Report for: Data built from an AQL search

 
12 rows returned
Mutation Text txt
A379V_human-PLA2G7 p.Val379Ala GTA->GCA rs1051931 Natural mutant
D166E_human-PLA2G7 Natural mutant
I198T_human-PLA2G7 Common polymorphism; associated with asthma and atopy. rs1805018 Natural mutant
I317N_human-PLA2G7 p.I317N Ile317Asn c.950T>A exon 10 compound heterozygote with the common V279F mutation. This mutation would create a new N-linked glycosylation site (N-X-S) on the Lp-PLA2 protein Natural mutant
K191N_human-PLA2G7 p.Lys191Asn AAG->AAC rs45454695 Natural mutant
Q281R_human-PLA2G7 p.Q281R Gln281Arg rs201256712 Natural mutant
R92H_human-PLA2G7 p.Arg92His CGC->CAC Common polymorphism; rs1805017 Natural mutant
V279F_human-PLA2G7 p.V279F Val279Phe c.G994T in PAFAD; loss of function; risk factor for coronary arthery disease and stroke. rs76863441 Natural mutant
Y63X_human-PLA2G7 p.Y63X Tyr63Ter c.191insA (exon 3) found in an heterozygote patient Natural mutant
F322H_human-PLA2G7 Tentative to engineer plasma platelet-activating factor acetylhydrolase by amino acid substitution into OP-hydrolyzing variants (bioscavengers). L153H, and F322H have essentially no hydrolytic activity against the nerve agents tested. In contrast, the W298H mutant displayed novel somanase activity with a kcat of 5min-1 and a KM of 590muM at pH7.5. Site directed mutagenesis
L153H_human-PLA2G7 Tentative to engineer plasma platelet-activating factor acetylhydrolase by amino acid substitution into OP-hydrolyzing variants (bioscavengers). L153H, and F322H have essentially no hydrolytic activity against the nerve agents tested. In contrast, the W298H mutant displayed novel somanase activity with a kcat of 5min-1 and a KM of 590muM at pH7.5. Site directed mutagenesis
W298H_human-PLA2G7 Tentative to engineer plasma platelet-activating factor acetylhydrolase by amino acid substitution into OP-hydrolyzing variants (bioscavengers). L153H, and F322H have essentially no hydrolytic activity against the nerve agents tested. In contrast, the W298H mutant displayed novel somanase activity with a kcat of 5min-1 and a KM of 590muM at pH7.5. Site directed mutagenesis

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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