β-Glucosidases

Cairns, James R. Ketudat; Esen, Asım

doi:10.1007/s00018-010-0399-2

Cited by 452 publications

(237 citation statements)

References 139 publications

(222 reference statements)

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“…Beta-glucosidases participate in lignification of the cell walls, b-glucan catabolism, activation of phytohormones, stimulation of the aromatic compounds synthesis and in other defensive processes (Cairns and Esen 2010). In response to drought stress, bglucosidases may increase the amount of abscisic acid (ABA)-an essential signaling factor which is involved in adapting plants to stress conditions (Bargmann and Munnik 2006;Cairns and Esen 2010;Wang et al 2011).…”

Section: Discussionmentioning

confidence: 99%

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

2013

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Osmotic stress causes many adverse symptoms in plants, which include, for example, growth limitation and decrease or even absence of yield. Proteomic analyses of plant responses to stressors could lead to the introduction of crops with high resistance to osmotic stress. Such plants would be characterized by high yield even under unfavorable environmental conditions. In this article we describe changes in the protein profiles occurring in response to mild and moderate osmotic stress in triticale roots. Analysis of the protein profiles of these roots showed an increased abundance of 14 and a decreased abundance of 11 proteins under mild osmotic stress conditions while a moderate osmotic stress caused an increased abundance of 18 and a decreased abundance of 33 proteins. Twenty-five proteins, whose quantity altered under stress were identified using MALDI-TOF mass spectrometry. The identified proteins were classified into the categories of proteins associated with: defense mechanisms, metabolism, transcription, cell structure, protein synthesis, transport and signal transduction. The functions of identified proteins were discussed in relation to osmotic stress. Some of the identified proteins may be responsible for the adaptation of plants to adverse conditions.

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Section: Discussionmentioning

confidence: 99%

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

2013

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“…β-glucosidases play important roles in cell wall formation and plant development, because they participate in cell wall polysaccharide turnover [47]. In sugarcane [30] and B. distachyon [31], more GH1 were found in cell wall proteomes of growing organs, such as young leaves and apical internodes, than in mature organs.…”

Section: Gh1 Gh3 and Gh51mentioning

confidence: 99%

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

Calderan-Rodrigues¹,

Fonseca²,

Clemente³

et al. 2018

Advances in Biofuels and Bioenergy

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Glycoside hydrolases (GHs) are enzymes that are able to rearrange the plant cell wall polysaccharides, being developmental-and stress-regulated. Such proteins are used in enzymatic cocktails for biomass hydrolysis in the second-generation ethanol (E2G) production. In this chapter, we investigate GHs identified in plant cell wall proteomes by predicting their functions through alignment with homologous plant and microorganism sequences and identification of functional domains. Up to now, 49 cell wall GHs were identified in sugarcane and 114 in Brachypodium distachyon. We could point at candidate proteins that could be targeted to lower biomass recalcitrance. We more specifically addressed several GHs with predicted cellulase, hemicellulase, and pectinase activities, such as β-xylosidase, α and β-galactosidase, α-N-arabinofuranosidases, and glucan β-glucosidases. These enzymes are among the most used in enzymatic cocktails to deconstruct plant cell walls. As an example, the fungi arabinofuranosidases belonging to the GH51 family, which were also identified in sugarcane and B. distachyon, have already been associated to the degradation of hemicellulosic and pectic polysaccharides, through a peculiar mechanism, probably more efficient than other GH families. Future research will benefit from the information available here to design plant varieties with self-disassembly capacity, making the E2G more cost-effective through the use of more efficient enzymes.

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“…12 Their active sites contain a conserved aspartate that functions as a nucleophile and a glutamate that serves as a proton donor. 13 Their catalytic mechanisms proceed through retention of configuration about the anomeric carbon. 13 In the first step of the reaction, the conserved glutamate donates a proton to the leaving group whereas the conserved aspartate attacks the sugar C-1 carbon to form an enzyme intermediate with an a-linkage.…”

Section: Introductionmentioning

confidence: 99%

“…13 Their catalytic mechanisms proceed through retention of configuration about the anomeric carbon. 13 In the first step of the reaction, the conserved glutamate donates a proton to the leaving group whereas the conserved aspartate attacks the sugar C-1 carbon to form an enzyme intermediate with an a-linkage. Subsequently, the glutamate, now deprotonated, activates a water molecule, which in turn attacks the enzyme intermediate to release the sugar moiety.…”

Section: Introductionmentioning

confidence: 99%

The structure of DesR from Streptomyces venezuelae, a β‐glucosidase involved in macrolide activation

2013

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Antibiotics have, indeed, altered the course of human history as is evidenced by the increase in human life expectancy since the 1940s. Many of these natural compounds are produced by bacteria that, by necessity, must have efficient self-resistance mechanisms. The methymycin/pikromycin producing species Streptomyces venezuelae, for example, utilizes b-glucosylation of its macrolide products to neutralize their effects within the confines of the cell. Once released into the environment, these compounds are activated by the removal of the glucose moiety. In S. venezuelae, the enzyme responsible for removal of the sugar from the parent compound is encoded by the desR gene and referred to as DesR. It is a secreted enzyme containing 828 amino acid residues, and it is known to be a retaining glycosidase. Here, we describe the structure of the DesR/D-glucose complex determined to 1.4-Å resolution. The overall architecture of the enzyme can be envisioned in terms of three regions: a catalytic core and two auxiliary domains. The catalytic core harbors the binding platform for the glucose ligand. The first auxiliary domain adopts a ''PA14 fold,'' whereas the second auxiliary domain contains an immunoglobulin-like fold. Asp 273 and Glu 578 are in the proper orientation to function as the catalytic base and proton donor, respectively, required for catalysis. The overall fold of the core region places DesR into the GH3 glycoside hydrolase family of enzymes. Comparison of the DesR structure with the b-glucosidase from Kluyveromyces marxianus shows that their PA14 domains assume remarkably different orientations.

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β-Glucosidases

Cited by 452 publications

References 139 publications

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

The structure of DesR from Streptomyces venezuelae, a β‐glucosidase involved in macrolide activation

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