The Enzymatic Activity of Lipases Correlates with Polarity-Induced Conformational Changes: A Trp-Induced Quenching Fluorescence Study

Triacylglycerol hydrolases (EC 3.1.1.3) are thought to become activated when they encounter the water–lipid interface causing a “lid” region to move and expose the catalytic site. Here, we tested this idea by looking for lid movements in Thermomyces lanuginosus lipase (TL lipase), and in variants wi...

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Veröffentlicht in:	Biochemistry (Easton) 2015-07, Vol.54 (27), p.4186-4196
Hauptverfasser:	Skjold-Jørgensen, Jakob, Bhatia, Vikram K, Vind, Jesper, Svendsen, Allan, Bjerrum, Morten J, Farrens, David
Format:	Artikel
Sprache:	eng
Schlagworte:	Ascomycota - chemistry Ascomycota - enzymology Ascomycota - metabolism Enzyme Activation Enzyme Stability Lipase - chemistry Lipase - metabolism Models, Molecular Protein Conformation Solvents - chemistry Spectrometry, Fluorescence
Online-Zugang:	Volltext
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