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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.