Substrate kinetic isotope effects in dehydrogenase coupled active transport in membrane visicles in Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (12) ◽  
pp. 2619-2628 ◽  
Author(s):  
Gregory J. Kaczorowski ◽  
Yak-Fa Cheung ◽  
Christopher Walsh
1989 ◽  
Vol 257 (2) ◽  
pp. 355-359 ◽  
Author(s):  
P K Lehikoinen ◽  
M L Sinnott ◽  
T A Krenitsky

1. alpha-Deuterium kinetic isotope effects on the phosphorolysis of inosine catalysed by Escherichia coli purine nucleoside phosphorylase were measured by the equilibrium-perturbation technique, by using the change in absorbance at 250 nm (approx. 20%). 2. Values of 2H(V/K) of 1.13(9) at pH 5.0, 1.10(5) at pH 6.1, 1.09(4) at pH 7.3, 1.08 at pH 8.4 and 1.16(4) at pH 9.4 were obtained. 3. These are compared with literature alpha-deuterium kinetic isotope effects for this and related reactions. 4. The equilibrium constant, defined as [inosine].[H2PO4-]/[hypoxanthine] [alpha-Rib f OPO3H-], is 46 at 25 degrees C. 5. N-3-beta-D-Ribofuranosylhypoxanthine, an impurity in chemically synthesized inosine, is a substrate.


2005 ◽  
Vol 1751 (2) ◽  
pp. 140-149 ◽  
Author(s):  
Cindy Hunt ◽  
Niloufar Gillani ◽  
Anthony Farone ◽  
Mansoureh Rezaei ◽  
Paul C. Kline

2020 ◽  
Vol 124 (51) ◽  
pp. 10678-10686
Author(s):  
Yuqing Xu ◽  
Kin-Yiu Wong ◽  
Meishan Wang ◽  
Desheng Liu ◽  
Wenkai Zhao ◽  
...  

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