Characterization of the glutathione S-transferases that belong to the GSTFuA class in Ceriporiopsis subvermispora: Implications in intracellular detoxification and metabolism of wood-derived compounds
| Autor: | Meng-I Lin, Wan Hasnidah Wan Osman, Takashi Nagata, Keiko Kondo, Masato Katahira |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cellular detoxification Intracellular Space medicine.disease_cause Biochemistry Esterase Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Structural Biology medicine Lignin Amino Acid Sequence Cloning Molecular Molecular Biology Escherichia coli Glutathione Transferase chemistry.chemical_classification Temperature General Medicine Glutathione Metabolism Hydrogen-Ion Concentration Wood Kinetics 030104 developmental biology Enzyme chemistry Cumene hydroperoxide Inactivation Metabolic Coriolaceae |
| Zdroj: | International Journal of Biological Macromolecules. 113:1158-1166 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2018.03.029 |
| Popis: | Glutathione S-transferases (GSTs) of wood-degrading fungi play essential roles in cellular detoxification processes and endogenous metabolism. Fungal GSTs of GSTFuA class are suggested to be involved in lignin degradation. Ceriporiopsis subvermispora is one of the important model fungi of the selective lignin degraders, we found it interesting to study its GSTs. Here, we characterized the activities of two GSTs of the GSTFuA class of C. subvermispora (CsGST63524 and CsGST83044). A high-yield expression systems involving Escherichia coli was developed for each of these enzymes. Both enzymes were found to exhibit GSH-conjugation activity toward 1-chloro-2,4-dinitrobenzene, and GSH-peroxidase activity toward cumene hydroperoxide. Both enzymes showed high GSH-conjugation activity under basic conditions (pH8.0 to 9.0), and the optimum temperature for their activity was 40°C. In addition, three fluorescent compounds were used i.e., methylumbelliferyl acetovanillone was used to monitor etherase activity, and 5-chloromethylfluorescein diacetate and 4-methylumbelliferyl acetate to monitor esterase activity. CsGST83044 exhibited both etherase and esterase activities, while CsGST63524 displayed only esterase activity, which was much higher than that of CsGST83044. These findings imply the functional diversity of the GSTFuA class GSTs of C. subvermispora, suggesting that each protein plays distinctive roles in both the fungal detoxification system and wood compound metabolism. |
| Databáze: | OpenAIRE |
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