3 results match your criteria: "CNRS-Aix-Marseille Université-Enzymologie Interfaciale et Physiologie de la Lipolyse-UPR 9025[Affiliation]"
Biochim Biophys Acta
December 2010
CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse UPR 9025, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France.
Phospholipase Cs (PLCs) contribute importantly to the virulence and pathogenicity of several bacteria. It has been reported in previous studies that mutations in the four predicted plc genes of Mycobacterium tuberculosis inhibit the growth of these bacteria during the late phase of infection in mice. These enzymes have not yet been fully characterised, mainly because they are not easy to produce in large quantities.
View Article and Find Full Text PDFBiochim Biophys Acta
April 2010
CNRS-Aix-Marseille Université-Enzymologie Interfaciale et Physiologie de la Lipolyse-UPR 9025, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
Monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG) are the most abundant lipids in nature, mainly as important components of plant leaves and chloroplast membranes. Pancreatic lipase-related protein 2 (PLRP2) was previously found to express galactolipase activity, and it is assumed to be the main enzyme involved in the digestion of these common vegetable lipids in the gastrointestinal tract. Most of the previous in vitro studies were however performed with medium chain synthetic galactolipids as substrates.
View Article and Find Full Text PDFBiochim Biophys Acta
October 2009
CNRS-Aix-Marseille Université-Enzymologie Interfaciale et Physiologie de la Lipolyse-UPR 9025, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
Galactolipids are the main lipids from plants and galactolipases play a major role in their metabolism. These enzymes were however poorly studied so far and only few assays have been developed. A specific and continuous galactolipase assay using synthetic medium chain monogalactosyl diacylglycerol (MGDG) as substrate was developed using the pH-stat technique and recombinant human (rHPLRP2) and guinea pig (rGPLRP2) pancreatic lipase-related protein 2 as model enzymes.
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