Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering

Planas, Antoni

doi:10.1016/s0167-4838(00)00231-4

Cited by 241 publications

(248 citation statements)

References 168 publications

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“…This implies that extended binding of polysaccharides in the active-site cleft may overcome such limitations. Regardless, the mode of action of PtEG16 on mixed linkage glucans appears distinct from that of archetypical GH16 licheninases, which explicitly require a ␤(133) linkage to span the Ϫ2 and Ϫ1 subsites to yield limit digestion products of the series G3G, G4G3G, G4G4G3G, and G4G4G4G3G (16).…”

Section: Limit Digestion Products From Mixed Linkage Glucans-furthermentioning

confidence: 99%

“…S9A), thereby narrowing the active-site cleft (Fig. 6) and contributing many structural features necessary for specific recognition of kinked mixed linkage glucan chains (16,48,71). The removal of this loop in plant PtEG16 and XTH gene products is a clear prerequisite for the binding of highly branched xyloglucans (72)(73)(74).…”

Section: Limit Digestion Products From Mixed Linkage Glucans-furthermentioning

confidence: 99%

“…In addition to the plant XTH gene products, GH16 counts a broad range of microbial endoglucanases and endogalactanases among its functionally characterized members, spanning those active on terrestrial and marine polysaccharides to yeast cell wall chitin/␤-glucan transglycosylases (13). Despite significant sequence divergence, all GH16 enzymes are predicted to share both a common overall ␤-jellyroll protein fold and the canonical retaining GH catalytic mechanism (15)(16)(17).…”

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confidence: 99%

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Structure-Function Analysis of a Broad Specificity Populus trichocarpa Endo-β-glucanase Reveals an Evolutionary Link between Bacterial Licheninases and Plant XTH Gene Products

Eklöf

Shojania

Okon

et al. 2013

Journal of Biological Chemistry

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Background: The evolution of the plant xyloglucan endotransglycosylase/hydrolase (XTH) genes in glycoside hydrolase family 16 (GH16) is enigmatic. Results: A unique, mixed function endo(xylo)glucanase from black cottonwood has been biochemically and structurally characterized. Conclusion:This enzyme is an important link between extant bacterial endoglucanases and plant XTH gene products. Significance: New insights into the molecular evolution of XTH gene products and further unification of GH16 enzymes have been gained.

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Section: Limit Digestion Products From Mixed Linkage Glucans-furthermentioning

confidence: 99%

Section: Limit Digestion Products From Mixed Linkage Glucans-furthermentioning

confidence: 99%

mentioning

confidence: 99%

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Structure-Function Analysis of a Broad Specificity Populus trichocarpa Endo-β-glucanase Reveals an Evolutionary Link between Bacterial Licheninases and Plant XTH Gene Products

Eklöf

Shojania

Okon

et al. 2013

Journal of Biological Chemistry

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“…Structurally, β-glucans are comprised of β-1,3-, β-1,6-and β-1,4-linked D-glucopyranosyl units (Planas 2000, Parrish et al 1960. β-1,3-glucanase is an enzyme with strict cleavage specificity for β-1,3-linkages (Planas 2000).…”

Section: Introductionmentioning

confidence: 99%

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Sena

Valasques

Góes-Neto

et al. 2011

An. Acad. Bras. Ciênc.

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The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology -RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L −1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33, 1.86 and 3.03, respectively. The partially purified enzymatic extract showed an optimum pH of 5.0 and an optimum temperature of 40 • C. The enzymatic activity increased in the presence of KCl at all concentrations studied. The glucanase activity was highest in the presence of 0.2 M NaCl. The enzyme showed high thermal stability, losing only 10.20% of its specific activity after 40 minutes of incubation at 90 • C. A purified enzyme with relatively good thermostability that is stable at low pH might be used in future industrial applications.

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“…The ␤(1,3;1,4)-glucanases specifically cleave ␤(1,4)-linkages adjacent to ␤(1, 3)-bonds (3). Although ␤(1,3;1,4)-glucanases are encountered in several GH 2 families of the Carbohydrate-Active Enzyme (CAZy) database (4) (www.cazy.org), most are found in families GH5 and GH16.…”

mentioning

confidence: 99%

The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans

Lafond

Sulzenbacher

Freyd

et al. 2016

Journal of Biological Chemistry

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In the Carbohydrate-Active Enzyme (CAZy) database, glycoside hydrolase family 5 (GH5) is a large family with more than 6,000 sequences. Among the 51 described GH5 subfamilies, subfamily GH5_26 contains members that display either endo-␤(1,4)-glucanase or ␤(1,3;1,4)-glucanase activities. In this study, we focused on the GH5_26 enzyme from Saccharophagus degradans (SdGluc5_26A), a marine bacterium known for its capacity to degrade a wide diversity of complex polysaccharides. SdGluc5_26A displays lichenase activity toward ␤(1,3; 1,4)-glucans with a side cellobiohydrolase activity toward ␤(1, 4)-glucans. The three-dimensional structure of SdGluc5_26A adopts a stable trimeric quaternary structure also observable in solution. The N-terminal region of SdGluc5_26A protrudes into the active site of an adjacent monomer. To understand whether this occupation of the active site could influence its activity, we conducted a comprehensive enzymatic characterization of SdGluc5_26A and of a mutant truncated at the N terminus. Ligand complex structures and kinetic analyses reveal that the N terminus governs the substrate specificity of SdGluc5_26A. Its deletion opens the enzyme cleft at the ؊3 subsite and turns the enzyme into an endo-␤(1,4)-glucanase. This study demonstrates that experimental approaches can reveal structure-function relationships out of reach of current bioinformatic predictions.

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Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering

Cited by 241 publications

References 168 publications

Structure-Function Analysis of a Broad Specificity Populus trichocarpa Endo-β-glucanase Reveals an Evolutionary Link between Bacterial Licheninases and Plant XTH Gene Products

Structure-Function Analysis of a Broad Specificity Populus trichocarpa Endo-β-glucanase Reveals an Evolutionary Link between Bacterial Licheninases and Plant XTH Gene Products

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans

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