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Título

Activation in the family of Candida rugosa isolipases by polyethylene glycol

AutorOtero, Cristina; Fernández-Pérez, Mónica; Hermoso, Juan A. ; Martínez-Ripoll, Martín
Palabras claveLipase
Candida rugosa
Cholesterol esterase
Activation
Polyethylene glycol
Fecha de publicación11-jun-2005
EditorElsevier
CitaciónJournal of Molecular Catalysis B: Enzymatic 32 (2005) 225–229
ResumenWe have investigated activation of two isoenzymes (lip1 and lip3) from Candida rugosa in polyethylene glycol (PEG) media. Aqueous solutions of PEG 8000 and 20,000 activate lip3 but not lip1 from C. rugosa. Maximum activation (260%) of lip3 requires 6 h of pre-incubation with PEG 8000 (4%, w/v). PEG seems to shift the equilibrium between the open and the closed forms of lip3 towards the active conformation. Inhibition experiments demonstrate that ligands have easier access to the lip3 active site than to the lip1 active site, both in the presence and the absence of PEG. The presence of PEG in the crystallization medium is responsible for reported differences in the crystal structures of lip1 and lip3. A comparative analysis of crystallographic models of lip1 and lip3 suggests a role for PEG in activation of lip3 and further stabilization of the activated/open form via dimerization in aqueous media.
DescripciónDisponible en: http://www.xtal.iqfr.csic.es/publications/jmolcat2005.pdf
Versión del editorhttp://dx.doi.org/10.1016/j.molcatb.2004.12.008
URIhttp://hdl.handle.net/10261/12522
DOI10.1016/j.molcatb.2004.12.008
ISSN1381-1177
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