?-Fructosidase superfamily: Homology with some ?-L-arabinases and ?-D-xylosidases

Naumoff, D. G.

doi:10.1002/1097-0134(20010101)42:1<66::aid-prot70>3.0.co;2-4

Cited by 61 publications

(46 citation statements)

References 47 publications

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“…Arabinanases and arabinofuranosidases catalyze the hydrolysis of ␣-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides (151,179). GH43 and GH93 arabinanases share extensive amino acid sequence similarities with ␤-fructosidases (GH32 and GH68), with multiple homologous domains (180).…”

Section: Hemicellulasesmentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

112

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SUMMARY Biomass is constructed of dense recalcitrant polymeric materials: proteins, lignin, and holocellulose, a fraction constituting fibrous cellulose wrapped in hemicellulose-pectin. Bacteria and fungi are abundant in soil and forest floors, actively recycling biomass mainly by extracting sugars from holocellulose degradation. Here we review the genome-wide contents of seven Aspergillus species and unravel hundreds of gene models encoding holocellulose-degrading enzymes. Numerous apparent gene duplications followed functional evolution, grouping similar genes into smaller coherent functional families according to specialized structural features, domain organization, biochemical activity, and genus genome distribution. Aspergilli contain about 37 cellulase gene models, clustered in two mechanistic categories: 27 hydrolyze and 10 oxidize glycosidic bonds. Within the oxidative enzymes, we found two cellobiose dehydrogenases that produce oxygen radicals utilized by eight lytic polysaccharide monooxygenases that oxidize glycosidic linkages, breaking crystalline cellulose chains and making them accessible to hydrolytic enzymes. Among the hydrolases, six cellobiohydrolases with a tunnel-like structural fold embrace single crystalline cellulose chains and cooperate at nonreducing or reducing end termini, splitting off cellobiose. Five endoglucanases group into four structural families and interact randomly and internally with cellulose through an open cleft catalytic domain, and finally, seven extracellular β-glucosidases cleave cellobiose and related oligomers into glucose. Aspergilli contain, on average, 30 hemicellulase and 7 accessory gene models, distributed among 9 distinct functional categories: the backbone-attacking enzymes xylanase, mannosidase, arabinase, and xyloglucanase, the short-side-chain-removing enzymes xylan α-1,2-glucuronidase, arabinofuranosidase, and xylosidase, and the accessory enzymes acetyl xylan and feruloyl esterases.

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Section: Hemicellulasesmentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

112

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“…This domain belongs to the ␤-furanosidase superfamily (37), which contains four other members: GH43 arabinase, GH62 arabinofuranosidase (with no three-dimensional structure known up to now), GH68 levansucrase, and a group of hypothetical proteins, some of which are also predicted to be glycosylhydrolases. Interestingly, this was the first glycosylhydrolase superfamily shown to include enzymes with both inversion (GH43) and retention (GH32 and GH68) mechanisms of action (37). Furthermore, this clan shares the five-bladed ␤-propeller fold with tachylectin II, which was the first protein described as showing this folding (38), and human apyrase (39).…”

Section: Mutantmentioning

confidence: 99%

Structural and Kinetic Analysis of Schwanniomyces occidentalis Invertase Reveals a New Oligomerization Pattern and the Role of Its Supplementary Domain in Substrate Binding

Álvaro-Benito

Polo

González

et al. 2010

Journal of Biological Chemistry

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Schwanniomyces occidentalis invertase is an extracellular enzyme that hydrolizes sucrose and releases ␤-fructose from various oligosaccharides and essential storage fructan polymers such as inulin. We report here the three-dimensional structure of Sw. occidentalis invertase at 2.9 Å resolution and its complex with fructose at 1.9 Å resolution. The monomer presents a bimodular arrangement common to other GH32 enzymes, with an N-terminal 5-fold ␤-propeller catalytic domain and a C-terminal ␤-sandwich domain for which the function has been unknown until now. However, the dimeric nature of Sw. occidentalis invertase reveals a unique active site cleft shaped by both subunits that may be representative of other yeast enzymes reported to be multimeric. Binding of the tetrasaccharide nystose and the polymer inulin was explored by docking analysis, which suggested that medium size and long substrates are recognized by residues from both subunits. The identified residues were mutated, and the enzymatic activity of the mutants against sucrose, nystose, and inulin were investigated by kinetic analysis. The replacements that showed the largest effect on catalytic efficiency were Q228V, a residue putatively involved in nystose and inulin binding, and S281I, involved in a polar link at the dimer interface. Moreover, a significant decrease in catalytic efficiency against inulin was observed in the mutants Q435A and Y462A, both located in the ␤-sandwich domain of the second monomer. This highlights the essential function that oligomerization plays in substrate specificity and assigns, for the first time, a direct catalytic role to the supplementary domain of a GH32 enzyme.Fructans, the fructose-rich polymers derived biosynthetically from sucrose, are important storage oligosaccharides and polysaccharides in many bacteria and fungi and numerous plant species. Furthermore, sucrose is one of the most widespread disaccharides in nature and is especially ubiquitous in higher plants as the first free sugar resulting from photosynthesis. It is the major transport compound to bring energy and carbon skeletons from source to sink tissues. Carbohydrate partitioning and sugar sensing are intimately connected to sucrose metabolism; these processes are vital throughout plant development. Therefore, the enzymes involved in fructans and sucrose processing are essential to plant cell metabolism.The enzymes that hydrolyze sucrose are referred to collectively as invertases or ␤-fructofuranosidases (EC 3.2.1.26) and catalyze the release of ␤-fructose from the nonreducing end of various ␤-D-fructofuranoside substrates (Fig. 1). The cleavage of the ␤-glycosidic bond is carried out by a double displacement catalytic mechanism that retains the configuration of the fructose anomeric carbon, two conserved residues, an aspartic and a glutamic acid, being the nucleophile and the general acid-base catalyst, respectively. On the basis of the amino acid sequences (1) they are classified into family 32 of the glycosylhydrolases (GH32), 3 which are included in...

