Glycosidases

Divakar, Soundar

doi:10.1007/978-81-322-0873-0_2

Cited by 9 publications

(5 citation statements)

References 126 publications

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“…Glycosidases such as glycosyl hydrolases, beta-glucosidases, galactosidases and mannosidases, xylosidases and alpha amylases were abundant in A. castellanii EVs. These compose a universe of carbohydrate-processing enzymes that have had wide industrial applications due to their hydrolase efficiency, such as in the food and bio-bleaching in the paper and pulp industry [110,111,112]. As the glycosydases are also involved in many biological processes such as cell growth, cell recognition and parasitic infections, they have become attractive targets for the pharmaceutical industry [113].…”

Section: Conclusion Remarksmentioning

confidence: 99%

Extracellular Vesicles from the Protozoa Acanthamoeba castellanii: Their Role in Pathogenesis, Environmental Adaptation and Potential Applications

2019

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Extracellular vesicles (EVs) are membranous compartments of distinct cellular origin and biogenesis, displaying different sizes and include exosomes, microvesicles, and apoptotic bodies. The EVs have been described in almost every living organism, from simple unicellular to higher evolutionary scale multicellular organisms, such as mammals. Several functions have been attributed to these structures, including roles in energy acquisition, cell-to-cell communication, gene expression modulation and pathogenesis. In this review, we described several aspects of the recently characterized EVs of the protozoa Acanthamoeba castellanii, a free-living amoeba (FLA) of emerging epidemiological importance, and compare their features to other parasites’ EVs. These A. castellanii EVs are comprised of small microvesicles and exosomes and carry a wide range of molecules involved in many biological processes like cell signaling, carbohydrate metabolism and proteolytic activity, such as kinases, glucanases, and proteases, respectively. Several biomedical applications of these EVs have been proposed lately, including their use in vaccination, biofuel production, and the pharmaceutical industry, such as platforms for drug delivery.

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Section: Conclusion Remarksmentioning

confidence: 99%

Extracellular Vesicles from the Protozoa Acanthamoeba castellanii: Their Role in Pathogenesis, Environmental Adaptation and Potential Applications

2019

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“…In particular, glutamate acts as a nucleophile in enzymes from GH1 family, characterizing them in the GH-A clan [56,57]. The family presents the nucleophile located close to the carboxy-terminus from β-strand 7 and a sequence of asparagine-glutamate (an asparagine residue preceding the general acid/base catalyst) close to the carboxy-terminus from β-strand 4, except for myrosinase, where the acid/base glutamate is replaced by glutamine [58,59]. Henrissat et al [60] suggested that the two key active site glutamic acids are about 200 amino acid residues apart from each other and these enzymes are able to hydrolyze a wide diversity of substrates with a similar disposition of their identical catalytic residues.…”

Section: The Gh1 Family Of Enzymesmentioning

confidence: 99%

“…The first one involves the nucleophile attack in the anomeric carbon (C-1) of the substrate resulting in a covalent glycosyl–enzyme intermediate with concomitant release of the aglycone after the protonation of the glucosidic oxygen by the acid catalyst, step called glycosylation. The second step corresponds to the hydrolysis of the covalent intermediate glycosyl–enzyme, with the acid catalyst acting as a base and a water molecule functioning as the nucleophile, releasing the glucose and regenerating the nucleophile residue [58,65].…”

Section: The Gh1 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented.

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“…Glycosidases catalyze the hydrolysis of glycosidic bonds present in a variety of molecules such as carbohydrates, glycolipids, and glycoproteins [ 1 ]. By virtue of this property, most of these enzymes play a crucial role in numerous biological processes including the digestion of carbohydrates, the degradation of complex macromolecules, the regulation of cell signaling, and the modification of glycans during glycoprotein and glycoconjugate synthesis.…”

Section: Introductionmentioning

confidence: 99%

“…The reaction may retain the sugar anomeric configuration as α → α or β → β or α → β or β → α, depending on the orientation of the nucleophilic attack and the relative position of the outgoing group in the substrate. It is worth noting that glycosidase itself plays a relevant role in providing a favorable environment and facilitating the correct orientation of the substrate for the hydrolytic reaction to occur in an efficient manner [ 1 , 4 , 5 ]. In fungi and most organisms, secreted or membrane-associated glycosidases play a fundamental role in the decomposition of organic matter and the use of products as sources of carbon and energy [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Fungal Glycosidases in Sporothrix Species and Candida albicans

Ortiz-Ramírez,

Cuéllar-Cruz,

Villagómez-Castro

et al. 2023

JoF

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Glycoside hydrolases (GHs) are enzymes that participate in many biological processes of fungi and other organisms by hydrolyzing glycosidic linkages in glycosides. They play fundamental roles in the degradation of carbohydrates and the assembly of glycoproteins and are important subjects of studies in molecular biology and biochemistry. Based on amino acid sequence similarities and 3-dimensional structures in the carbohydrate-active enzyme (CAZy), they have been classified in 171 families. Members of some of these families also exhibit the activity of trans-glycosydase or glycosyl transferase (GT), i.e., they create a new glycosidic bond in a substrate instead of breaking it. Fungal glycosidases are important for virulence by aiding tissue adhesion and colonization, nutrition, immune evasion, biofilm formation, toxin release, and antibiotic resistance. Here, we review fungal glycosidases with a particular emphasis on Sporothrix species and C. albicans, two well-recognized human pathogens. Covered issues include a brief account of Sporothrix, sporotrichosis, the different types of glycosidases, their substrates, and mechanism of action, recent advances in their identification and characterization, their potential biotechnological applications, and the limitations and challenges of their study given the rather poor available information.

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Glycosidases

Cited by 9 publications

References 126 publications

Extracellular Vesicles from the Protozoa Acanthamoeba castellanii: Their Role in Pathogenesis, Environmental Adaptation and Potential Applications

Extracellular Vesicles from the Protozoa Acanthamoeba castellanii: Their Role in Pathogenesis, Environmental Adaptation and Potential Applications

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Fungal Glycosidases in Sporothrix Species and Candida albicans

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