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Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
The Lipase Engineering Database: a navigation and analysis tool for protein families
Markus Fischer1, Jürgen Pleiss
1Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
Nucleic Acids Research
|January 10, 2003
Summary
The Lipase Engineering Database (LED) offers integrated data on lipase and esterase sequences, structures, and functions. This resource aids in analyzing enzyme relationships and designing mutants with specific substrate properties.
Area of Science:
- Biochemistry
- Bioinformatics
- Enzymology
Background:
- Lipases and esterases are crucial enzymes with diverse functions.
- Understanding their sequence-structure-function relationships is vital for protein engineering.
- Existing databases may lack comprehensive integration of these data.
Purpose of the Study:
- To develop and present the Lipase Engineering Database (LED).
- To provide a centralized resource for lipase, esterase, and related protein information.
- To facilitate the analysis of sequence-structure-function relationships in this enzyme class.
Main Methods:
- Integration of sequence, structure, and functional data for 806 protein entries.
- Classification into 38 homologous families and 16 superfamilies.
- Generation of multisequence alignments with annotated functional residues.
- Superposition and annotation of 45 experimental protein structures.
- Development of phylogenetic trees for navigation within superfamilies.
Main Results:
- The LED successfully integrates diverse data for lipases and esterases.
- Homologous proteins are organized into families and superfamilies, revealing evolutionary relationships.
- Functionally relevant residues, beyond the active site, are identified.
- The database supports systematic analysis of enzyme properties.
Conclusions:
- The Lipase Engineering Database (LED) is a valuable tool for researchers.
- It enables systematic analysis of sequence-structure-function relationships in lipases and esterases.
- LED facilitates the design of enzyme mutants with tailored substrate specificities.
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