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The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis
The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. The crystal structure of the MauG-preMADH compl...
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| 主要な著者: | , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2010
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3061978/ https://ncbi.nlm.nih.gov/pubmed/21128656 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi101819m |
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