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A Phospholipase with a Novel Catalytic Triad
Author(s) -
Heinz Dirk W.
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19990816)38:16<2348::aid-anie2348>3.0.co;2-o
Subject(s) - triad (sociology) , catalytic triad , catalysis , chemistry , enzyme , substrate (aquarium) , phospholipase , sulfur , function (biology) , mutagenesis , stereochemistry , biochemistry , mutation , active site , biology , organic chemistry , genetics , psychology , ecology , gene , psychoanalysis
Catalytic triads are a long‐standing paradigm of enzyme catalysis. By using a “matched mutation” approach, that is, a simultaneous exchange of the protein (through mutagenesis) and the substrate (through substitution of oxygen atoms by sulfur atoms) followed by enzyme kinetic analysis, a novel catalytic triad (see figure) with an unusual amino acid composition is now proposed for a phospholipase that fulfills a dual function in catalysis.