EC Number   |
General Information |
Reference |
|---|
   3.1.1.111 | physiological function |
both wild-type and the natural splicing variant bind to heparin. The heparin binding site is located in N-terminal region of the enzyme |
754052 |
| 3.1.1.111 | physiological function |
enzyme stimulates histamine release from rat peritoneal mast cells through production of 2-acyl-1-lyso-phosphatidylserine in the presence of FcepsilonRI cross-linker. The potency of 2-acyl-1-lyso-phosphatidylserine is almost equal to that of 1-acyl-2-lyso-phosphatidylserine. The enzyme stimulates the histamine release more efficiently when rat peritoneal mast cells are mixed with apoptotic Jurkat cells. Heparin has affinity for PS-PLA1 and completely blocks the stimulatory effect of the enzyme |
754062 |
| 3.1.1.111 | physiological function |
isoform Ps-PLA1beta shows high affinity to heparin |
754071 |
| 3.1.1.111 | physiological function |
PLA1A is upregulated by hepatitis C virus HCV infection, and PLA1A knockdown significantly reduces J399EM (genotype 2a) HCV propagation at the assembly step but not the entry, RNA replication, and protein translation steps of the life cycle. PLA1A has a role in the interaction of viral proteins NS2-E2 and NS2-NS5A. PLA1A stabilizes the nonstructural proteins NS2/NS5A dotted structure during infection |
754543 |
| 3.1.1.111 | physiological function |
review on extracellular PLA1s including phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta. The tertiary structures of lipases show two surface loops, the lid and the beta9 loop. The lid and the beta9 loop cover the active site in its closed conformation. Phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta have short lids and short loops. They specifically hydrolyze phospatidylserine and phosphatidic acid, respectively, producing their corresponding lysophospholipids |
752867 |
