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A Single-Site Mutation at Ser146 Expands the Reactivity of the Oxygenase Component of p-Hydroxyphenylacetate 3-Hydroxylase.
Dhammaraj, Taweesak; Pinthong, Chatchadaporn; Visitsatthawong, Surawit; Tongsook, Chanakan; Surawatanawong, Panida; Chaiyen, Pimchai.
Afiliação
  • Dhammaraj T; Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University , Rama 6 Road, Bangkok 10400, Thailand.
  • Pinthong C; Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University , Rama 6 Road, Bangkok 10400, Thailand.
  • Visitsatthawong S; Institute for Innovative Learning, Mahidol University , Nakhon Pathom 73170, Thailand.
  • Tongsook C; Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahidol University , Rama 6 Road, Bangkok 10400, Thailand.
  • Surawatanawong P; Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University , Rama 6 Road, Bangkok 10400, Thailand.
  • Chaiyen P; Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahidol University , Rama 6 Road, Bangkok 10400, Thailand.
ACS Chem Biol ; 11(10): 2889-2896, 2016 10 21.
Article em En | MEDLINE | ID: mdl-27541707
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Oxigenases de Função Mista / Mutação Idioma: En Ano de publicação: 2016 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Oxigenases de Função Mista / Mutação Idioma: En Ano de publicação: 2016 Tipo de documento: Article