Stadler_1996_Biochim.Biophys.Acta_1304_229

Reference

Title : Inhibition of microbial lipases with stereoisomeric triradylglycerol analog phosphonates - Stadler_1996_Biochim.Biophys.Acta_1304_229
Author(s) : Stadler P , Zandonella G , Haalck L , Spener F , Hermetter A , Paltauf F
Ref : Biochimica & Biophysica Acta , 1304 :229 , 1996
Abstract :

1,2(2,3)-Diradylglycero O-(p-nitrophenyl) n-hexylphosphonates were synthesized, with the diradylglycerol moiety being di-O-octylglycerol, 1-O-hexadecyl-2-O-pyrenedecanylglycerol, or 1-O-octyl-2-oleoyl-glycerol, and tested for their ability to inactivate lipases from Chromobacterium viscosum (CVL) and Rhizopus oryzae (ROL). The experimental data indicate the formation of stable, covalent 1:1 enzyme-inhibitor adducts with the di-O-alkylglycero phosphonates. The differences in reactivity of diastereomeric phosphonates with opposite configuration at the glycerol backbone was less expressed with both enzymes tested as compared to the influence of the stereochemistry at the phosphorus. Both lipases exhibited the same preference for the chirality at the phosphorus that was independent from the absolute configuration at the glycerol backbone. However, with CVL and ROL the inhibitors with the active site serine-directed phosphonate linked at position sn-1 of the glycerol moiety reacted significantly faster than the corresponding sn-3 analogs, reflecting the sn-1 stereopreference of the enzymes towards triacylglycerol analogs with a sn-2 O-alkyl substituent. In contrast, the phosphonates based on the 1-O-octyl-2-oleoylglycerol did not significantly inactivate CVL. Unexpectedly, these substances were hydrolyzed in the presence of lipase.

PubMedSearch : Stadler_1996_Biochim.Biophys.Acta_1304_229
PubMedID: 8982269
Gene_locus related to this paper: burgl-lipas

Citations formats

Stadler P, Zandonella G, Haalck L, Spener F, Hermetter A, Paltauf F (1996)
Inhibition of microbial lipases with stereoisomeric triradylglycerol analog phosphonates
Biochimica & Biophysica Acta 1304 :229

Stadler P, Zandonella G, Haalck L, Spener F, Hermetter A, Paltauf F (1996)
Biochimica & Biophysica Acta 1304 :229