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PubMed Publications| Keyword search (4,163 papers available) |  |
"Zhao H" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Adaptive sliding mode fault-tolerant control of an over-actuated hybrid VTOL fixed-wing UAV under transition flight | Wang B; Zhao H; Hu X; Shen Y; Li N; | 41475926 ENCS |
| 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 | 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 |
| 4 | Author Correction: Building a global alliance of biofoundries. | Hillson N, Caddick M, Cai Y, Carrasco JA, Chang MW, Curach NC, Bell DJ, Feuvre RL, Friedman DC, Fu X, Gold ND, Herrgård MJ, Holowko MB, Johnson JR, Johnson RA, Keasling JD, Kitney RI, Kondo A, Liu C, Martin VJJ, Menolascina F, Ogino C, Patron NJ, Pavan M, Poh CL, Pretorius IS, Rosser SJ, Scrutton NS, Storch M, Tekotte H, Travnik E, Vickers CE, Yew WS, Yuan Y, Zhao H, Freemont PS | 31296848 CHEMBIOCHEM |
| 5 | A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. | Zhao H, Ghirlando R, Alfonso C, Arisaka F, Attali I, Bain DL, Bakhtina MM, Becker DF, Bedwell GJ, Bekdemir A, Besong TM, Birck C, Brautigam CA, Brennerman W, Byron O, Bzowska A, Chaires JB, Chaton CT, Cölfen H, Connaghan KD, Crowley KA, Curth U, Daviter T, Dean WL, Díez AI, Ebel C, Eckert DM, Eisele LE, Eisenstein E, England P, Escalante C, Fagan JA, Fairman R, Finn RM, Fischle W, de la Torre JG, Gor J, Gustafsson H, Hall D, Harding SE, Cifre JG, Herr AB, Howell EE, Isaac RS, Jao SC, Jose D, Kim SJ, Kokona | 25997164 NA |
| 6 | Building a global alliance of biofoundries. | Hillson N, Caddick M, Cai Y, Carrasco JA, Chang MW, Curach NC, Bell DJ, Le Feuvre R, Friedman DC, Fu X, Gold ND, Herrgård MJ, Holowko MB, Johnson JR, Johnson RA, Keasling JD, Kitney RI, Kondo A, Liu C, Martin VJJ, Menolascina F, Ogino C, Patron NJ, Pavan M, Poh CL, Pretorius IS, Rosser SJ, Scrutton NS, Storch M, Tekotte H, Travnik E, Vickers CE, Yew WS, Yuan Y, Zhao H, Freemont PS | 31068573 CHEMBIOCHEM |
| 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. |
