Thioesterase and protein deacylase activities of porcine pancreatic phospholipase A2.
The thioesterase activity of porcine pancreatic phospholipase A2 has been investigated with non-phospholipid substrates. The acyl-CoA hydrolase activity towards acyl-CoA derivatives is specific for long chain fatty acids (14 C, 16 C) but is unable to hydrolyze short chain acyl-CoA compounds (below 8 C). The same enzyme also shows protein deacylase activity liberating [3H]palmitic acid from [3H]palmitoyl-acyl carrier protein.
Nocito
M
M
Department of Immunology, Hospital Ramón y Cajal, Madrid, Spain.
Roy
G
G
Villar
L M
LM
Palacios
C
C
Serrano
A
A
Alvarez-Cermeño
J C
JC
González-Porqué
P
P
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D010170:Palmitoyl-CoA Hydrolase / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D013552:Swine; D013869:Thiolester Hydrolases / Q000378:metabolism*
D000217:Acyltransferases; C065617:acyl carrier protein acylase; D010741:Phospholipases A; D054467:Phospholipases A2; D013869:Thiolester Hydrolases; D010170:Palmitoyl-CoA Hydrolase