Links between kinetic data and sequences in the alpha/beta-hydrolases fold database

Area of Science:

• Biochemistry
• Structural Biology
• Bioinformatics

Background:

• The rapid increase in sequenced genes contrasts with a more limited number of protein structural families.
• Experimental data on protein sequences, mutations, and functions are often sparse in current databases.
• Homologous proteins can exhibit diverse roles due to variations in enzymatic activity or protein interactions.

Purpose of the Study:

• To establish links between experimental kinetic data and protein sequences, mutations, and structures within the ESTHER database.
• To enhance the functional annotation of protein families, specifically alpha/beta-hydrolases.
• To facilitate the integration of pharmacological data with large-scale genomic databases.

Main Methods:

• Developing and implementing methods to associate experimental kinetic data with specific protein entries in the ESTHER database.
• Curating and linking sequence, mutation, structural, and kinetic information for alpha/beta-hydrolases.
• Exploring data integration strategies between the ESTHER database and genome-wide resources.

Main Results:

• Demonstrated the feasibility of linking diverse experimental data types (kinetic, sequence, mutation, structure) for protein families.
• Established a framework for enriching protein annotations with functional and structural information.
• Initiated the process of connecting protein-specific experimental data with broader genomic contexts.

Conclusions:

• Integrating experimental kinetic data with protein sequence, mutation, and structure information significantly enhances functional characterization.
• The ESTHER database serves as a model for linking detailed experimental data to protein families.
• This approach paves the way for integrating pharmacological data into genome-wide databases, advancing drug discovery and protein engineering.