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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: | 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. |
