An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli.

Lignende værker

• Cloning of the ilvA538 gene coding for feedback-hypersensitive threonine deaminase from Escherichia coli K-12.
  af: Calhoun, D H, et al.
  Udgivet: (1982)
• Translational coupling between the ilvD and ilvA genes of Escherichia coli.
  af: Harms, E, et al.
  Udgivet: (1988)
• IS2 activates the ilvA gene of Pseudomonas cepacia in Escherichia coli.
  af: Barsomian, G, et al.
  Udgivet: (1987)
• Reduced Transaminase B (IlvE) Activity Caused by the Lack of yjgF Is Dependent on the Status of Threonine Deaminase (IlvA) in Salmonella enterica Serovar Typhimurium
  af: Schmitz, George, et al.
  Udgivet: (2004)
• Complementation Between Different Mutations in the ilvA Gene of Escherichia coli K-12
  af: Favre, Renée, et al.
  Udgivet: (1974)