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[The structure-function relationship of thermostable beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology - 1 Jan 2005

Yang Xue-Peng, Yang Shou-Jun, Han Bei-Zhong, Jin Cheng

Abstract excerpt

Beta-glycosidase (Tngly) from the thermophilic eubacterium Thermus nonproteolyticus HG102, which is a thermostable monomeric protein and adopts the (beta/alpha)8 barrel fold, is an excellent model system to be investigated for the thermostable mechanism, activity and substrate specificity. Here, based on the analysis of structural basis for thermostability of Tngly (Wang et al, 2003) and comparison of other...

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PMID: 15859334

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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