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Lipases and esterases: a review of their sequences, structure and evolution
H W Anthonsen1, A Baptista, F Drabløs
1MR-Center, SINTEF UNIMED, Trondheim, Norway.
Biotechnology Annual Review
|January 1, 1995
Summary
This review analyzes lipases and esterases, focusing on conserved residues and structure-function relationships. We explore interfacial activation and pH effects, highlighting NMR
Area of Science:
- Biochemistry
- Enzymology
Background:
- Lipases and esterases form a large enzyme family with diverse functions.
- Understanding their structure-function relationships is crucial due to a growing number of sequences and limited 3D structures.
Purpose of the Study:
- To review the enzyme family of lipases and esterases.
- To analyze sequences, 3D structures, and pH-dependent electrostatic signatures.
- To identify conserved residues and understand structure-function relationships.
Main Methods:
- Comparative analysis of enzyme sequences and 3D structures.
- Identification of conserved residues in active sites.
- Analysis of pH-dependent electrostatic signatures and isopotential surfaces.
Main Results:
- Identified similarities and differences in active sites among lipases and esterases.
- Highlighted conserved residues important for structural integrity and activity.
- Presented pH variations in isopotential surfaces for selected lipases.
Conclusions:
- Conserved residues play key roles in protein structure, activity, and specificity.
- Functional diversity arises from differences in surface residue utilization, particularly charged residues.
- NMR shows promise as a tool for studying lipase and esterase kinetics.