Fluorescence and nucleotide binding properties of Escherichia coli uridine diphosphate galactose 4-epimerase: support for a model for nonstereospecific action

Biochemistry ◽  
1977 ◽  
Vol 16 (2) ◽  
pp. 298-305 ◽  
Author(s):  
Shan S. Wong ◽  
Perry A. Frey
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Binding ◽  
Uridine Diphosphate ◽  
Binding Properties ◽  
Uridine Diphosphate Galactose

scholarly journals The concerted inactivation of Escherichia coli uridine diphosphate galactose 4-epimerase by sugar nucleotide together with a free sugar

1976 ◽  
Vol 155 (2) ◽  
pp. 225-229 ◽  
Author(s):  
P Blackburn ◽  
W Ferdinand
Keyword(s):  
Escherichia Coli ◽  
Free Sugar ◽  
Uridine Diphosphate ◽  
Hydroxymethyl Group ◽  
Free Sugars ◽  
Sugar Nucleotides ◽  
Sugar Nucleotide ◽  
First Order ◽  
First Order Kinetics ◽  
Uridine Diphosphate Galactose

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.

scholarly journals Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase (Short Communication)

1973 ◽  
Vol 131 (2) ◽  
pp. 421-423 ◽  
Author(s):  
M. Spencer ◽  
P. Blackburn ◽  
W. Ferdinand ◽  
G. M. Blackburn
Keyword(s):  
Escherichia Coli ◽  
Short Communication ◽  
Competitive Inhibition ◽  
Uridine Diphosphate ◽  
Uridine Diphosphate Galactose

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.

scholarly journals Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function

2008 ◽  
Vol 11 (11) ◽  
pp. 2551-2560 ◽  
Author(s):  
Cosmin Saveanu ◽  
Simona Miron ◽  
Tudor Borza ◽  
Constantin T. Craescu ◽  
Gilles Labesse ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Unknown Function ◽  
Nucleotide Binding ◽  
Binding Properties
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