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The fungus Candida rugosa produces several lipase isoenzymes and the 3D structure of two were solved (Lip1 and Lip3). We have isolated homodimers of Lip3 isoenzyme, maintained by hydrophobic interactions, which were stable in aqueous solutions. Under kinetic conditions, the dimers were still functional and showed an increased capability to hydrolysed soluble triacylglycerides compared to the monomeric...
We have investigated the interfacial activation process of two isoenzymes from Candida rugosa (Lip1 and Lip3) using triacetin as substrate. Kinetics were coupled to inhibition experiments in order to analyse the transition between the open and closed conformers. This process was slow, particularly for Lip1, in the absence of an interface provided by the substrate or a detergent. Dimers of Lip3 were...
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