PMID: 9161720May 1, 1997Paper

The structural and functional essentiality of the N-terminal alpha-helix in the phospholipase A2 of the Taiwan banded krait

Biochemistry and Molecular Biology International
L S ChangP F Wu

Abstract

In order to identify the structural and functional essentiality of the N-terminal alpha-helix of Bungarus multicinctus PLA2 for its enzymatic activity, comparative studies of the biochemical properties of native and recombinant PLA2 were made. It was found that the appearance of a Met residue preceding the N-terminus Asn-1 of the recombinant protein appreciably affected PLA2 activity and the hydrophobic character of the ANS-binding site. Additionally, the charged state and the hydrophobicity of the molecular surface changed as well. However, removal of the N-terminal Met-1 from the recombinant PLA2 resulted in the production of a fully active PLA2, whose biochemical properties were indistinguishable from those of the native enzyme. These observations, together with the findings that the helical wheel plot of the N-terminal alpha-helix showed distinct hydrophobic and hydrophilic faces and that the ANS-binding site was the active site of PLA2 enzymes, suggest that the hydrophobic face of the N-terminal alpha-helix in native PLA2 should be in the interior of the enzyme molecule for binding with ANS and the phospholipid/substrate.

Citations

Mar 17, 2004·Toxicon : Official Journal of the International Society on Toxinology·Lucimara Chioato, Richard J Ward

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