Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p

• DOI: 10.1016/j.bbalip.2016.02.005
• Publication Date: 2016-02-09T07:16:29Z
• Authors: Philipp Aschauer; Srinivasan Rengac...; Joerg Lichtenegger; Matthias Schittmayer; Krishna Mohan Pad...; Nicole Mayer; Rolf Breinbauer; Ruth Birner-Gruen...; Christian C. Gruber; Robert Zimmermann; Karl Gruber; Monika Oberer
• Keywords: Monoglyceride; Acyltransferases

Monoglyceride lipases (MGLs) are a group of α/β-hydrolases that catalyze the hydrolysis monoglycerides (MGs) into free fatty acids and glycerol. This reaction serves different physiological functions, namely in last step phospholipid triglyceride degradation, mammalian endocannabinoid arachidonic acid metabolism, detoxification processes microbes. Previous crystal structures MGLs from humans bacteria revealed conformational plasticity cap region this protein gave insight substrate binding. In study, we present structure MGL Saccharomyces cerevisiae called Yju3p its form complex with covalently bound analog mimicking tetrahedral intermediate MG hydrolysis. These reveal high conservation overall shape also provide evidence for changes Yju3p. The reveals that, despite structural similarity, seems to have an additional opening binding pocket at position compared human bacterial MGL. Substrate specificities towards MGs saturated unsaturated alkyl chains lengths were tested highest activity containing C18:1 acid.