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Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

Nature Structural Biology volume 4, pages 975–979 (1997)Cite this article

The flavin mononucleotide (FMN)-binding protein from Desulfovibrio vulgaris (Miyazaki F) is structurally related to a so far hypothetical single-domain precursor of chymotrypsin, with the FMN-binding site coinciding with part of the active site of the protease.

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Author notes

  1. Edvards Liepinsh and Masaya Kitamura: The first two authors contributed equally to the work.

Authors and Affiliations

  1. Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden

    Edvards Liepinsh & Gottfried Otting

  2. Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka, 558, Japan

    Masaya Kitamura, Takayuki Murakami & Tadao Nakaya

Authors
  1. Edvards Liepinsh
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  2. Masaya Kitamura
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  3. Takayuki Murakami
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  4. Tadao Nakaya
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  5. Gottfried Otting
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Liepinsh, E., Kitamura, M., Murakami, T. et al. Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). Nat Struct Mol Biol 4, 975–979 (1997). https://doi.org/10.1038/nsb1297-975

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