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

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.

Bibliographic Details
Main Authors:	Toshinori Oozeki, Tadashi Nakai, Kazuki Kozakai, Kazuki Okamoto, Shun’ichi Kuroda, Kazuo Kobayashi, Katsuyuki Tanizawa, Toshihide Okajima
Format:	Article
Language:	English
Published:	Nature Publishing Group 2021-02-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-021-21200-9

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spelling	doaj-cef3949c87c645ccb83918d7a82e65972021-02-14T12:12:23ZengNature Publishing GroupNature Communications2041-17232021-02-0112111210.1038/s41467-021-21200-9Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactorToshinori Oozeki0Tadashi Nakai1Kazuki Kozakai2Kazuki Okamoto3Shun’ichi Kuroda4Kazuo Kobayashi5Katsuyuki Tanizawa6Toshihide Okajima7Institute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityInstitute of Scientific and Industrial Research, Osaka UniversityAn 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.https://doi.org/10.1038/s41467-021-21200-9
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Toshinori Oozeki Tadashi Nakai Kazuki Kozakai Kazuki Okamoto Shun’ichi Kuroda Kazuo Kobayashi Katsuyuki Tanizawa Toshihide Okajima
spellingShingle	Toshinori Oozeki Tadashi Nakai Kazuki Kozakai Kazuki Okamoto Shun’ichi Kuroda Kazuo Kobayashi Katsuyuki Tanizawa Toshihide Okajima Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor Nature Communications
author_facet	Toshinori Oozeki Tadashi Nakai Kazuki Kozakai Kazuki Okamoto Shun’ichi Kuroda Kazuo Kobayashi Katsuyuki Tanizawa Toshihide Okajima
author_sort	Toshinori Oozeki
title	Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
title_short	Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
title_full	Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
title_fullStr	Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
title_full_unstemmed	Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
title_sort	functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2021-02-01
description	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.
url	https://doi.org/10.1038/s41467-021-21200-9
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Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor

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