Structural and Functional Analyses of β-Glucosidase 3B from Thermotoga neapolitana: A Thermostable Three-Domain Representative of Glycoside Hydrolase 3

Pozzo, Tania; Pasten, Javier Linares; Karlsson, Eva Nordberg; Logan, D.T.

doi:10.1016/j.jmb.2010.01.072

Cited by 128 publications

(122 citation statements)

References 51 publications

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“…In JMB19063, the Ca 2ϩ ion helps position a loop, consisting of residues 664 -674, that is at the dimer interface and makes five hydrogen bonds with the other monomer. Another three-domain ␤-glucosidase from the GH3 family has recently been described in Thermotoga neapolitana (TnBgl3B) (28). The majority of the TnBgl3B structure superposes well with JMB19063 (Fig.…”

Section: Resultsmentioning

confidence: 93%

From Soil to Structure, a Novel Dimeric β-Glucosidase Belonging to Glycoside Hydrolase Family 3 Isolated from Compost Using Metagenomic Analysis

McAndrew

Park

Heins

et al. 2013

Journal of Biological Chemistry

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Background: ␤-Glucosidases hydrolyze cellobiose and are an important step in biomass saccharification. Results: The structure of JMB19063 is a homodimer, and residues from the partnering monomer form a portion of the active site. Conclusion: JMB19063 is the first structure in the GH3 family that requires dimerization for catalysis. Significance: Structural characterization of novel ␤-glucosidases may provide insights into improving biofuel production.

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Section: Resultsmentioning

confidence: 93%

From Soil to Structure, a Novel Dimeric β-Glucosidase Belonging to Glycoside Hydrolase Family 3 Isolated from Compost Using Metagenomic Analysis

McAndrew

Park

Heins

et al. 2013

Journal of Biological Chemistry

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“…3), and it also has been identified in eukaryotic GH3 ␤-glucosidases (38)(39)(40), but its function is unknown to date. Figure S2 in the supplemental material (residue numbering refers to that of the TnBgl3B sequence) highlights the conserved amino acid residues identified in GH3 ␤-glucosidases (37,40) compared to three GH3 ␤-xylosidase sequences. Notable differences are that D58 and W243 appear not to be conserved in GH3 xylosidases.…”

Section: Resultsmentioning

confidence: 99%

A Versatile Family 3 Glycoside Hydrolase from Bifidobacterium adolescentis Hydrolyzes β-Glucosides of the Fusarium Mycotoxins Deoxynivalenol, Nivalenol, and HT-2 Toxin in Cereal Matrices

Michlmayr

Varga

Malachová

et al. 2015

Appl Environ Microbiol

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Infestation of cereals by phytopathogenic fungi is a global threat to the human food supply. In addition to economically devastating losses through yield and quality deterioration of agricultural products, contamination with mycotoxins poses a serious challenge for food safety (1). Among the most relevant mycotoxin producers worldwide are Fusarium species, causing Fusarium head blight disease of small-grain cereals (FHB; also known as Fusarium ear blight or scab). Trichothecene class mycotoxins inhibit eukaryotic protein synthesis and are important Fusarium virulence factors. Furthermore, they can cause apoptotic cell death and immunosuppression and trigger proinflammatory responses in humans and animals (1-3). The most important groups with regard to food safety are type A (T-2 toxin and HT-2 toxin [HT2]) and type B (nivalenol [NIV] and deoxynivalenol [DON]) trichothecenes (4). The type A trichothecene T-2 toxin possesses high acute toxicity and has caused fatal outbreaks of alimentary toxic aleukia in the last century (1). DON is the predominant trichothecene toxin produced by the Fusarium graminearum species complex and ranks among the most frequent contaminants of cereals. Although the acute toxicity of DON is lower than that of type A trichothecenes, its ubiquitous presence in Fusarium-infected cereals creates an important food safety issue (2). Acute symptoms of DON ingestion are gastroenteritis and emesis (hence, the colloquial term vomitoxin). Maximum levels for DON in cereal-based foodstuff are set in Commission Regulation 1881/2006 (5), and indicative levels are provided for the sum of T-2 toxin and HT-2 toxin in Commission Recommendation 2013/165/EU (6) in Europe to protect consumers.The glycosylation of small molecules is a major route to inactivate endogenous and exogenous (xenobiotic) metabolites in plants (7-9). For example, formation of DON-3-O-␤-D-glucopyranoside (DON-3G) is an important factor in plant defense against FHB and has been proposed to be the molecular basis of the still-unidentified FHB1 gene (Fusarium head blight resistance quantitative trait locus) in wheat (10). DON-3G has been detected in a wide range of cereal commodities, with concentrations of about 20% relative to that of DON (11,12). However, high regional and seasonal variations have been reported, and in some cases, the content of DON-3G even exceeded that of DON (13,14). Evidence for glucosylated metabolites of NIV and type A trichothecenes has been presented as well (15)(16)(17). Such glucoconjugates of plant origin have been termed masked mycotoxins (13, 18), implying that they escape detection through

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“…On the other hand, it was observed that the pH optimum shifted from 5.3 to 5.8 when total reaction rate or r s /r h , respectively, were considered, suggesting that the ionization state of the enzyme influences its nucleophile specificity. It was later established that these catalytic features were closely related to structural issues (Pozzo et al, 2010). The glucosidase, which had a three-domain structure, quite uncommon for GH3 enzymes, displayed an active site much more accessible to solvent molecules than the corresponding site of structurally homologous enzymes.…”

Section: Glucosidasesmentioning

confidence: 99%

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes

2014

Front. Mar. Sci.

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Evidence that support the marine environment as source of useful biocatalysts for application in several areas of industry pile up, both as scientific reports or patent applications. Marine microorganisms have to endure habitats characterized by extreme conditions of salinity, temperature or pressure. Their enzymes present concomitant features, viz. thermostability or halostability, which are appealing for practical applications. The food sector is a field where enzymes are used, given their specificity, compliance with strict regulations, relatively mild operational conditions required and environmental friendly nature. The specific features presented by marine enzymes can be advantageously used both for process improvement or to develop new processes and products. In the present review the role of relevant types of enzymes for the food sector is described and recent findings on those enzymes from marine are put into context. The information provided is illustrative that in spite of the relative novelty concerning the use of marine enzymes within the scope of the food sector, some processes have reached commercial status and promising results are being obtained with several others. Moreover, there is still a vast field of resources for enzyme activity to be explored, namely since the screening process that has been considerably improved with the contribution of metagenomic libraries. It can thus be considered that future and exciting developments can be expected concerning the use of marine enzymes in the food and feed areas.

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Structural and Functional Analyses of β-Glucosidase 3B from Thermotoga neapolitana: A Thermostable Three-Domain Representative of Glycoside Hydrolase 3

Cited by 128 publications

References 51 publications

From Soil to Structure, a Novel Dimeric β-Glucosidase Belonging to Glycoside Hydrolase Family 3 Isolated from Compost Using Metagenomic Analysis

From Soil to Structure, a Novel Dimeric β-Glucosidase Belonging to Glycoside Hydrolase Family 3 Isolated from Compost Using Metagenomic Analysis

A Versatile Family 3 Glycoside Hydrolase from Bifidobacterium adolescentis Hydrolyzes β-Glucosides of the Fusarium Mycotoxins Deoxynivalenol, Nivalenol, and HT-2 Toxin in Cereal Matrices

Marine enzymes and food industry: insight on existing and potential interactions

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