When substrate inhibits and inhibitor activates: implications of β-glucosidases

详细信息    查看全文

• 作者：Silja Kuusk ; Priit Väljamäe
• 关键词：β ; glucosidase ; Glucose tolerance ; Glucose inhibition ; Glucose activation ; Nonproductive binding ; Transglycosylation
• 刊名：Biotechnology for Biofuels
• 出版年：2017
• 出版时间：December 2017
• 年：2017
• 卷：10
• 期：1
• 全文大小：3512KB
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology; Plant Breeding/Biotechnology; Environmental Engineering/Biotechnology; Renewable and Green Energy; Renewable and Green Energy; Microbiology;
• 出版者：BioMed Central
• ISSN：1754-6834
• 卷排序：10

文摘

Backgroundβ-glucosidases (BGs) catalyze the hydrolysis of β-glycosidic bonds in glucose derivatives. They constitute an important group of enzymes with biotechnological interest like supporting cellulases in degradation of lignocellulose to fermentable sugars. In the latter context, the glucose tolerant BGs are of particular interest. These BGs often show peculiar kinetics, including inhibitory effects of substrates and activating effects of inhibitors, such as glucose or xylose. The mechanisms behind the activating/inhibiting effects are poorly understood. The nonproductive binding of substrate is expected in cases where enzymes with multiple consecutive binding subsites are studied on substrates with a low degree of polymerization. The effects of inhibitors to BGs exerting nonproductive binding of substrate have not been discussed in the literature before.