Two potent competitive inhibitors discriminating α-glucosidase family I from family II
書誌事項
- 公開日
- 2004-04
- 権利情報
-
- https://www.elsevier.com/tdm/userlicense/1.0/
- DOI
-
- 10.1016/j.carres.2003.10.035
- 公開者
- Elsevier BV
この論文をさがす
説明
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 IsoAca, in which the K(i) values of AcvGlc (0.35-3.0 microM) were 21- to 440-fold smaller than those of IsoAca. However, the second group of enzymes showed similar K(i) values, ranging from 1.6 to 8.0 microM 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 IsoAca and AcvGlc. The two groups of alpha-glucosidases seemed to recognize distinctively the extra reducing-terminal glucose unit in IsoAca.
収録刊行物
-
- Carbohydrate Research
-
Carbohydrate Research 339 (6), 1035-1040, 2004-04
Elsevier BV
