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Protein Engineering vol. 4 no. 8 pp. 929-934, 1991
© 1991 Oxford University Press

RESEARCH-ARTICLE

Changes in activity of porcine phospholipase A2 brought about by charge engineering of a major structural element to alter stability

P.W. Goodenough1, K.M. Bhat, M.E. Collins, B.N. Perry, R.W. Pickersgill, I.G. Sumner, J. Warwicker, G.H. de Haas2 and H.M. Verheij2

Protein Engineering Department, AFRC Institute of Food Research, Reading Laboratory Shinfield, Reading RG2 9AT, UK 2Department of Enzymology and Protein Engineering, University of Utrecht 3508 TB Utrecht, The Netherlands

1To whom correspondence should be addressed

We have modified the stability of porcine phospholipase A2 by charge engineering. The mutations are situated at the N-terminal of a major helix and are N89D and N89D/E92Q. This engineering has significantly altered the activity of the enzyme to aggregated and monomeric substrates. A N89D/E92K mutant is more stable but considerably less active than wild type. An N89D mutant is more stable and of similar activity to wild type. The substantial change in activity may be due to direct interaction of residue 92 with aggregated substrate or may be via second calcium binding. Second calcium binding may be more probable as activity against monomers is also affected. Additional calcium binding may therefore be an important way of manipulating the activity of phospholipase A2.

Keywords: electrostatics/{alpha}-helices/pla2

Received March 3, 1991; revised August 12, 1991;
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