STEREOCHEMICAL COURSE OF GLUCAN HYDROLYSIS BY BARLEY (1-]3)-BETA-GLUCANASES AND (1-]3,1-]4)-BETA-GLUCANASES

被引：16

作者：

CHEN, L

SADEK, M

STONE, BA

BROWNLEE, RTC

FINCHER, GB

HOJ, PB

机构：

[1] UNIV ADELAIDE, DEPT HORT VITICULTURE & OENOL, GLEN OSMOND, SA 5064, AUSTRALIA

[2] LA TROBE UNIV, SCH BIOCHEM, BUNDOORA, VIC 3083, AUSTRALIA

[3] LA TROBE UNIV, SCH CHEM, BUNDOORA, VIC 3083, AUSTRALIA

[4] UNIV ADELAIDE, DEPT PLANT SCI, GLEN OSMOND, SA 5064, AUSTRALIA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1995年 / 1253卷 / 01期

基金：

澳大利亚研究理事会;

关键词：

BETA-GLUCANASE; (1-]3,1-]4); REACTION MECHANISM; NMR; (BARLEY); (ESCHERICHIA-COLI); (L-DIGITATA);

D O I：

10.1016/0167-4838(95)00157-P

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 stereochemical course of hydrolysis of Laminaria digitata laminarin and barley (1 --> 3,1 --> 4)-beta-glucan by barley (1 --> 3)-beta-glucanase (E.C. 3.2.1.39) isoenzyme GII and (1 --> 3,1 --> 4)-beta-glucanase (EC 3.2.1.73) isoenzyme EII, respectively, has been determined by H-1-NMR. Both enzymes catalyse hydrolysis with retention of anomeric configuration (e --> e) and may therefore operate via a double displacement mechanism. We predict that all other members of Family 17 of beta-glycosyl hydrolases also follow this stereochemical course of hydrolysis.

引用

页码：112 / 116

页数：5

共 23 条

[1] NEW SUBSTRATE FOR INVESTIGATING SPECIFICITY OF BETA-GLUCAN HYDROLASES [J].