Interaction between uridine diphosphate galactose and uridine diphosphate galactose 4-epimerase from Escherichia coli

Biochemistry ◽  
1972 ◽  
Vol 11 (1) ◽  
pp. 40-44 ◽  
Author(s):  
Y. Seyama ◽  
H. M. Kalckar
1976 ◽  
Vol 155 (2) ◽  
pp. 225-229 ◽  
Author(s):  
P Blackburn ◽  
W Ferdinand

1. The combined effect of the sugar nucleotides UDP-D-fucose or UDP-D-glucuronic acid together with the free sugars D-fucose or L-arabinose is the inactivation of the Escherichia coli enzyme UDP-galactose 4-epimerase (EC 5.1.3.2). The sugar nucleotide or the free sugar alone or the sugar nucleotide plus 5'-Ump do not inactivate the enzyme. 2. The inactivation of the enzyme by its substrate UDP-D-glucose was not affected by the presence of free sugar. 3. In all cases the inactivation observed follows pseudo-first-order kinetics. 4. A comparison of various sugar nucleotides indicates that the hydroxymethyl group at position 6 of the sugar moiety of the natural substrates is important for substrate binding.


1973 ◽  
Vol 131 (2) ◽  
pp. 421-423 ◽  
Author(s):  
M. Spencer ◽  
P. Blackburn ◽  
W. Ferdinand ◽  
G. M. Blackburn

UDP-6-deoxygalactose inhibits the UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli in a competitive manner with respect to the substrate UDP-galactose, giving Ki 1.3×10-3m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained. Possible causes of this behaviour are discussed.


1986 ◽  
Vol 144 (3) ◽  
pp. 150-151 ◽  
Author(s):  
Francis G. Bowling ◽  
David K.B. Fraser ◽  
Alan E. Clague ◽  
Darryl J. Morris ◽  
Alan Hayes

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