A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum

Cavazzini, D.; Grossi, Guido; Levati, Elisabetta; Vallese, Francesca; Montanini, Barbara; Bolchi, Angelo; Zanotti, Giuseppe; Ottonello, Simone

doi:10.1038/s41598-017-08007-9

Cited by 9 publications

(3 citation statements)

References 72 publications

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“…The pH pattern is more diverse: Sto-Est from Sulfolobus tokodaii, SshEstI from Sulfolobus shibatae DSM5389 and PestE from Pyrobaculum calidifontis have their pH optimum in the range of 7.0-9.0 (Hotta et al, 2002;Palm et al, 2011;Angkawidjaja et al, 2012;Ohara et al, 2014) while EstFa_R from Ferroplasma acidiphilum is a slightly acidophilic carboxylesterase and showed the highest activity at pH 5.0 (Ohara et al, 2014). The two fungal esterases share similar optimal conditions: RmEstA from Rhizomucor miehei catalyzes the reaction best at 50 • C and pH 7.5 while TmelEST2 from Tuber melanosporum has its maximum activity at 68.3 • C and pH 7.0 (Yang et al, 2015;Cavazzini et al, 2017).…”

Section: Structural Comparison Of E53 and Other Esterasesmentioning

confidence: 99%

Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated From Erythrobacter longus

Ding

Nie²,

Yang

et al. 2022

Front. Microbiol.

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Esterases are a class of enzymes that split esters into an acid and an alcohol in a chemical reaction with water, having high potential in pharmaceutical, food and biofuel industrial applications. To advance the understanding of esterases, we have identified and characterized E53, an alkalophilic esterase from a marine bacterium Erythrobacter longus. The crystal structures of wild type E53 and three variants were solved successfully using the X-ray diffraction method. Phylogenetic analysis classified E53 as a member of the family IV esterase. The enzyme showed highest activity against p-nitrophenyl butyrate substrate at pH 8.5–9.5 and 40°C. Based on the structural feature, the catalytic pocket was defined as R1 (catalytic center), R2 (pocket entrance), and R3 (end area of pocket) regions. Nine variants were generated spanning R1–R3 and thorough functional studies were performed. Detailed structural analysis and the results obtained from the mutagenesis study revealed that mutations in the R1 region could regulate the catalytic reaction in both positive and negative directions; expanding the bottleneck in R2 region has improved the enzymatic activity; and R3 region was associated with the determination of the pH pattern of E53. N166A in R3 region showed reduced activity only under alkaline conditions, and structural analysis indicated the role of N166 in stabilizing the loop by forming a hydrogen bond with L193 and G233. In summary, the systematic studies on E53 performed in this work provide structural and functional insights into alkaliphilic esterases and further our knowledge of these enzymes.

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Section: Structural Comparison Of E53 and Other Esterasesmentioning

confidence: 99%

Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated From Erythrobacter longus

Ding

Nie²,

Yang

et al. 2022

Front. Microbiol.

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“…There are lipase crystal structures with PMSF bound to active serine (PDB ID 5MII, 3RLI, and 3H17), but the PMSF molecule was not added in any step of purification or crystallization in our experiment (40)(41)(42). In the blocked crystal structure, Ser114-bound BMK forms stable tetrahedral intermediate coordination.…”

Section: Structural and Functional Study Of C Acnes Lipase 731mentioning

confidence: 99%

The grease trap: uncovering the mechanism of the hydrophobic lid in Cutibacterium acnes lipase

Kim

Lee

Kwon

2020

Journal of Lipid Research

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Acne is one of the most common dermatological conditions, but the details of its pathology are unclear, and current management regimens often have adverse effects. Cutibacterium acnes is known as a major acne-associated bacterium that derives energy from lipase-mediated sebum lipid degradation. C. acnes is commensal, but lipase activity has been observed to differ among C. acnes types. For example, higher populations of the type IA strains are present in acne lesions with higher lipase activity. In the present study, we examined a conserved lipase in types IB and II that was truncated in type IA C. acnes strains. Closed, blocked, and open structures of C. acnes ATCC11828 lipases were elucidated by X-ray crystallography at 1.6–2.4 Å. The closed crystal structure, which is the most common form in aqueous solution, revealed that a hydrophobic lid domain shields the active site. By comparing closed, blocked, and open structures, we found that the lid domain-opening mechanisms of C. acnes lipases (CAlipases) involve the lid-opening residues, Phe-179 and Phe-211. To the best of our knowledge, this is the first structure-function study of CAlipases, which may help to shed light on the mechanisms involved in acne development and may aid in future drug design.

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“…Analysis of amino acid composition of thermophilic, mesophilic, and cold-adapted proteins and exoenzyme of strain RGM 2184. References [ 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 ] are cited in the Supplementary Materials.…”

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Identification of Exoenzymes Secreted by Entomopathogenic Fungus Beauveria pseudobassiana RGM 2184 and Their Effect on the Degradation of Cocoons and Pupae of Quarantine Pest Lobesia botrana

Arias-Aravena

Altimira

Gutiérrez

et al. 2022

JoF

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Beauveria pseudobassiana RGM 2184 has shown 80% maximum efficacy against the pest Lobesia botrana in the autumn and winter seasons. This suggests that the strain possesses an interesting battery of enzymes that are cold-adapted to penetrate the thick and hydrophobic cocoon of L. botrana. In this study, screening of the proteolytic, lipolytic, and chitinolytic activity of enzyme extracts secreted by the RGM 2184 strain was carried out in various culture media. The enzyme extracts with the highest activity were subjected to zymography and mass spectrometry. These analyses allowed the identification of two proteases, two lipases, and three chitinases. Comparative analysis indicated that the degree of similarity between these enzymes was substantially reduced when the highest degree of taxonomic relatedness between RGM 2184 and the entomopathogenic fungus strain was at the family level. These results suggest that there is a wide variety of exoenzymes in entomopathogenic fungi species belonging to the order Hypocreales. On the other hand, exoenzyme extract exposure of cocoons and pupae of L. botrana provoked damage at 10 °C. Additionally, an analysis of the amino acid composition of the RGM 2184 exoenzyme grouped them close to the cold-adapted protein cluster. These results support the use of this strain to control pests in autumn and winter. Additionally, these antecedents can form a scaffold for the future characterization of these exoenzymes along with the optimization of the strain’s biocontrol ability by overexpressing them.

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A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum

Cited by 9 publications

References 72 publications

Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated From Erythrobacter longus

Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated From Erythrobacter longus

The grease trap: uncovering the mechanism of the hydrophobic lid in Cutibacterium acnes lipase

Identification of Exoenzymes Secreted by Entomopathogenic Fungus Beauveria pseudobassiana RGM 2184 and Their Effect on the Degradation of Cocoons and Pupae of Quarantine Pest Lobesia botrana

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