Abstract
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25–45°C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The structure of the Proteus mirabilis lipase was solved in the absence and presence of a bound phosphonate inhibitor. Unexpectedly, both the apo and inhibitor bound forms of P. mirabilis lipase were found to be in a closed conformation. The structure reveals a unique oxyanion hole and a wide active site that is solvent accessible even in the closed conformation. A distinct mechanism for Ca2+ coordination may explain how these lipases can fold without specific chaperones.
Highlights
The ability of an organism to convert triacylglycerol to free fatty acids is mediated by lipases [1,2,3]
Lipases from family I.1 and I.2 share greater than 40% sequence identity and are nearly exclusively found in Pseudomonas and Proteus species
While structures of PAL, BCL, and Burkholderia glumae (BGL) provide a general rationale for lid opening, novel structures are needed to elucidate the specific features governing the molecular basis of catalysis and enantioselectivity catalyzed by individual lipases
Summary
The ability of an organism to convert triacylglycerol to free fatty acids is mediated by lipases (triacylglycerol hydrolase, EC 3.1.1.3) [1,2,3]. While structures of PAL, BCL, and BGL provide a general rationale for lid opening (interfacial activation), novel structures are needed to elucidate the specific features governing the molecular basis of catalysis and enantioselectivity catalyzed by individual lipases. Both PML structures have been solved in the closed conformation and provide further insight into catalysis by family I.1 and I.2 lipases.
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