THIOESTERASE AND PROTEIN DEACYLASE ACTIVITIES OF PORCINE PANCREATIC PHOSPHOLIPASE A(2)

Authors
NOCITO M ROY G VILLAR LM PALACIOS C SERRANO A ALVAREZCERMENO JC GONZALEZPORQUE P
Citation
M. Nocito et al., THIOESTERASE AND PROTEIN DEACYLASE ACTIVITIES OF PORCINE PANCREATIC PHOSPHOLIPASE A(2), Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1299(1), 1996, pp. 17-22
Citations number
23
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta, L. Lipids and lipid metabolism → ACNP
ISSN journal
00052760
Volume
1299
Issue
1
Year of publication
1996
Pages
17 - 22
Database
ISI
SICI code
0005-2760(1996)1299:1<17:TAPDAO>2.0.ZU;2-J
Abstract
The thioesterase activity of porcine pancreatic phospholipase A, has b een investigated with non-phospholipid substrates. The acyl-CoA hydrol ase activity towards acyl-CoA derivatives is specific for long chain f atty acids (14 C, 16 C) but is unable to hydrolyze short chain acyl-Co A compounds (below 8 C). The same enzyme also shows protein deacylase activity liberating [H-3]palmitic acid from [H-3]palmitoyl-acyl carrie r protein.