Properties, structure, and applications of microbial sterol esterases

Vaquero, María Eugenia; Barriuso, Jorge; Martı́nez, Marı́a Jesús; Prieto, Alicia

doi:10.1007/s00253-015-7258-x

Cited by 42 publications

(22 citation statements)

References 82 publications

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“…It is therefore possible that the optimal configuration of the active site might be achieved upon binding the asyet-unknown substrate. This type of catalytic triad has been previously identified in proteases, lipases, and esterases (24)(25)(26). Therefore, DWV may use the putative catalytic activity of its P domains in cell entry.…”

Section: Resultsmentioning

confidence: 79%

Structure of deformed wing virus, a major honey bee pathogen

Škubník

Nováček

Füzik

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The worldwide population of western honey bees (Apis mellifera) is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family Iflaviridae, together with its vector, the mite Varroa destructor, is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Åusing cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments.colony collapse disorder | virus | structure | Apis mellifera | honey bee

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Section: Resultsmentioning

confidence: 79%

Structure of deformed wing virus, a major honey bee pathogen

Škubník

Nováček

Füzik

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…This could be explained by reasoning that in some enzymes of the family, the tunnel extension is long enough to communicate the end of the substrate-binding pocket with the outside of the protein, creating a narrow exit tunnel to release the reaction products [6, 8]. The evolutionary advantage of having a longer tunnel, as those found in some of the current proteins, could be related to a better accommodation of the acyl moiety of the substrate, increasing the specificity of the enzyme as reported for C. rugosa lipase isoenzymes and the lipase/esterase from O. piceae [2, 46]. …”

Section: Discussionmentioning

confidence: 99%

“…They are able not only to catalyze hydrolysis reactions under aqueous conditions, but also to carry out synthesis reactions, such as esterification and transesterification, in the presence of organic solvents [2]. All of them display the α/β-hydrolase fold, with their catalytic machinery formed by a catalytic triad (serine, histidine and glutamic acid) and the oxyanion hole [3].…”

Section: Introductionmentioning

confidence: 99%

“…Among filamentous fungi and yeasts, some extracellular proteins show wide substrate specificity and combine the properties from lipases and sterol esterases, being active towards acylglycerols and sterol esters [2, 5]. These enzymes belong to the Candida rugosa -like lipase family (abH03.01), and their reclassification as “Versatile lipases” has been recently proposed [6].…”

Section: Introductionmentioning

confidence: 99%

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Evolutionary history of versatile-lipases from Agaricales through reconstruction of ancestral structures

Barriuso

Martı́nez

2017

BMC Genomics

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BackgroundFungal “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.ResultsThe properties of the ancestral candidates are discussed on the basis of their three-dimensional structural models, the hydrophobicity of the lid, and the substrate binding intramolecular tunnel, revealing all of them featured properties of these enzymes. The evolutionary history of the putative lipases revealed an increase on the length and hydrophobicity of the lid region, as well as in the size of the substrate binding pocket, during evolution time. These facts suggest the enzymes’ specialization towards certain substrates and their subsequent loss of promiscuity.ConclusionsThese results bring to light the presence of different pools of lipases in fungi with different habitats and life styles. Despite the consistency of the data gathered from reconstruction of ancestral sequences, the heterologous expression of some of these candidates would be essential to corroborate enzymes’ activities.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-3419-2) contains supplementary material, which is available to authorized users.

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“…A common feature of extracellular sterol esterases and lipases is the presence of the secondary gene situated immediately downstream from the hydrolase enzyme. The product of the secondary gene is required for correct folding of the respective esterases and lipases (8, 9). The hydrolase gene showed 99% amino acid sequence identity with the lipA gene of B. cepacia recorded as GenBank accession no.…”

Section: Genome Announcementmentioning

confidence: 99%