Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis.

Lignende værker

• Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active-site loop.
  af: Rodrigues-Lima, F, et al.
  Udgivet: (2001)
• Identification of amino acids imparting acceptor substrate selectivity to human arylamine acetyltransferases NAT1 and NAT2.
  af: Goodfellow, G H, et al.
  Udgivet: (2000)
• Probing the Catalytic Potential of the Hamster Arylamine N-Acetyltransferase 2 Catalytic Triad by Site-directed Mutagenesis of the Proximal Conserved Residue, Tyrosine 190
  af: Zhou, Xin, et al.
  Udgivet: (2009)
• Alternative catalytic residues in the active site of Esco acetyltransferases
  af: Ajam, Tahereh, et al.
  Udgivet: (2020)
• Characterization of Evolutionarily Conserved Trypanosoma cruzi NatC and NatA-N-Terminal Acetyltransferase Complexes
  af: Ochaya, Stephen, et al.
  Udgivet: (2019)