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PubMed Publications| Keyword search (4,163 papers available) |  |
"Bellemare A" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Expansion of Auxiliary Activity Family 5 sequence space via biochemical characterization of six new copper radical oxidases | Fong JK; Mathieu Y; Vo MT; Bellemare A; Tsang A; Brumer H; | 38953370 CSFG |
| 2 | Functional screening pipeline to uncover laccase-like multicopper oxidase enzymes that transform industrial lignins | Sharan AA; Bellemare A; DiFalco M; Tsang A; Vuong TV; Edwards EA; Master ER; | 38000639 CSFG |
| 3 | Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation | Mathieu Y; Raji O; Bellemare A; Di Falco M; Nguyen TTM; Viborg AH; Tsang A; Master E; Brumer H; | 37679837 CSFG |
| 4 | Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93 | Zhao H; Karppi J; Nguyen TTM; Bellemare A; Tsang A; Master E; Tenkanen M; | 36476312 CSFG |
| 5 | Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity | Venegas FA; Koutaniemi S; Langeveld SMJ; Bellemare A; Chong SL; Dilokpimol A; Lowden MJ; Hilden KS; Leyva-Illades JF; Mäkelä MR; My Pham TT; Peng M; Hancock MA; Zheng Y; Tsang A; Tenkanen M; Powlowski J; de Vries RP; | 35405333 CSFG |
| 6 | Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases | Dilokpimol A; Verkerk B; Li X; Bellemare A; Lavallee M; Frommhagen M; Nørmølle Underlin E; Kabel MA; Powlowski J; Tsang A; de Vries RP; | 35187647 CSFG |
| 7 | Fungal Genomic DNA Extraction Methods for Rapid Genotyping and Genome Sequencing. | Bellemare A, John T, Marqueteau S | 29876805 CSFG |
| Title: | Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93 | ||||
| Authors: | Zhao H, Karppi J, Nguyen TTM, Bellemare A, Tsang A, Master E, Tenkanen M | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/36476312/ | ||||
| DOI: | 10.1186/s13068-022-02231-w | ||||
| Publication: | Biotechnology for biofuels and bioproducts | ||||
| Keywords: | AA3_1; CAZy AA3; Cellobiose dehydrogenase; Thermothelomyces myriococcoides; Xylooligosaccharide dehydrogenase; | ||||
| PMID: | 36476312 | Category: | Date Added: | 2022-12-08 | |
| Dept Affiliation: |
CSFG
1 Department of Food and Nutrition, University of Helsinki, Helsinki, Finland. hongbo.zhao@helsinki.fi. 2 Department of Food and Nutrition, University of Helsinki, Helsinki, Finland. 3 Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, QC, H4B 1R6, Canada. 4 Department of Bioproducts and Biosystems, Aalto University, Espoo, Finland. 5 Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON, Canada. |
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Description: |
Background: The Carbohydrate-Active enZymes (CAZy) auxiliary activity family 3 (AA3) comprises flavin adenine dinucleotide-dependent (FAD) oxidoreductases from the glucose-methanol-choline (GMC) family, which play auxiliary roles in lignocellulose conversion. The AA3 subfamily 1 predominantly consists of cellobiose dehydrogenases (CDHs) that typically comprise a dehydrogenase domain, a cytochrome domain, and a carbohydrate-binding module from family 1 (CBM1). Results: In this work, an AA3_1 gene from T. myriococcoides CBS 398.93 encoding only a GMC dehydrogenase domain was expressed in Aspergillus niger. Like previously characterized CDHs, this enzyme (TmXdhA) predominantly accepts linear saccharides with ß-(1 ? 4) linkage and targets the hydroxyl on the reducing anomeric carbon. TmXdhA was distinguished, however, by its preferential activity towards xylooligosaccharides over cellooligosaccharides. Amino acid sequence analysis showed that TmXdhA possesses a glutamine at the substrate-binding site rather than a threonine or serine that occupies this position in previously characterized CDHs, and structural models suggest the glutamine in TmXdhA could facilitate binding to pentose sugars. Conclusions: The biochemical analysis of TmXdhA revealed a catalytic preference for xylooligosaccharide substrates. The modeled structure of TmXdhA provides a reference for the screening of oxidoreductases targeting xylooligosaccharides. We anticipate TmXdhA to be a good candidate for the conversion of xylooligosaccharides to added-value chemicals by its exceptional catalytic ability. |
