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

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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Ogawa T,Shimohigashi Y,Ohno M

doi

10.1093/oxfordjournals.jbchem.a021857

subject

Has Abstract

pub_date

1997-11-01 00:00:00

pages

955-60

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

122

pub_type

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