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Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.
Frank, Annika; Seel, Catharina Julia; Groll, Michael; Gulder, Tanja.
Afiliación
  • Frank A; Department Chemie, Center for Integrated Protein Science at the Department Chemie and Catalysis Research Center (CRC), Technische Universität München, Lichtenbergstrasse 4, 85747, Garching, Germany.
  • Seel CJ; Department Chemie, Center for Integrated Protein Science at the Department Chemie and Catalysis Research Center (CRC), Technische Universität München, Lichtenbergstrasse 4, 85747, Garching, Germany.
  • Groll M; Department Chemie, Center for Integrated Protein Science at the Department Chemie and Catalysis Research Center (CRC), Technische Universität München, Lichtenbergstrasse 4, 85747, Garching, Germany.
  • Gulder T; Department Chemie, Center for Integrated Protein Science at the Department Chemie and Catalysis Research Center (CRC), Technische Universität München, Lichtenbergstrasse 4, 85747, Garching, Germany. tanja.gulder@tum.de.
Chembiochem ; 17(21): 2028-2032, 2016 11 03.
Article en En | MEDLINE | ID: mdl-27542168
ABSTRACT
Vanadium-dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina (AmVHPO), including its structure determination by X-ray crystallography. Compared to other VHPOs, the AmVHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high-yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Peroxidasas / Cianobacterias / Halogenación / Biocatálisis Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2016 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Peroxidasas / Cianobacterias / Halogenación / Biocatálisis Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2016 Tipo del documento: Article País de afiliación: Alemania