PLA1A Human

Phospholipase A1 Member A (PLA1A) is an enzyme that plays a crucial role in the metabolism of phospholipids. It is part of the phospholipase family, which is responsible for hydrolyzing phospholipids to produce lysophospholipids and fatty acids. PLA1A is particularly significant due to its involvement in various biological processes, including membrane maintenance, remodeling, and the regulation of cellular mechanisms.

PLA1A is a protein-coding gene that produces a single, non-glycosylated polypeptide chain consisting of 454 amino acids . The recombinant form of PLA1A is typically produced in Escherichia coli (E. coli) and is fused to a 23 amino acid His-tag at the N-terminus to facilitate purification . The molecular mass of the recombinant PLA1A is approximately 49.5 kDa .

PLA1A hydrolyzes phospholipids at the sn-1 position, resulting in the formation of 2-acyl-lysophospholipids and fatty acids . This enzymatic activity is conserved across a wide range of organisms and is essential for various cellular functions. PLA1A acts as a digestive enzyme, plays a central role in membrane maintenance and remodeling, and regulates important cellular mechanisms by producing lysophospholipid mediators such as lysophosphatidylserine and lysophosphatidic acid .

The PLA1A gene is associated with several diseases, including poor metabolism of thiopurines and methylmalonic aciduria and homocystinuria, cblC type . Understanding the function and regulation of PLA1A is crucial for developing therapeutic strategies for these conditions.

Recombinant PLA1A is used in various research applications to study its enzymatic activity, structure-function relationships, and potential therapeutic uses. It is also employed in biochemical assays to investigate the role of phospholipids in cellular processes.