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Understanding Structural Features of Microbial Lipases—An Overview

Author(s): John Geraldine Sandana Mala | Satoru Takeuchi

Journal: Analytical Chemistry Insights
ISSN 1177-3901

Volume: 3;
Start page: 9;
Date: 2008;
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Keywords: active site | bioinformatics | Candida rugosa lipase | crystallization | lipase structure | structure prediction

The structural elucidations of microbial lipases have been of prime interest since the 1980s. Knowledge of structural features plays an important role in designing and engineering lipases for specific purposes. Significant structural data have been presented for few microbial lipases, while, there is still a structure-deficit, that is, most lipase structures are yet to be resolved. A search for ‘lipase structure’ in the RCSB Protein Data Bank ( returns only 93 hits (as of September 2007) and, the NCBI database ( reports 89 lipase structures as compared to 14719 core nucleotide records. It is therefore worthwhile to consider investigations on the structural analysis of microbial lipases. This review is intended to provide a collection of resources on the instrumental, chemical and bioinformatics approaches for structure analyses. X-ray crystallography is a versatile tool for the structural biochemists and is been exploited till today. The chemical methods of recent interests include molecular modeling and combinatorial designs. Bioinformatics has surged striking interests in protein structural analysis with the advent of innumerable tools. Furthermore, a literature platform of the structural elucidations so far investigated has been presented with detailed descriptions as applicable to microbial lipases. A case study of Candida rugosa lipase (CRL) has also been discussed which highlights important structural features also common to most lipases. A general profi le of lipase has been vividly described with an overview of lipase research reviewed in the past.
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