mansurova, Madina ;
Humphry, Matt ;
Consonni, Chiara ;
Panstruga, Ralph ;
Sanchez-Vallet, Andrea ;
Molina, Antonio ;
Schulze-Lefert, Paul .
SCIENCE, 2009, 323 (5910) :101-106
[8]   Substrate (aglycone) specificity of human cytosolic β-glucosidase [J].
Berrin, JG ;
Czjzek, M ;
Kroon, PA ;
McLauchlan, WR ;
Puigserver, A ;
Williamson, G ;
Juge, N .
BIOCHEMICAL JOURNAL, 2003, 373 :41-48
[9]   Functional expression of human liver cytosolic β-glucosidase in Pichia pastoris -: Insights into its role in the metabolism of dietary glucosides [J].
Berrin, JG ;
McLauchlan, WR ;
Needs, P ;
Williamson, G ;
Puigserver, A ;
Kroon, PA ;
Juge, N .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (01) :249-258
[10]   Identification of β-glucosidase aggregating factor (BGAF) and mapping of BGAF binding regions on maize β-glucosidase [J].
Blanchard, DJ ;
Cicek, M ;
Chen, JL ;
Esen, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (15) :11895-11901