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Structural and biochemical data of Trichoderma harzianum GH1 ?-glucosidases.

ABSTRACT: Here the statistics concerning X-ray data processing and structure refinement are given, together with the substrate preference analysis for ThBgl1 and ThBgl2. Finally, the analysis of the influence of temperature and pH on the activities of both enzymes are shown.

SUBMITTER: Florindo RN

PROVIDER: S-EPMC5712062 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Structural and biochemical data of <i>Trichoderma harzianum</i> GH1 β-glucosidases.

Florindo Renata N RN Souza Valquiria P VP Mutti Hemily S HS Margarido Lívia R Manzine LRM Camilo Cesar C Marana Sandro R SR Polikarpov Igor I Nascimento Alessandro S AS

Data in brief 20170922

Here the statistics concerning X-ray data processing and structure refinement are given, together with the substrate preference analysis for ThBgl1 and ThBgl2. Finally, the analysis of the influence of temperature and pH on the activities of both enzymes are shown. ...[more]

PMID: 29214196

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Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions.

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