Mechanistic studies on the single-turnover yeast thiamin pyrimidine synthase: Characterization of the inactive enzyme was written by Lai, Rung-Yi;Mondal, Anushree;Fedoseyenko, Dmytro;Begley, Tadhg P.. And the article was included in Journal of the American Chemical Society in 2022.Reference of 54-47-7 The following contents are mentioned in the article:
The eukaryotic thiamin pyrimidine synthase, THI5p, has been identified as a suicidal/single-turnover enzyme that catalyzes the conversion of its active site histidine and lysine-bound pyridoxal phosphate (PLP) to the thiamin pyrimidine (HMP-P). Here we identify the histidine and PLP fragments using bottom-up proteomics and LC-MS anal. We also identify the active form of the iron cofactor and quantitate the oxygen requirement of the THI5p reaction. This information is integrated into a mechanistic proposal for this remarkable reaction. This study involved multiple reactions and reactants, such as (4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate (cas: 54-47-7Reference of 54-47-7).
(4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate (cas: 54-47-7) belongs to pyridine derivatives. The pyridine ring occurs in many important compounds, including agrochemicals, pharmaceuticals, and vitamins. Pyridine derivatives are also useful as small-molecule ä¼?helix mimetics that inhibit protein-protein interactions, as well as functionally selective GABA ligands.Reference of 54-47-7