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Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis
The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Catalysis proceeds through a high valent bis-Fe(IV) redox state and require...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , , , , , |
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| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
2011
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3193188/ https://ncbi.nlm.nih.gov/pubmed/21969534 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1109423108 |
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