A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity
Biliverdin reductase (BVR) catalyses the last step in haem degradation. Here the authors present the crystal structure of cyanobacterial BVR bound to its substrate biliverdin and oxidised cofactor NADP+, which was used to propose the catalytic mechanism of this enzyme.
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Nature Portfolio
2017
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oai:doaj.org-article:b06cc2b209254f53ab3b9dcf32b22df82021-12-02T14:40:46ZA substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity10.1038/ncomms143972041-1723https://doaj.org/article/b06cc2b209254f53ab3b9dcf32b22df82017-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms14397https://doaj.org/toc/2041-1723Biliverdin reductase (BVR) catalyses the last step in haem degradation. Here the authors present the crystal structure of cyanobacterial BVR bound to its substrate biliverdin and oxidised cofactor NADP+, which was used to propose the catalytic mechanism of this enzyme.Haruna TakaoKei HirabayashiYuki NishigayaHaruna KourikiTetsuko NakaniwaYoshinori HagiwaraJiro HaradaHideaki SatoToshimasa YamazakiYoichi SakakibaraMasahito SuikoYujiro AsadaYasuhiro TakahashiKen YamamotoKeiichi FukuyamaMasakazu SugishimaKei WadaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Haruna Takao Kei Hirabayashi Yuki Nishigaya Haruna Kouriki Tetsuko Nakaniwa Yoshinori Hagiwara Jiro Harada Hideaki Sato Toshimasa Yamazaki Yoichi Sakakibara Masahito Suiko Yujiro Asada Yasuhiro Takahashi Ken Yamamoto Keiichi Fukuyama Masakazu Sugishima Kei Wada A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| description |
Biliverdin reductase (BVR) catalyses the last step in haem degradation. Here the authors present the crystal structure of cyanobacterial BVR bound to its substrate biliverdin and oxidised cofactor NADP+, which was used to propose the catalytic mechanism of this enzyme. |
| format |
article |
| author |
Haruna Takao Kei Hirabayashi Yuki Nishigaya Haruna Kouriki Tetsuko Nakaniwa Yoshinori Hagiwara Jiro Harada Hideaki Sato Toshimasa Yamazaki Yoichi Sakakibara Masahito Suiko Yujiro Asada Yasuhiro Takahashi Ken Yamamoto Keiichi Fukuyama Masakazu Sugishima Kei Wada |
| author_facet |
Haruna Takao Kei Hirabayashi Yuki Nishigaya Haruna Kouriki Tetsuko Nakaniwa Yoshinori Hagiwara Jiro Harada Hideaki Sato Toshimasa Yamazaki Yoichi Sakakibara Masahito Suiko Yujiro Asada Yasuhiro Takahashi Ken Yamamoto Keiichi Fukuyama Masakazu Sugishima Kei Wada |
| author_sort |
Haruna Takao |
| title |
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| title_short |
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| title_full |
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| title_fullStr |
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| title_full_unstemmed |
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| title_sort |
substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/b06cc2b209254f53ab3b9dcf32b22df8 |
| work_keys_str_mv |
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