Literature DB >> 1478461

Lipase of Staphylococcus hyicus: analysis of the catalytic triad by site-directed mutagenesis.

S Jäger1, G Demleitner, F Götz.   

Abstract

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 Ser369 and His600 in catalysis. Asp559 is postulated to be the third amino acid of the triad.

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Year:  1992        PMID: 1478461     DOI: 10.1111/j.1574-6968.1992.tb14048.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  4 in total

1.  Genetic and biochemical characterization of a new extracellular lipase from Streptomyces cinnamomeus.

Authors:  P Sommer; C Bormann; F Götz
Journal:  Appl Environ Microbiol       Date:  1997-09       Impact factor: 4.792

2.  Purification and characterization of extracellular Staphylococcus warneri lipase.

Authors:  R Talon; N Dublet; M C Montel; M Cantonnet
Journal:  Curr Microbiol       Date:  1995-01       Impact factor: 2.188

3.  Nucleotide sequence of a novel arylesterase gene from Vibro mimicus and characterization of the enzyme expressed in Escherichia coli.

Authors:  J F Shaw; R C Chang; K H Chuang; Y T Yen; Y J Wang; F G Wang
Journal:  Biochem J       Date:  1994-03-15       Impact factor: 3.857

4.  Role of lipase from community-associated methicillin-resistant Staphylococcus aureus strain USA300 in hydrolyzing triglycerides into growth-inhibitory free fatty acids.

Authors:  Brigitte Cadieux; Vithooshan Vijayakumaran; Mark A Bernards; Martin J McGavin; David E Heinrichs
Journal:  J Bacteriol       Date:  2014-09-15       Impact factor: 3.490

  4 in total

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