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<< < Results 51 - 57 of 57
EC Number Inhibitors Commentary Structure
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1RNAi transketolase-like-1 gene is significantly downregulated in human colon cancer cell line cells transfected with small interfering RNA transketolase-like-1 constructs compared with cells transfected with control vector and cells without transfection. Anti-transketolase-like-1 small interfering RNA construct significantly decreases the level of transketolase in the transfected human colon cancer cell line cells, arrests them in G0/G1 phase and substantially inhibits cell proliferation Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1RNAi inhibits expression of TKTL1, whereas total transketolase activity is dramatically downregulated and proliferation of cancer cells is significantly inhibited in CNE cells Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sulfate - Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1thiamine thiazolone retains thiamine pyrophosphokinase activity, is a significantly better binder to transketolase than thiamine Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1thiamine thiazolone diphosphate is a significantly better binder to transketolase than thiamine Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1Urea denaturation of holo-transketolase by urea displays at least three transitions, where only the final equilibrium denaturation transition is the same for both apo-transketolase and holo-transketolase. Enzyme is deactivated initially by changes in structure associated with the cofactors, but this event does not release the cofactor from the enzyme. Holo-transketolase does not denature to apo-transketolase at 2 M urea. Complete dissociation of cofactors from holo-transketolase at 3.8 M urea without formation of the compact form of apo-transketolase (intermediate form). Holo-transketolase and apo-transketolase at 7.2 M urea both show a common denatured form Go to the Ligand Summary Page
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1ZINC12007063 i.e. 2-[(2,2-dimethyl-3H-benzofuran-7-yl)oxy]-N-[2-(4-ethyl]-6-oxo-1H-pyrimidin-2-yl)-5-(2-furyl)pyrazol-3 Go to the Ligand Summary Page
<< < Results 51 - 57 of 57