Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor.
作者： Katsuyuki Tanizawa , Kazuki Okamoto , Shun’ichi Kuroda , Toshihide Okajima , Tadashi Nakai
DOI: 10.1038/S41467-021-21200-9
关键词:
摘要: Bioconversion of peptidyl amino acids into enzyme cofactors is an important post-translational modification. Here, we report a flavoprotein, essential for biosynthesis protein-derived quinone cofactor, cysteine tryptophylquinone, contained in widely distributed bacterial enzyme, quinohemoprotein amine dehydrogenase. The purified flavoprotein catalyzes the single-turnover dihydroxylation tryptophylquinone-precursor, tryptophan, protein substrate containing triple intra-peptidyl crosslinks that are pre-formed by radical S-adenosylmethionine within ternary complex these proteins. Crystal structure tryptophan dihydroxylase reveals large pocket may dock with bound flavin adenine dinucleotide situated close to precursor tryptophan. Based on enzyme-protein docking model, propose chemical reaction mechanism catalyzed monooxygenase. diversity tryptophylquinone-generating systems suggests convergent evolution tryptophan-derived different An type modification conversion acid cofactor. authors functional and structural characterization monooxygenase tryptophylquinone (CTQ)
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