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“…The β-fructofuranosidase enzyme and the three components of the ABC transport system share 48-71% identity (Table S1) with similar proteins encoded in an identical cluster structure by C. beijerinckii NCIMB 8052 (genome sequence accession number CP000721). These β-fructofuranosidases contain the three crucial active-site residues, D/D/E(C) within the conserved domains D1, N3, and N5 (16). No characteristic signal peptide (SignalP predict program) or membrane-anchoring domain could be identified on the R. inulinivorans enzyme.…”

Section: Microarray Detection Of Genes Differentially Expressed Duringmentioning

confidence: 99%

“…Despite the diversity in nomenclature of this group of enzymes (β-fructosidases, β-fructofuranosidases, sucrose-6-phosphate hydrolases, endo-inulinases, exo-inulinases, invertases, and saccharases), they all contain highly conserved residues and motifs and are members of glycosyl hydrolase (GH) families 32 or 68. This superfamily also includes fungal enzymes (15,16). Exoacting β-fructofuranosidases cleave the terminal β,2-1 bonds linking the fructose monomers, but most enzymes also have some invertase activity against the β,2-6 bonds between the terminal glucose-fructose units (17).…”

mentioning

confidence: 99%

Substrate-driven gene expression in Roseburia inulinivorans : Importance of inducible enzymes in the utilization of inulin and starch

Scott

Martin

Chassard

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

117

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Roseburia inulinivorans is a recently identified motile representative of the Firmicutes that contributes to butyrate formation from a variety of dietary polysaccharide substrates in the human large intestine. Microarray analysis was used here to investigate substratedriven gene-expression changes in R. inulinivorans A2-194. A cluster of fructo-oligosaccharide/inulin utilization genes induced during growth on inulin included one encoding a β-fructofuranosidase protein that was prominent in the proteome of inulin-grown cells. This cluster also included a 6-phosphofructokinase and an ABC transport system, whereas a distinct inulin-induced 1-phosphofructokinase was linked to a fructose-specific phosphoenolpyruvatedependent sugar phosphotransferase system (PTS II transport enzyme). Real-time PCR analysis showed that the β-fructofuranosidase and adjacent ABC transport protein showed greatest induction during growth on inulin, whereas the 1-phosphofructokinase enzyme and linked sugar phosphotransferase transport system were most strongly up-regulated during growth on fructose, indicating that these two clusters play distinct roles in the use of inulin. The R. inulinivorans β-fructofuranosidase was overexpressed in Escherichia coli and shown to hydrolyze fructans ranging from inulin down to sucrose, with greatest activity on fructo-oligosaccharides. Genes induced on starch included the major extracellular α-amylase and two distinct α-glucanotransferases together with a gene encoding a flagellin protein. The latter response may be concerned with improving bacterial access to insoluble starch particles.anaerobic gut bacteria | differential gene expression | fructooligosaccharides | butyrate | prebiotic P lant cell wall polysaccharides, storage polysaccharides such as resistant starch and inulin, and many oligosaccharides of plant origin remain undigested in the upper gastrointestinal tract and become important substrates for the growth of colonic bacteria. Prebiotics are defined as dietary substrates that reach the colon where they selectively stimulate the growth of beneficial gut bacteria (1), with the most widely used prebiotics being the fructans inulin and fructo-oligosaccharides (FOS). Inulin is a linear polymer [degree of polymerization (DP) = 3-60] of β-2,1-linked fructose monomers with a terminal glucose residue, whereas FOS have the same backbone but a maximal chain length of 8 monomeric units. The increasing use of prebiotics to enhance gut health is driving research into their mode of action. Many studies have shown that both inulin and FOS selectively stimulate the growth of potentially beneficial gut bacteria such as bifidobacteria and lactobacilli (reviewed in ref.2). However, only a few studies have considered the potential for stimulation of other bacterial groups that may also be beneficial (3-6).The bifidogenic dose of inulin has been defined as 5-8 g/d (7), yet the effect of such supplementation on other beneficial groups of gut bacteria and the differences relating to different compositions of inulin...

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?-Fructosidase superfamily: Homology with some ?-L-arabinases and ?-D-xylosidases

Cited by 61 publications

References 47 publications

Genomics Review of Holocellulose Deconstruction by Aspergilli

Genomics Review of Holocellulose Deconstruction by Aspergilli

Structural and Kinetic Analysis of Schwanniomyces occidentalis Invertase Reveals a New Oligomerization Pattern and the Role of Its Supplementary Domain in Substrate Binding

Substrate-driven gene expression in Roseburia inulinivorans : Importance of inducible enzymes in the utilization of inulin and starch

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