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

Lignende værker

• Regiospecific Chlorination of (S)-β-Tyrosyl-S-Carrier Protein Catalyzed by SgcC3 in the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027
  af: Lin, Shuangjun, et al.
  Udgivet: (2007)
• 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
  af: Chang, Chin-Yuan, et al.
  Udgivet: (2016)
• Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027
  af: Van Lanen, Steven G., et al.
  Udgivet: (2009)
• Specificity of the Ester Bond-Forming Condensation Enzyme SgcC5 in C-1027 Biosynthesis
  af: Lin, Shuangjun, et al.
  Udgivet: (2012)
• Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism
  af: Van Lanen, Steven G., et al.
  Udgivet: (2008)