Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
In: Nature Communications, Jg. 12 (2021), Heft 1, S. 1-12
Online
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Zugriff:
Bioconversion of peptidyl amino acids into enzyme cofactors is an important post-translational modification. Here, we report a flavoprotein, essential for biosynthesis of a protein-derived quinone cofactor, cysteine tryptophylquinone, contained in a widely distributed bacterial enzyme, quinohemoprotein amine dehydrogenase. The purified flavoprotein catalyzes the single-turnover dihydroxylation of the tryptophylquinone-precursor, tryptophan, in the protein substrate containing triple intra-peptidyl crosslinks that are pre-formed by a radical S-adenosylmethionine enzyme within the ternary complex of these proteins. Crystal structure of the peptidyl tryptophan dihydroxylase reveals a large pocket that may dock the protein substrate with the bound flavin adenine dinucleotide situated close to the precursor tryptophan. Based on the enzyme-protein substrate docking model, we propose a chemical reaction mechanism of peptidyl tryptophan dihydroxylation catalyzed by the flavoprotein monooxygenase. The diversity of the tryptophylquinone-generating systems suggests convergent evolution of the peptidyl tryptophan-derived cofactors in different proteins.
An important type of post-translational protein modification is the conversion of peptidyl amino acid into enzyme cofactor. Here, the authors report functional and structural characterization of a flavoprotein monooxygenase essential for biosynthesis of cysteine tryptophylquinone (CTQ) cofactor.
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Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
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Autor/in / Beteiligte Person: | Nakai, Tadashi ; Kobayashi, Kazuo ; Oozeki, Toshinori ; Kozakai, Kazuki ; Okajima, Toshihide ; Tanizawa, Katsuyuki ; Okamoto, Kazuki ; Kuroda, Shun'ichi |
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Zeitschrift: | Nature Communications, Jg. 12 (2021), Heft 1, S. 1-12 |
Veröffentlichung: | Nature Portfolio, 2021 |
Medientyp: | unknown |
ISSN: | 2041-1723 (print) |
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