Open AccessLipase of Staphylococcus hyicus : Analysis of the catalytic triad by site‐directed mutagenesis
Author(s) -
Jäger Stephan,
Demleitner Gabriele,
Götz Friedrich
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb14048.x
Subject(s) - catalytic triad , lipase , site directed mutagenesis , mutagenesis , biochemistry , mutant , biology , insertional mutagenesis , enzyme , triacylglycerol lipase , chemistry , active site , gene
In this study the putative catalytic triad Ser‐His‐Asp of the Staphylococcus hyicus ssp. hyicus lipase was investigated. Putative catalytic sites determined by homology comparisons of three staphylococcal and other non‐staphylococcal lipases were altered by site‐directed mutagenesis. Since the mutations did not influence the secretion of the lipase, the decrease in lipase activity of the mutants strongly supports the proposed involvement of Ser 369 and His 600 in catalysis. Asp 559 is postulated to be the third amino acid of the triad.