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Table 2 Quinuclidinone reductase activities of the wild-type and mutant RrQR enzymes

From: Structural basis of stereospecific reduction by quinuclidinone reductase

  Mutation Relative activity for 3-qinuclidinonea Km(mM)b Vmax(unit/mg)a kcat(sec-1)
  WT 100 440 31.2 15.1
Catalytic site S166A ND    
  Y181A ND    
  Y181F ND    
  K185A ND    
Substrate-binding site I167A ND    
  I167V 24.5 308 5.56 2.69
  S168A 115.7 168 19.9 9.64
  N173A 97.8 100 11.6 5.62
  Q178A 164.5 103 20.2 9.79
  F212A ND    
  F212L ND    
  1. ND: not detected.
  2. aThe analyses were performed in the presence of 125 mM 3-quinuclidinone.
  3. bThe analyses were performed in the presence of 350 μM NADPH.