| Autor: |
Thomas D, Niehaus, Jenelle A, Patterson, Danny C, Alexander, Jakob S, Folz, Michal, Pyc, Brian S, MacTavish, Steven D, Bruner, Robert T, Mullen, Oliver, Fiehn, Andrew D, Hanson |
| Rok vydání: |
2018 |
| Předmět: |
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| Zdroj: |
The Biochemical journal. 476(4) |
| ISSN: |
1470-8728 |
| Popis: |
The tripeptide glutathione (GSH) is implicated in various crucial physiological processes including redox buffering and protection against heavy metal toxicity. GSH is abundant in plants, with reported intracellular concentrations typically in the 1-10 mM range. Various aminotransferases can inadvertently transaminate the amino group of the γ-glutamyl moiety of GSH to produce deaminated glutathione (dGSH), a metabolite damage product. It was recently reported that an amidase known as Nit1 participates in dGSH breakdown in mammals and yeast. Plants have a hitherto uncharacterized homolog of the Nit1 amidase. We show that recombinant |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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