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Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase.
Chen, Ridao; Gao, Bingquan; Liu, Xiao; Ruan, Feiying; Zhang, Yong; Lou, Jizhong; Feng, Keping; Wunsch, Carsten; Li, Shu-Ming; Dai, Jungui; Sun, Fei.
Afiliação
  • Chen R; State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
  • Gao B; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
  • Liu X; University of Chinese Academy of Sciences, Beijing, China.
  • Ruan F; State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
  • Zhang Y; State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
  • Lou J; Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
  • Feng K; Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
  • Wunsch C; State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
  • Li SM; Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Marburg, Germany.
  • Dai J; Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Marburg, Germany.
  • Sun F; State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
Nat Chem Biol ; 13(2): 226-234, 2017 02.
Article em En | MEDLINE | ID: mdl-27992881
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aspergillus / Dimetilaliltranstransferase Idioma: En Ano de publicação: 2017 Tipo de documento: Article
Texto completo
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XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aspergillus / Dimetilaliltranstransferase Idioma: En Ano de publicação: 2017 Tipo de documento: Article