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

Tomohisa Ogawa, Yasuyuki Shimohigashi, Motonori Ohno

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)955-960
Number of pages6
JournalJournal of biochemistry
Volume122
Issue number5
DOIs
Publication statusPublished - 1997 Nov

Keywords

  • Arachidonoyl phosphatidylcholine
  • Phospholipase A
  • Site-directed mutagenesis
  • Snake venom

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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