A heterotetrameric alpha-amylase inhibitor from emmer (Triticum dicoccon Schrank) seeds

被引：22
作者：
Capocchi, A. [1 ]
Muccilli, V. [2 ]
Cunsolo, V. [2 ]
Saletti, R. [2 ]
Foti, S. [2 ]
Fontanini, D. [1 ]
机构：
[1] Univ Pisa, Dept Biol, I-56126 Pisa, Italy
[2] Univ Catania, Dept Chem Sci, I-95125 Catania, Italy
来源：
PHYTOCHEMISTRY | 2013年 / 88卷
关键词：
Triticum dicoccon; Heterotetrameric alpha-amylase inhibitor; CM protein; Tandem mass spectrometry; Kinetic study; Homology modeling; X-RAY-ANALYSIS; TETRAMERIC INHIBITOR; WHEAT; COMPLEX; PURIFICATION; PROTEINS; SUBUNITS;
D O I：
10.1016/j.phytochem.2012.12.010
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：
Plants have developed a constitutive defense system against pest attacks, which involves the expression of a set of inhibitors acting on heterologous amylases of different origins. Investigating the soluble protein complement of the hulled wheat emmer we have isolated and characterized a heterotetrameric alpha-amylase inhibitor (ETI). Based on mass spectrometry data, it is an assembly of proteins highly similar to the CM2/CM3/CM16 found in durum wheat. Our data indicate that these proteins can also inhibit exogenous alpha-amylases in binary assemblies. The calculated dissociation constants (K-i) for the pancreatic porcine amylase- and human salivary amylase-ETI complexes are similar to those found in durum and soft wheat. Homology modeling of the CM subunits indicate structural similarities with other proteins belonging to the cereal family of trypsin/alpha-amylase inhibitors; a possible homology modeled structure for a tetrameric assembly of the subunits is proposed. (C) 2012 Elsevier Ltd. All rights reserved.
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页码：6 / 14
页数：9
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