scholarly journals Fatty Acid Selectivity of Various Microbial Lipases for Esterification.

1996 ◽  
Vol 45 (1) ◽  
pp. 45-50 ◽  
Author(s):  
Hiroshi YAMASHITA ◽  
Setsuko HARA ◽  
Yoichiro TOTANI
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Selectivity ◽  
Microbial Lipases

scholarly journals Molecular basis of fatty acid selectivity in the zDHHC family of S-acyltransferases revealed by click chemistry

2017 ◽  
Vol 114 (8) ◽  
pp. E1365-E1374 ◽  
Author(s):  
Jennifer Greaves ◽  
Kevin R. Munro ◽  
Stuart C. Davidson ◽  
Matthieu Riviere ◽  
Justyna Wojno ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Click Chemistry ◽  
Mammalian Cells ◽  
Transmembrane Domain ◽  
Acyl Chain ◽  
Fatty Acid Selectivity ◽  
Molecular Determinants ◽  
Chain Acyl ◽  
Domain 3 ◽  
Acylated Proteins

S-acylation is a major posttranslational modification, catalyzed by the zinc finger DHHC domain containing (zDHHC) enzyme family. S-acylated proteins can be modified by different fatty acids; however, very little is known about how zDHHC enzymes contribute to acyl chain heterogeneity. Here, we used fatty acid-azide/alkyne labeling of mammalian cells, showing their transformation into acyl-CoAs and subsequent click chemistry-based detection, to demonstrate that zDHHC enzymes have marked differences in their fatty acid selectivity. This difference in selectivity was apparent even for highly related enzymes, such as zDHHC3 and zDHHC7, which displayed a marked difference in their ability to use C18:0 acyl-CoA as a substrate. Furthermore, we identified isoleucine-182 in transmembrane domain 3 of zDHHC3 as a key determinant in limiting the use of longer chain acyl-CoAs by this enzyme. This study uncovered differences in the fatty acid selectivity profiles of cellular zDHHC enzymes and mapped molecular determinants governing this selectivity.

Fatty acid selectivity of a lipase purified from Vernonia galamensis seed

1995 ◽  
Vol 1257 (2) ◽  
pp. 149-156 ◽  
Author(s):  
Ignatious Ncube ◽  
Thomas Gitlesen ◽  
Patrick Adlercreutz ◽  
John S. Read ◽  
Bo Mattiasson
Keyword(s):  
Fatty Acid ◽  
Vernonia Galamensis ◽  
Fatty Acid Selectivity

Evaluation of the fatty acid selectivity of a phosphatidylinositol-specific cytosolic phospholipase C from pig and human platelets

1984 ◽  
Vol 62 (2-3) ◽  
pp. 115-120 ◽  
Author(s):  
Bruce J. Holub ◽  
Bernadette Celi
Keyword(s):  
Fatty Acid ◽  
Phospholipase C ◽  
Human Platelets ◽  
Gas Liquid Chromatography ◽  
Fatty Acid Selectivity ◽  
Sheep Liver ◽  
Cytosolic Phospholipase ◽  
Naturally Occurring ◽  
Relative Conversion ◽  
Fatty Acid Compositions

The fatty acid selectivity of cytosolic phospholipase C (phosphatidylinositol phosphodiesterase) from pig and human platelets towards phosphatidylinositol was evaluated. For this purpose, the relative conversion of rat liver phosphatidylinositol (enriched in stearate and arachidonate) and sheep liver phosphatidylinositol (enriched in stearate plus oleate and containing linoleate and arachidonate) was compared and, in addition, the fatty acid compositions of the diacylglycerol products were determined by gas–liquid chromatography. The cytosolic enzyme exhibited essentially complete specificity for phosphatidylinositol when choline-, ethanolamine-, serine-, or inositol-containing phospholipids labelled with [14C]stearate were tested as substrates. Similar percentage conversions of rat and sheep liver phosphatidylinositols to 1,2-diacylglycerol were found with phospholipase C from either pig or human platelets. Furthermore, the newly formed diacylglycerols and the unreacted phospholipid had fatty acid compositions which were very similar to the corresponding substrates. These results suggest that the phospholipase C from isolated platelet cytosol is highly selective towards phosphatidylinositol, but not with respect to the fatty acid composition of naturally occurring phosphatidylinositol. They also suggest that any preferential release of arachidonoyl diacylglycerol in stimulated human platelets is more likely controlled by compartmentation of the corresponding phosphatidylinositol precursor within platelet membranes and its availability, rather than directly by a marked enzyme preference for arachidonate-containing species.

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