Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Chang RC, Chen JC and ShawJF
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------>journal_name=Biochem. Biophys. Res. Commun.
------>paper_name=Facile purification of highly active recombinant Staphylococcus hyicus lipase fragment and characterization of a putative lid region.
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------>fullAbstract=A fragment of Staphylococcus hyicus lipase gene (Ala248 to Ala640) was inserted into plasmid pET20(b+). The resulting His-tagged recombinant protein (49 kDa) was overexpressed in Escherichia coli BL21(DE3) as an highly active lipase and was purified by nickel-coupled resin. Site-directed mutagenesis showed that in comparison with wild type enzyme, the L326F and L326A enzymes showed a 3.4 and 5 fold increase in the K(m), respectively, but only a 44% and a 64% decrease in the kcat/K(m), respectively, suggesting that Leu326 of the putative lid participated in substrate-binding.
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------>authors=Chang RC, Chen JC and ShawJF
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------>updateTitle=Facile purification of highly active recombinant Staphylococcus hyicus lipase fragment and characterization of a putative lid region.
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------>publish_year=1996
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z