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Donor substrate promiscuity of bacterial ß1-3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of ß1-4-galactosyltransferases.
Li, Yanhong; Xue, Mengyang; Sheng, Xue; Yu, Hai; Zeng, Jie; Thon, Vireak; Chen, Yi; Muthana, Musleh M; Wang, Peng G; Chen, Xi.
Afiliação
  • Li Y; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
  • Xue M; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA; National Glycoengineering Research Center and Shandong Province Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, Shandong 250100, China.
  • Sheng X; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
  • Yu H; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
  • Zeng J; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA; School of Food Science, Henan Institute of Science and Technology, Xinxiang, Henan 453003, China.
  • Thon V; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA; Department of Chemistry, Georgia State University, Atlanta, GA 30303, USA.
  • Chen Y; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
  • Muthana MM; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
  • Wang PG; National Glycoengineering Research Center and Shandong Province Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, Shandong 250100, China; Department of Chemistry, Georgia State University, Atlanta, GA 30303, USA.
  • Chen X; Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA. Electronic address: xiichen@ucdavis.edu.
Bioorg Med Chem ; 24(8): 1696-705, 2016 Apr 15.
Article em En | MEDLINE | ID: mdl-26968649
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Helicobacter pylori / N-Acetilglucosaminiltransferases / Galactosiltransferases / Neisseria meningitidis Idioma: En Revista: Bioorg Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Reino Unido
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Helicobacter pylori / N-Acetilglucosaminiltransferases / Galactosiltransferases / Neisseria meningitidis Idioma: En Revista: Bioorg Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Reino Unido