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A peptide corresponding to a potential polyphosphoinositide binding site of phospholipase C ‐β 2 enhances its catalytic activity
Author(s) -
Simoes Ana Paula,
Schnabel Petra,
Pipkom Rüdiger,
Camps Montserrat,
Gierschik Peter
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80346-v
Subject(s) - peptide , phospholipase c , enzyme , phospholipase , phosphoinositide phospholipase c , biochemistry , chemistry , recombinant dna , enzyme activator , peptide sequence , active site , stereochemistry , biology , gene
A peptide corresponding to a basic consensus amino acid motif present in both actin‐binding proteins and phosphoinositide‐specific phospholipases C was synthesized and its effect on the activity of a recombinant phospholipase C‐β 2 (PLCβ 2 ) expressed in baculovirus‐infected insect cells was studied. The peptide markedly and specifically stimulated the activity of the enzyme. This stimulatory effect required a particular primary and/or secondary structure of the peptide and occurred without lowering the affinity of the enzyme for Ca 2+ . The function of the PLCβ 2 segment corresponding to the peptide might be to bind and offer the substrate to the catalytic domain of this enzyme in a more favorable configuration or, alternatively, to interact with a hypothetical inhibitory constraint.