Plant Phospholipases D: Case Study of Oat PLD

Plant Phospholipases D: Case Study of Oat PLD

DOI: 10.4018/978-1-5225-7482-8.ch005

Abstract

Studying phospholipases D (PLDs) from plants is very interesting as these enzymes might play important roles in many processes. PLDs are thought to cleave the phosphodiesteric bonds of the head group of phospholipids. The structure and function of oat (Avena sativa) PLD remain poorly understood, and their properties need to be further elucidated. In the chapter, functional proteomics and bioinformatic approaches were used to identify and characterize isoforms of oat PLD. Insights into structural characterization of oat predicted isozymes were analyzed using in silico approaches. Primary structures were analyzed, and a phylogeny analysis and protein motif/domain identification were presented. A multiple sequence alignment of the putative oat PLD revealed consensus sequences with the well-known important putative catalytic residues characterized by such enzymes. The results here provide a detailed view of the main residues involved in catalysis in this kind of enzyme.
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Background

Phospholipids (PLs) and related enzymes, i.e. phospholipases are important components of cells that worth better characterization either as cellular/molecular level or as external applications i.e., in food, pharmaceutical, and medicine, etc. For example, PLs could be used as emulsifiers, components of cosmetics, liposome preparations, and for medical formulations. A recent reflection done by Dowhan in 2017 highlighted some vital functions of PLs (Dowhan, 2017).

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