Molecular characterization of the patatin multigene family of potato
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Structure characterization and potential role of soybean phospholipases A multigene family in response to multiple abiotic stress uncovered by CRISPR/Cas9 technology
2021, Environmental and Experimental BotanyCitation Excerpt :The classification is based on the site of bond cleavage in their phospholipid substrates (Aloulou et al., 2012; Hao et al., 2012). The sub-class phospholipase A (PLAs) have intensively been studied in Arabidopsis (Chen et al., 2013), potato (Mignery et al., 1988) and rice (Singh et al., 2012). Arabidopsis and rice genomes have 29 and 31 PLA proteins, respectively, which are further categorized into phospholipase A1 (PLA1), patatin-like PLAs (pPLA) and low molecular weight of secretory phospholipase A2 (sPLA2) (Ryu, 2004).
Biotechnological Approaches
2016, Ecofriendly Pest Management for Food SecurityScreening for hydrolytic enzymes reveals Ayr1p as a novel triacylglycerol lipase in Saccharomyces cerevisiae
2013, Journal of Biological ChemistryCitation Excerpt :Tgl3p, Tgl4p, and Tgl5p share a common consensus sequence GXSXG, where serine is the essential residue of the catalytic triad aspartic acid/glutamic acid and histidine (17). They also contain a patatin domain, named after a plant storage protein that possesses lipid acylhydrolase activity (18). In vitro, all three proteins exhibit lipolytic activity, whereas in vivo only Tgl3p and Tgl4p mobilize TG efficiently.
Subchronic toxicity evaluation of potato protein isolates
2012, Food and Chemical ToxicologyCitation Excerpt :While these values are low in relation to many other vegetable sources of dietary protein (Singh and Kaur, 2009), potato proteins have been noted to have high protein biological values, in the range of 90–100 (Camire et al., 2009), which compares well to other foodstuffs commonly associated with having high quality protein content such as whole eggs, soybean, and beans, where corresponding protein biological values of 100, 84, and 73, respectively, have been reported. Patatin is the major protein present in potato tubers, making up about 40% of the water soluble protein (Mignery et al., 1988; Shewry, 2003), and has been reported to have allergenic properties in sensitive individuals (Camire et al., 2009; Seppälä et al., 1999, 2000). However, this allergenicity is greatly reduced upon heating (Koppelman et al., 2002).
Characteristics of plant pre-mrna introns and transposable elements
2012, Plant Molecular Biology LabFax: A Volume in LabFaxAlteration of plasma membrane-bound redox systems of iron deficient pea roots by chitosan
2011, Journal of ProteomicsCitation Excerpt :It is possible that soluble HSP, which are often regulated under different stresses, inherit more essential roles in the long-term stress response [46]. A patatin (spot no. 845) decreased specifically under iron deficiency was identified and regulation of patatins by stress was already observed in the past [47]. Patatins known as storage proteins also have an enzymatic activity as a lipid acyl hydrolase [48].
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