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PubMed Publications| Keyword search (4,164 papers available) |  |
"Nguyen TTM" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Comparative genomic analysis of thermophilic fungi reveals convergent evolutionary adaptations and gene losses | Steindorff AS; Aguilar-Pontes MV; Robinson AJ; Andreopoulos B; LaButti K; Kuo A; Mondo S; Riley R; Otillar R; Haridas S; Lipzen A; Grimwood J; Schmutz J; Clum A; Reid ID; Moisan MC; Butler G; Nguyen TTM; Dewar K; Conant G; Drula E; Henrissat B; Hansel C; Singer S; Hutchinson MI; de Vries RP; Natvig DO; Powell AJ; Tsang A; Grigoriev IV; | 39266695 CSFG |
| 2 | Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases | Zhao H; Karppi J; Mototsune O; Poshina D; Svartström J; Nguyen TTM; Vo TM; Tsang A; Master E; Tenkanen M; | 38539167 CSFG |
| 3 | Comparative analysis of functional diversity of rumen microbiome in bison and beef heifers | Nguyen TTM; Badhan AK; Reid ID; Ribeiro G; Gruninger R; Tsang A; Guan LL; McAllister T; | 38054735 CSFG |
| 4 | 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 |
| 5 | 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 |
| 6 | Identification of a Novel Biosynthetic Gene Cluster in Aspergillus niger Using Comparative Genomics | Evdokias G; Semper C; Mora-Ochomogo M; Di Falco M; Nguyen TTM; Savchenko A; Tsang A; Benoit-Gelber I; | 34064722 BIOLOGY |
| 7 | Application of Transcriptomics to Compare the Carbohydrate Active Enzymes That Are Expressed by Diverse Genera of Anaerobic Fungi to Degrade Plant Cell Wall Carbohydrates. | Gruninger RJ, Nguyen TTM, Reid ID, Yanke JL, Wang P, Abbott DW, Tsang A, McAllister T | 30061875 CSFG |
| 8 | Efficient genome editing using tRNA promoter-driven CRISPR/Cas9 gRNA in Aspergillus niger. | Song L, Ouedraogo JP, Kolbusz M, Nguyen TTM, Tsang A | 30142205 CSFG |
| 9 | The gold-standard genome of Aspergillus niger NRRL 3 enables a detailed view of the diversity of sugar catabolism in fungi. | Aguilar-Pontes MV, Brandl J, McDonnell E, Strasser K, Nguyen TTM, Riley R, Mondo S, Salamov A, Nybo JL, Vesth TC, Grigoriev IV, Andersen MR, Tsang A, de Vries RP | 30425417 CSFG |
| 10 | Genomic and exoproteomic diversity in plant biomass degradation approaches among Aspergilli | Mäkelä MR; DiFalco M; McDonnell E; Nguyen TTM; Wiebenga A; Hildén K; Peng M; Grigoriev IV; Tsang A; de Vries RP; | 30487660 CSFG |
| Title: | Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases | ||||
| Authors: | Zhao H, Karppi J, Mototsune O, Poshina D, Svartström J, Nguyen TTM, Vo TM, Tsang A, Master E, Tenkanen M | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/38539167/ | ||||
| DOI: | 10.1186/s13068-024-02491-8 | ||||
| Publication: | Biotechnology for biofuels and bioproducts | ||||
| Keywords: | CAZy family AA3_2; Gentiobiose; Oxidoreductase; Phenoxy radical; Sequence similarity network; | ||||
| PMID: | 38539167 | Category: | Date Added: | 2024-03-28 | |
| Dept Affiliation: |
CSFG
1 Department of Food and Nutrition, University of Helsinki, Helsinki, Finland. hongbo.zhao@helsinki.fi. 2 Department of Bioproducts and Biosystems, Aalto University, Espoo, Finland. 3 Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON, Canada. 4 Department of Food and Nutrition, University of Helsinki, Helsinki, Finland. 5 Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, QC, H4B 1R6, Canada. |
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Description: |
Background: Oxidative enzymes targeting lignocellulosic substrates are presently classified into various auxiliary activity (AA) families within the carbohydrate-active enzyme (CAZy) database. Among these, the fungal AA3 glucose-methanol-choline (GMC) oxidoreductases with varying auxiliary activities are attractive sustainable biocatalysts and important for biological function. CAZy AA3 enzymes are further subdivided into four subfamilies, with the large AA3_2 subfamily displaying diverse substrate specificities. However, limited numbers of enzymes in the AA3_2 subfamily are currently biochemically characterized, which limits the homology-based mining of new AA3_2 oxidoreductases. Importantly, novel enzyme activities may be discovered from the uncharacterized parts of this large subfamily. Results: In this study, phylogenetic analyses employing a sequence similarity network (SSN) and maximum likelihood trees were used to cluster AA3_2 sequences. A total of 27 AA3_2 proteins representing different clusters were selected for recombinant production. Among them, seven new AA3_2 oxidoreductases were successfully produced, purified, and characterized. These enzymes included two glucose dehydrogenases (TaGdhA and McGdhA), one glucose oxidase (ApGoxA), one aryl alcohol oxidase (PsAaoA), two aryl alcohol dehydrogenases (AsAadhA and AsAadhB), and one novel oligosaccharide (gentiobiose) dehydrogenase (KiOdhA). Notably, two dehydrogenases (TaGdhA and KiOdhA) were found with the ability to utilize phenoxy radicals as an electron acceptor. Interestingly, phenoxy radicals were found to compete with molecular oxygen in aerobic environments when serving as an electron acceptor for two oxidases (ApGoxA and PsAaoA), which sheds light on their versatility. Furthermore, the molecular determinants governing their diverse enzymatic functions were discussed based on the homology model generated by AlphaFold. Conclusions: The phylogenetic analyses and biochemical characterization of AA3_2s provide valuable guidance for future investigation of AA3_2 sequences and proteins. A clear correlation between enzymatic function and SSN clustering was observed. The discovery and biochemical characterization of these new AA3_2 oxidoreductases brings exciting prospects for biotechnological applications and broadens our understanding of their biological functions. |
