Evidence for functional involvement of asparagine 67 in substrate recognition by snake venom phospholipases A2

Journal of Biochemistry
T OgawaM Ohno

Abstract

Site-directed mutagenesis studies of recombinant Trimeresurus flavoviridis venom gland phospholipase A2 (PLA2) showed that the Asn residue at position 67 takes part in recognition of the substrate 2-arachidonoyl sn-glycero-3-phosphocholine in both monomeric and micellar states. The amount of arachidonate released from phosphatidylcholine mixed micelles was reduced to 30% for N67D and N67K mutants, and to 70% for N67G mutant, but remained unchanged for N67S mutant. In contrast, for monomeric substrate, the activity was decreased to 40% for N67D and N67G and to 60% for N67K but remained unchanged for N67S. These results suggest that the properties of the side chain of residue 67 exert a significant influence on recognition of 2-arachidonoyl sn-glycero-3-phosphocholine.

Citations

Mar 17, 2004·Toxicon : Official Journal of the International Society on Toxinology·R Manjunatha Kini
Mar 17, 2004·Toxicon : Official Journal of the International Society on Toxinology·Motonori OhnoShosaku Hattori
Sep 11, 2002·Toxicon : Official Journal of the International Society on Toxinology·Inn-Ho TsaiYing-Ming Wang
Jul 13, 2006·The Biochemical Journal·R Manjunatha Kini
Oct 31, 2008·Chembiochem : a European Journal of Chemical Biology·Silke C WenzelRolf Müller

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