Changing the substrate specificity of penicillin G acylase from Kluyvera citrophila through selective pressure.

Eitemau Tebyg

• Structure mediation in substrate binding and post-translational processing of penicillin acylases: Information from mutant structures of Kluyvera citrophila penicillin G acylase
  gan: Chand, Deepak, et al.
  Cyhoeddwyd: (2015)
• Chemical modification of serine at the active site of penicillin acylase from Kluyvera citrophila.
  gan: Martín, J, et al.
  Cyhoeddwyd: (1991)
• Rapid burst kinetics in the hydrolysis of 4-nitrophenyl acetate by penicillin G acylase from Kluyvera citrophila. Effects of mutation F360V on rate constants for acylation and de-acylation.
  gan: Roa, A, et al.
  Cyhoeddwyd: (1996)
• Cloning, overexpression, crystallization and preliminary X-ray crystallographic analysis of a slow-processing mutant of penicillin G acylase from Kluyvera citrophila
  gan: Varshney, Nishant Kumar, et al.
  Cyhoeddwyd: (2013)
• Inactivation of penicillin acylase from Kluyvera citrophila by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline: a case of time-dependent non-covalent enzyme inhibition.
  gan: Martín, J, et al.
  Cyhoeddwyd: (1993)