Structural Insights into the Free-standing Condensation Enzyme SgcC5 Catalyzing Ester Bond Formation in the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027

Ítems similars

• Crystal Structures of SgcE6 and SgcC, the Two-Component Monooxygenase That Catalyzes Hydroxylation of a Carrier Protein-Tethered Substrate during the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027 in Streptomyces globisporus
  per: Chang, Chin-Yuan, et al.
  Publicat: (2016)
• Specificity of the Ester Bond-Forming Condensation Enzyme SgcC5 in C-1027 Biosynthesis
  per: Lin, Shuangjun, et al.
  Publicat: (2012)
• Crystal Structure of SgcJ, An NTF2-Like Superfamily Protein Involved in Biosynthesis of the 9-Membered Enediyne Antitumor Antibiotic C-1027
  per: Huang, Tingting, et al.
  Publicat: (2016)
• Regiospecific Chlorination of (S)-β-Tyrosyl-S-Carrier Protein Catalyzed by SgcC3 in the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027
  per: Lin, Shuangjun, et al.
  Publicat: (2007)
• Characterization of the Two-Component, FAD-Dependent Monooxygenase SgcC That Requires Carrier Protein-Tethered Substrates for the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027
  per: Lin, Shuangjun, et al.
  Publicat: (2008)