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Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps.
Sato, Hideaki; Sugishima, Masakazu; Tsukaguchi, Mai; Masuko, Takahiro; Iijima, Mikuru; Takano, Mitsunori; Omata, Yoshiaki; Hirabayashi, Kei; Wada, Kei; Hisaeda, Yoshio; Yamamoto, Ken.
Afiliação
  • Sato H; Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan.
  • Sugishima M; Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan.
  • Tsukaguchi M; Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan.
  • Masuko T; Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
  • Iijima M; Department of Pure and Applied Physics, School of Advanced Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.
  • Takano M; Department of Pure and Applied Physics, School of Advanced Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.
  • Omata Y; Department of Molecular Biology, Faculty of Pharmaceutical Science, Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama 245-0066, Japan.
  • Hirabayashi K; Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
  • Wada K; Department of Medical Sciences, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.
  • Hisaeda Y; Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
  • Yamamoto K; Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan.
Biochem J ; 478(5): 1023-1042, 2021 03 12.
Article em En | MEDLINE | ID: mdl-33600566
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Porfobilinogênio / Hidroximetilbilano Sintase / Uroporfirinogênios Idioma: En Ano de publicação: 2021 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Porfobilinogênio / Hidroximetilbilano Sintase / Uroporfirinogênios Idioma: En Ano de publicação: 2021 Tipo de documento: Article