Analysis of the role of tryptophan residues in aspartate transcarbamylase by site-directed mutagenesis and fluorescence measurements

1992 ◽  
Author(s):  
Patrick Tauc ◽  
Luc Fetler ◽  
Guy Herve ◽  
Moncef Ladjmi ◽  
Jean-Claude Brochon
2009 ◽  
Vol 96 (3) ◽  
pp. 326a
Author(s):  
Ravi Kanth Kamlekar ◽  
Yongguang Gao ◽  
Helen Pike ◽  
Roopa Kenoth ◽  
Franklyn G. Prendergast ◽  
...  

1994 ◽  
Vol 300 (1) ◽  
pp. 111-115 ◽  
Author(s):  
M H Rider ◽  
K M Crepin ◽  
M De Cloedt ◽  
L Bertrand ◽  
L Hue

Asp-130 of the recombinant skeletal-muscle 6-phosphofructo-2-kinase (PFK-2)/fructose-2,6-bisphosphatase was mutated into Ala in order to study its role in catalysis and/or substrate binding. The D130A mutant displayed a 30- to 140-fold decreased 2-kinase Vmax, depending on the pH, and a 30- and 60-fold increase in Km for MgATP and Fru-6-P respectively at pH 8.5 compared with the wild-type. Mutagenesis of Asp-130 to Ala had no effect on the 2-phosphatase activity, and fluorescence measurements indicated that the changes in kinetic properties of PFK-2 in the D130A mutant were not due to instability. The role of Asp-130 in the 2-kinase reaction is discussed and compared with that of Asp-103 of 6-phosphofructo-1-kinase from Escherichia coli, which binds Mg2+.


1992 ◽  
Vol 267 (36) ◽  
pp. 25754-25758
Author(s):  
J Wu ◽  
D Filer ◽  
A.J. Friedhoff ◽  
M Goldstein

1990 ◽  
Vol 265 (20) ◽  
pp. 11788-11795
Author(s):  
K D Egeberg ◽  
B A Springer ◽  
S G Sligar ◽  
T E Carver ◽  
R J Rohlfs ◽  
...  

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