The Crystal Structure of Feruloyl Esterase A from Aspergillus niger Suggests Evolutive Functional Convergence in Feruloyl Esterase Family

Hermoso, J.A.; Sanz‐Aparicio, Julia; Molina, Rafael; Juge, Nathalie; González, R. N.; Faulds, Craig B.

doi:10.1016/j.jmb.2004.03.003

Cited by 107 publications

(98 citation statements)

References 59 publications

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“…Results were evaluated based on the resulting binding energy (more positive energies indicate stronger binding and negative energies mean no binding), the number of genetic runs per cluster, the orientation of the ligand per cluster, and the distance of carbonyl carbon from the catalytic serine of the cluster resulting in a catalytic orientation. This was determined according to Suzuki et al [33] based on the co-crystallization of FA with AnFaeA from Aspergillus niger [42] where the hydroxycinnamate moiety of the ligand is placed in the binding pocket while the substitution is extending outside the pocket. Ligand-receptor complexes were visualized and surface properties were calculated by YASARA [43].…”

Section: Bioinformatic Toolsmentioning

confidence: 99%

The Synthetic Potential of Fungal Feruloyl Esterases: A Correlation with Current Classification Systems and Predicted Structural Properties

et al. 2018

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Twenty-eight fungal feruloyl esterases (FAEs) were evaluated for their synthetic abilities in a ternary system of n-hexane: t-butanol: 100 mM MOPS-NaOH pH 6.0 forming detergentless microemulsions. Five main derivatives were synthesized, namely prenyl ferulate, prenyl caffeate, butyl ferulate, glyceryl ferulate, and L-arabinose ferulate, offering, in general, higher yields when more hydrophilic alcohol substitutions were used. Acetyl xylan esterase-related FAEs belonging to phylogenetic subfamilies (SF) 5 and 6 showed increased synthetic yields among tested enzymes. In particular, it was shown that FAEs belonging to SF6 generally transesterified aliphatic alcohols more efficiently while SF5 members preferred bulkier L-arabinose. Predicted surface properties and structural characteristics were correlated with the synthetic potential of selected tannase-related, acetyl-xylan-related, and lipase-related FAEs (SF1-2, -6, -7 members) based on homology modeling and small molecular docking simulations.

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Section: Bioinformatic Toolsmentioning

confidence: 99%

The Synthetic Potential of Fungal Feruloyl Esterases: A Correlation with Current Classification Systems and Predicted Structural Properties

et al. 2018

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“…The catalytic triad (Ser133-His247-Asp194) forms the active site of this enzyme. The active site cavity is confined by a lid, analogous to the case in lipases, and by a loop that confers plasticity to the substrate-binding site (221). Feruloyl esterases were initially classified by aromatic functional categories (222,223), and later the classification was extended to subfamilies A, B, C, and D, based on primary amino acid sequence similarity and substrate specificity against four model substrates, i.e., methyl 3-methoxy-4-hydroxycinnamate (MFA), methyl 3,4-dihydroxycinnamate (MCA), methyl 4-hydroxycinnamate (MpCA), and methyl 3,5-dimethoxy-4-hydroxycinnamate (MSA) (224,225).…”

Section: Hemicellulasesmentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

113

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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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“…On the basis of their primary sequences and substrate specificity against four model substrates, methyl ferulate (MFA), methyl caffeate (MCA), methyl p-coumarate (MpCA), and methyl sinapate (MSA), Faes are classified as types A, B, C, and D (8,36). Despite having various primary amino acid sequences, Faes share similar three-dimensional structures, with an ␣/␤-hydrolase having a serine, histidine, and aspartic acid catalytic triad (22,26,38).…”

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confidence: 99%

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Cai

Luo

et al. 2011

Appl Environ Microbiol

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Feruloyl esterases (Faes) constitute a subclass of carboxyl esterases that specifically hydrolyze the ester linkages between ferulate and polysaccharides in plant cell walls. Until now, the described microbial Faes were mainly from fungi. In this study, we report that Cellulosilyticum ruminicola H1, a previously described fibrolytic rumen bacterium, possesses three different active feruloyl esterases, FaeI, FaeII, and FaeIII. Phylogenetic analysis classified the described bacterial Faes into two types, FaeI and FaeII in type I and FaeIII in type II. Substrate specificity assays indicated that FaeI is more active against the ester bonds in natural hemicelluloses and FaeIII preferentially attacks the ferulate esters with a small moiety, such as methyl groups, while FaeII is active on both types of substrates. Among the three feruloyl esterase genes, faeI was the only one induced significantly by xylose and xylan, while pectin appeared to moderately induce the three genes during the late log phase to stationary phase. Western blot analysis determined that FaeI and FaeIII were secreted and cytoplasmic proteins, respectively, whereas FaeII seemed to be cell associated. The addition of FaeI and FaeII but not FaeIII enhanced the activity of a xylanase on maize cob, suggesting a synergy of the former two with xylanase. Hence, we propose that the three feruloyl esterases work in concert to hydrolyze ferulate esters in natural hemicelluloses.

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The Crystal Structure of Feruloyl Esterase A from Aspergillus niger Suggests Evolutive Functional Convergence in Feruloyl Esterase Family

Cited by 107 publications

References 59 publications

The Synthetic Potential of Fungal Feruloyl Esterases: A Correlation with Current Classification Systems and Predicted Structural Properties

The Synthetic Potential of Fungal Feruloyl Esterases: A Correlation with Current Classification Systems and Predicted Structural Properties

Genomics Review of Holocellulose Deconstruction by Aspergilli

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

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