Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor

Toshinori Oozeki, Tadashi Nakai, Kazuki Kozakai, Kazuki Okamoto, Shun’ichi Kuroda, Kazuo Kobayashi, Katsuyuki Tanizawa and Toshihide Okajima ()
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Toshinori Oozeki: Osaka University
Tadashi Nakai: Osaka University
Kazuki Kozakai: Osaka University
Kazuki Okamoto: Osaka University
Shun’ichi Kuroda: Osaka University
Kazuo Kobayashi: Osaka University
Katsuyuki Tanizawa: Osaka University
Toshihide Okajima: Osaka University

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21200-9

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DOI: 10.1038/s41467-021-21200-9

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