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标题：EMERGING ROLE OF N- AND C-TERMINAL INTERACTIONS IN STABILIZING (β;/α)8 FOLD WITH SPECIAL EMPHASIS ON FAMILY 10 XYLANASES
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作者：Amit Bhardwaj ; Pranjal Mahanta ; Suryanarayanarao Ramakumar 等
期刊名称：Computational and Structural Biotechnology Journal
印刷版ISSN：2001-0370
出版年度：2012
卷号：2
期号：3
DOI：10.5936/csbj.201209014
语种：
出版社：Computational and Structural Biotechnology Journal
摘要：Xylanases belong to an important class of industrial enzymes. Various xylanases have been purified and characterized from a plethora of organisms including bacteria, marine algae, plants, protozoans, insects, snails and crustaceans. Depending on the source, the enzymatic activity of xylanases varies considerably under various physico-chemical conditions such as temperature, pH, high salt and in the presence of proteases. Family 10 or glycosyl hydrolase 10 (GH10) xylanases are one of the well characterized and thoroughly studied classes of industrial enzymes. The TIM-barrel fold structure which is ubiquitous in nature is one of the characteristics of family 10 xylanases. Family 10 xylanases have been used as a “model system” due to their TIM-barrel fold to dissect and understand protein stability under various conditions. A better understanding of structure-stability-function relationships of family 10 xylanases allows one to apply these governing molecular rules to engineer other TIM-barrel fold proteins to improve their stability and retain function(s) under adverse conditions. In this review, we discuss the implications of N-and C-terminal interactions, observed in family 10 xylanases on protein stability under extreme conditions. The role of metal binding and aromatic clusters in protein stability is also discussed. Studying and understanding family 10 xylanase structure and function, can contribute to our protein engineering knowledge.
关键词：Family 10 Xylanase ; TIM barrel fold ; Thermal stability ; Metal binding ; Aromatic clusters ; Protein engineering