Purification and properties of mouse thymus thymidylate synthase. Comparison of the enzyme from mammalian normal and tumour tissues.
Mouse thymus thymidylate synthase has been purified to apparent electrophoretic homogeneity and compared with the enzyme from mouse tumour L1210 and Ehrlich ascites carcinoma cells. The enzyme is a dimer composed of 35,000 mol. wt monomers. Mouse thymus and tumour enzymes exhibit allosteric properties reflected by cooperative binding of both dUMP and 5-fluoro-dUMP. Activation energy for the reaction, catalyzed by thymidylate synthase from mouse tumour but not from mouse thymus, lowers at temperatures above 34 degrees C, reflecting a change of rate-limiting step in dTMP formation. MgATP at millimolar concentrations inhibits mouse thymus enzyme.
Rode
W
W
Cieśla
J
J
Zieliński
Z
Z
Kedzierska
B
B
D000494:Allosteric Regulation; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D004789:Enzyme Activation; D007700:Kinetics; D007939:Leukemia L1210 / Q000201:enzymology*; D046911:Macromolecular Substances; D051379:Mice; D008970:Molecular Weight; D013816:Thermodynamics; D013940:Thymidylate Synthase / Q000302:isolation & purification / Q000378:metabolism*; D013950:Thymus Gland / Q000201:enzymology*
D046911:Macromolecular Substances; D013940:Thymidylate Synthase