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Enzyme Activity Measurement for Phospholipase A1

Creative Enzymes is committed to being the most reliable service provider in the field of enzyme assays. We are well known for the high rate of customer satisfaction. Our prompt service, best customer care, and dedicated resources have made us a most preferred vendor in the global market. Herein, Creative Enzymes is proud to offer the precise enzymatic assay for phospholipase A1.

Phospholipase A1 (EC; phosphatidylcholine 1-acylhydrolase; PLA1) is an enzyme that hydrolyzes ester bonds of phospholipids at the sn-1 position and yields 2-acyl-lysophospholipids and fatty acids (FFAs). Both phospholipase A1 and phospholipase A2 (EC; phosphatidylcholine 2-acylhydrolase; PLA2) cleave glycerophospholipids into lysophospholipid and free fatty acids. They are classified as PLA1 and PLA2 based on whether they cleave the sn-1 or sn-2 position of phospholipids, respectively. PLA1 activities have been detected in many cells and tissues from various organisms, such as rat platelets, bovine brain, testis, hornet venom, bonito muscle, and fungi. Recently, several PLA1 isozymes have been identified and much has been learned about the structure and molecular function of PLA1. Currently nine PLA1 enzymes are known in mammals; six are extracellular enzymes and the other three are intracellular enzymes. The intracellular and extracellular PLA1’s share no sequence homologies and apparently have distinct functions. Some PLA1’s have a broad substrate specificity and hydrolyze both phospholipids and triacylglycerol (TG) as well as galactolipids. By contrast, other PLA1’s such as phosphatidylserine (PS)-specific PLA1 (PS-PLA1), membrane-associated phosphatidic acid (PA)-selective PLA1α (mPA-PLA1α), and mPA-PLA1β show a strict substrate specificity and specifically act on PS and PA. These PLA1’s may play a specific role in yielding bioactive lysophospholipids, lysophosphatidylserine (LPS), and lysophosphatidic acid (LPA). All extracellular PLA1 molecules belong to the pancreatic lipase gene family.

Enzyme Activity Measurement for Phospholipase A1 Figure 1: Catalytic reactions and products of PLA1 and PLA2.
Reference: Murayama K, Kano K, Matsumoto Y, et al. Journal of structural biology, 2013, 182(2): 192-196.

Functionally, PLA1’s play a pivotal role in medicine, nutrition, pharmaceutical, and food industries. For example, the recombinant PLA1 represents a good candidate for wasp venom immunotherapy. Moreover, PLA1 improves the foaming stability and properties of skim milk and whey, implying that PLA1 can be a useful tool for modifying the functionality of dairy products and ingredients. Recently, PLA1 has been reported as a potential processing aid in cheese-making, and a significant increase of cheese yield on a pilot as well as on an industrial scale was reported. Ultimately, it can be seen that PLA1’s serve as a critical part in many processes, and thus more detailed studies on these enzymes will start soon, which rely on proper enzymatic assays.

Creative Enzymes is a leading company of high-quality bioanalytical services and contract custom research specialized in enzyme activity analysis serving the needs of clients from the pharmaceutical, biotechnological, and environmental industries. We are fully prepared to offer the accurate activity assays for PLA1’s. The activities of PLA1’s are determined by using the fluorometric assays. Our test results are the most trusted and proven in the global market. Overall, Creative Enzymes is your best choice during development of products containing PLA1.

Enzyme Activity Measurement for Phospholipase A1 Figure 2: Ribbon representation of the PLA1 structure from Streptomyces albidoflavus NA297. Secondary structural elements are colored blue (helices) and pink (strands); aa residues in the active site are indicated as stick models.
Reference: Murayama K, Kano K, Matsumoto Y, et al. Journal of structural biology, 2013, 182(2): 192-196.

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