Two potent competitive inhibitors discriminating α-glucosidase family I from family II

被引:83
作者
Kimura, A [1 ]
Lee, JH
Lee, IS
Lee, HS
Park, KH
Chiba, S
Kim, D
机构
[1] Hokkaido Univ, Grad Sch Agr, Sapporo, Hokkaido 0608589, Japan
[2] Chonnam Natl Univ, Engn Res Inst, Gwangju 500757, South Korea
[3] Chonnam Natl Univ, Fac Appl Chem Engn, Gwangju 500757, South Korea
[4] Seoul Natl Univ, Ctr Agr Biomat, Natl Lab Funct Food Carbohydrates, Suwon 441744, South Korea
基金
新加坡国家研究基金会;
关键词
enzyme inhibitor; alpha-glucosidase family; isoacarbose; acarviosine-glucose; acarbose;
D O I
10.1016/j.carres.2003.10.035
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 inhibition kinetics for isoacarbose (a pseudotetrasaccharide, IsoAca) and acarviosine-glucose (pseudotrisaccharide, AcvGlc), both of which are derivatives of acarbose, were investigated with various types of alpha-glucosidases obtained from microorganisms, plants, and insects. IsoAca and AcvGlc, competitive inhibitors, allowed classification of alpha-glucosidases into two groups. Enzymes of the first group were strongly inhibited by AcvGlc and weakly by lsoAca, in which the K-i values of AcvGlc (0.35-3.0 PM) were 21 - to 440-fold smaller than those of lsoAca. However, the second group of enzymes showed similar Ki values, ranging from 1.6 to 8.0 muM for both compounds. This classification for alpha-glucosidases is in total agreement with that based on the similarity of their amino acid sequences (family I and family II). This indicated that the alpha-glucosidase families I and II could be clearly distinguished based on their inhibition kinetic data for lsoAca and AcvGlc. The two groups of alpha-glucosidases seemed to recognize distinctively the extra reducing-terminal glucose unit in IsoAca. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1035 / 1040
页数:6
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