Lipases and sterol esterases are enzymes with broad biotechnological applications, which catalyze the hydrolysis or synthesis of long-chain acylglycerols and sterol esters, respectively. In this paper, we review the current knowledge on the so-called Candida rugosa-like family of enzymes, whose members display in most cases affinity against the two substrates mentioned above. The family includes proteins with the α/β-hydrolase folding, sharing conserved motifs in their sequences, and common structural features. We will go through their production and purification, relate their described structures and catalytic activity, and discuss the influence of the hydrophobic character of these lipases on their aggregation state and activity. On the basis of the few crystal structures available, the role of each of the functional areas in catalysis will be analyzed. Considering the particular characteristics of this group, we propose their classification as "Versatile Lipases" (EC 3.1.1.x).
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Heterologous expression, purification, and characterization of a recombinant Cordyceps militaris lipase from Candida rugosa-like family in Pichia pastoris.
Enzyme Microb Technol
August 2023
Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea; Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Republic of Korea; Center for Agricultural Microorganism and Enzyme, Seoul National University, Seoul 08826, Republic of Korea; Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea. Electronic address:
Multiple sequence alignments of three lipase isoforms from the filamentous fungus, Cordyceps militaris, have revealed that the deduced protein from their common sequence belongs to the Candida rugosa lipase-like group. To express the protein in its active form, recombinant lipase from C. militaris (rCML) was extra cellularly expressed in Pichia pastoris X-33 after removing its signal peptide.
View Article and Find Full Text PDFVersatile Lipases from the -like Family: A Mechanistic Insight Using Computational Approaches.
J Chem Inf Model
February 2021
Centro de Investigaciones Biológicas Margarita Salas, Department of Environmental Biology, Consejo Superior de Investigaciones Científicas CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain.
Lipases are enzymes able to catalyze the hydrolysis or synthesis of triglycerides, depending on the reaction conditions, whereas sterol esterases show the same ability on sterol esters. Structurally, both kinds of enzymes display an α/β-hydrolase fold, with a substrate-binding pocket formed by a hydrophobic cavity covered by a mobile lid. However, it has been reported that some lipases from the -like family display wide substrate specificity on both triglycerides and sterol esters.
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Front Bioeng Biotechnol
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Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Some enzymes that belong to the -like lipase family (abH03. 01) combine the activities of lipases and sterol esterases. Thus, they can act on water-insoluble carboxylic esters releasing long-chain fatty acids but also on sterol esters, although with different activity and affinity.
View Article and Find Full Text PDFEvolutionary history of versatile-lipases from Agaricales through reconstruction of ancestral structures.
BMC Genomics
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Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Department of Environmental Biology, Ramiro de Maeztu 9, Madrid, E-28040, Spain.
Background: Fungal "Versatile carboxylic ester hydrolases" are enzymes with great biotechnological interest. Here we carried out a bioinformatic screening to find these proteins in genomes from Agaricales, by means of searching for conserved motifs, sequence and phylogenetic analysis, and three-dimensional modeling. Moreover, we reconstructed the molecular evolution of these enzymes along the time by inferring and analyzing the sequence of ancestral intermediate forms.
View Article and Find Full Text PDFStructural traits and catalytic versatility of the lipases from the Candida rugosa-like family: A review.
Biotechnol Adv
December 2017
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain. Electronic address:
Lipases and sterol esterases are enzymes with broad biotechnological applications, which catalyze the hydrolysis or synthesis of long-chain acylglycerols and sterol esters, respectively. In this paper, we review the current knowledge on the so-called Candida rugosa-like family of enzymes, whose members display in most cases affinity against the two substrates mentioned above. The family includes proteins with the α/β-hydrolase folding, sharing conserved motifs in their sequences, and common structural features.
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