Uridine Kinase: Altered Enzyme with Decreased Affinities for Uridine and CTP

1998 ◽  
Vol 359 (1) ◽  
pp. 63-68 ◽  
Author(s):  
Patricia A. Ropp ◽  
Thomas W. Traut
Keyword(s):  
Uridine Kinase

Donor activity of 5'-O-phosphonylmethyl analogues of ATP and GTP in the phosphorylation of uridine catalyzed by uridine kinase from mouse leukemic cells

1983 ◽  
Vol 48 (6) ◽  
pp. 1783-1787 ◽  
Author(s):  
Jiří Veselý ◽  
Ivan Rosenberg ◽  
Antonín Holý
Keyword(s):  
Leukemic Cells ◽  
Kinase Reaction ◽  
Uridine Kinase ◽  
Donor Activity

The phosphonate analogues of ATP and GTP can function as phosphate donors in uridine kinase reaction. The Km constants for ATP and its analogue ATPc (I) are identical, the Vmax value for ATP is five times higher than that for ATPc. Also the Vmax constants with respect to uridine follow the same pattern (250 nmol for ATP, 35.7 nmol for ATPc). The optimum Mg2+ concentration for the phosphonate is 3 times higher compared with ATP.

Inhibition by CTP and UTP analogues of uridine kinase from mouse leukemic cells

1982 ◽  
Vol 47 (12) ◽  
pp. 3464-3469 ◽  
Author(s):  
Jiří Veselý ◽  
Ivan Rosenberg ◽  
Antonín Holý
Keyword(s):  
Leukemic Cells ◽  
The Novel ◽  
Uridine Kinase ◽  
Phosphate Donor

The new phosphonate analogues of CTP and UTP (CTPc and UTPc) inhibit the phosphorylation of uridine catalysed by uridine kinase in the presence of ATP and Mg2+-ions. The inhibition is competitive with respect to phosphate donor, and non-competitive with respect to phosphate acceptor. With respect to uridine the Ki constants for CTPc and UTPc are 7.5 . 10-5 mol l-1 and 1.0 . 10-4 mol l-1, respectively. With respect to ATP the Ki value for CTPc (3.6 . 10-6 mol l-1) is 3x lower than that for CTP. The novel analogues could be useful for further study of uridine kinase.

Uridine kinase

1997 ◽  
pp. 847-852
Author(s):  
Dietmar Schomburg ◽  
Dörte Stephan
Keyword(s):  
Uridine Kinase

The Partial Purification and Properties of Uridine Kinase from Ehrlich Ascites Tumor Cells

1973 ◽  
Vol 51 (4) ◽  
pp. 379-389 ◽  
Author(s):  
Gerald Krystal ◽  
Peter G. Scholefield
Keyword(s):  
Molecular Weight ◽  
Tumor Cells ◽  
Weight Fraction ◽  
Ehrlich Ascites Tumor ◽  
Partial Purification ◽  
Heat Inactivation ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Uridine Kinase ◽  
Ehrlich Ascites

In the partial purification of uridine kinase (ATP:uridine 5′-phosphotransferase, EC 2.7.1.48) from Ehrlich ascites tumor cells, two active fractions were obtained by chromatography on Sepharose 6B. Their molecular weights, as determined by a gel filtration and sucrose density centrifugation, were approximately 120 000 and 30 000. The larger molecular weight species was less stable on incubation at 60° and slightly less sensitive to CTP inhibition than the lower molecular weight fraction. Both fractions were stabilized against heat inactivation by ATP and CTP.The two fractions displayed similar apparent Km values for uridine and ATP, similar specificities for substrates and inhibitors, and similar divalent cation requirements.In the partial purification of uridine kinase from mouse intestine, only the larger molecular weight fraction was obtained by chromatography on Sepharose 6B.In addition, some preliminary evidence for a monomer–polymer relationship between the two molecular weight species is presented.

Effects of age of culture and vaccinia infection on uridine kinase activity of L-cells

1964 ◽  
Vol 34 (2) ◽  
pp. 257-265 ◽  
Author(s):  
S. Kit ◽  
Y. Valladares ◽  
D.R. Dubbs
Keyword(s):  
Kinase Activity ◽  
Uridine Kinase ◽  
L Cells
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