Abstract
PHOSPHOLIPASE A2 (EC 3.1.1.4) catalyses the hydrolysis of the fatty acid ester bond at the 2-position of 1,2 diacyl sn-phosphoglycerides, and has been purified from many sources, such as mammalian pancreas1,2, snake venom3 and bee venom4. In mammals, the enzyme is produced as a precursor, which trypsin can convert into active phospholipase A2 by splitting the peptide bond Arg 7–Ala 8, with the removal of the N-terminal heptapeptide from the molecule5. The activity of the different phospholipases A2 depends on the physical state of the substrate. The enzyme from snake venom is highly active when the substrate is tightly packed in a membrane. Mammalian phospholipases cannot attack membranes; they can degrade the lecithin molecules most effectively when these are more loosely packed in micelles. All phospholipases also have some activity towards substrates in a monomeric solution. The precursors from mammalian pancreas phospholipases are also active towards the monomeric substrate molecules, but inactive to substrates in micellar form6. The primary structure of many of the phospholipases A2 is known. They have a single polypeptide chain of approximately 130 amino acid residues and six or seven disulphide bridges7–10. There is a high degree of homology between all the enzymes. We report here the three-dimensional structure of one of these enzymes, prephospholipase A2 from porcine pancreas.
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DRENTH, J., ENZING, C., KALK, K. et al. Structure of porcine pancreatic prephospholipase A2. Nature 264, 373–377 (1976). https://doi.org/10.1038/264373a0
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DOI: https://doi.org/10.1038/264373a0
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