Publication | Closed Access
Biology and Biochemistry of Plant Phospholipases
92
Citations
126
References
2011
Year
Plant Molecular BiologyBiosynthesisEngineeringBotanyBiochemistryPlant Phospholipase FamilyNatural SciencesVarious Phospholipase IsoformsMolecular BiologyAbstract PhospholipasesPlant BiochemistryCellular BiochemistryPlant PhospholipasesPlant Physiology
Abstract Phospholipases are a complex group of enzymes that hydrolyze phospholipids. The plant phospholipase family is composed of multiple members with varying positional specificity, and each type is represented by multiple isoforms distinguishable by their structural, catalytic, and physiological characteristics. A large number of phospholipase genes and gene families have been identified and the biochemical properties of several members have been characterized, revealing considerable molecular and catalytic diversity. Forward and reverse genetics has further revealed that phospholipases are widely involved in physiological processes including lipid metabolism, cell signaling, and responses to biotic and abiotic stresses. Such studies have highlighted the potential biotechnological value of phospholipases as targets for improving stress tolerance. The catalytic diversity of various phospholipase isoforms is also of increasing interest for industrial biocatalysis. This review focuses on recently acquired information on biochemical, molecular and functional aspects of plant phospholipases. Keywords: phospholipaselipid metabolismlipid messengerssignal transductionphosphatidic acidstress responseslipid acyl hydrolaselipasedroughtwoundingcell elongationshoot gravitropismlysophospholipiddiacylgly- cerol ACKNOWLEDGMENTS The authors gratefully acknowledge the support of the Natural Sciences and Engineering Research Council of Canada, AVAC Ltd, and the Canada Research Chairs Program. This work is also part of the European Commission Seventh Framework Programme sponsored project: Industrial Crops producing value Oils for Novel chemicals (ICON). We would like to thank Dr. David Hildebrand for reviewing the manuscript.
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