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The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold

Nature Structural Biology volume 1, pages 532–537 (1994)Cite this article

Abstract

The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 Å resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the α/β hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.

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Author information

Author notes

  1. H. Sobek

    Present address: Boehringer Mannheim GmbH, D-82372, Penzberg, Germany

Authors and Affiliations

  1. GBF (Gesellschaft für Biotechnologische Forschung), Department of Molecular Structure Research, Mascheroder Weg 1, D-38124, Braunschweig, Germany

    H.J. Hecht & H. Sobek

  2. Institute of Microbiology, University of Hohenheim, Garbenstr. 30, D-70593, Stuttgart, Germany

    T. Haag & O. Pfeifer

  3. Department of Biochemistry, Technical University of Dresden, D-01062, Dresden, Germany

    K.-H. van Pée

Authors
  1. H.J. Hecht
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  2. H. Sobek
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  3. T. Haag
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  4. O. Pfeifer
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  5. K.-H. van Pée
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Hecht, H., Sobek, H., Haag, T. et al. The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold. Nat Struct Mol Biol 1, 532–537 (1994). https://doi.org/10.1038/nsb0894-532

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  • DOI: https://doi.org/10.1038/nsb0894-532

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