STEREOCHEMICAL COURSE AND STRUCTURE OF THE PRODUCTS OF THE ENZYMATIC ACTION OF ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE FROM BACILLUS-LICHENIFORMIS

Authors
MALET C JIMENEZBARBERO J BERNABE M BROSA C PLANAS A
Citation
C. Malet et al., STEREOCHEMICAL COURSE AND STRUCTURE OF THE PRODUCTS OF THE ENZYMATIC ACTION OF ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE FROM BACILLUS-LICHENIFORMIS, Biochemical journal, 296, 1993, pp. 753-758
Citations number
44
Categorie Soggetti
Biology
Journal title
Biochemical journal → ACNP
ISSN journal
02646021
Volume
296
Year of publication
1993
Part
3
Pages
753 - 758
Database
ISI
SICI code
0264-6021(1993)296:<753:SCASOT>2.0.ZU;2-B
Abstract
The stereochemical course of the reaction catalysed by endo-1,3-1,4-be ta-D-glucan 4-glucanohydrolase (EC 3.2.1.73) has been determined by H- 1 n.m.r. The enzyme-catalysed hydrolysis of barley beta-glucan proceed s with overall retention of the anomeric configuration, indicating tha t the enzyme operates through a double-displacement mechanism. The str uctures of the final oligosaccharide products, 3-beta-O-cellobiosyl D- glucopyranoside and 3-beta-O-cellotriosyl D-glucopyranoside, have been completely assigned by H-1- and C-13-n.m.r. spectroscopy.