Trapping and structural characterization of a covalent intermediate in vitamin B6 biosynthesis catalysed by the Pdx1 PLP synthase was written by Rodrigues, Matthew J.;Giri, Nitai;Royant, Antoine;Zhang, Yang;Bolton, Rachel;Evans, Gwyndaf;Ealick, Steve E.;Begley, Tadhg;Tews, Ivo. And the article was included in RSC Chemical Biology in 2022.Safety of (4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate The following contents are mentioned in the article:
The Pdx1 enzyme catalyzes condensation of two carbohydrates and ammonia to form pyridoxal 5-phosphate (PLP) via an imine relay mechanism of carbonyl intermediates. The I333 intermediate characterised here using structural, UV-vis absorption spectroscopy and mass spectrometry analyses rationalises stereoselective deprotonation and subsequent substrate assisted phosphate elimination, central to PLP biosynthesis. This study involved multiple reactions and reactants, such as (4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate (cas: 54-47-7Safety of (4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate).
(4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate (cas: 54-47-7) belongs to pyridine derivatives. The ring atoms in the pyridine molecule are sp2-hybridized. The nitrogen is involved in the π-bonding aromatic system using its unhybridized p orbital. The lone pair is in an sp2 orbital, projecting outward from the ring in the same plane as the σ bonds. Pyridine derivatives are also useful as small-molecule α-helix mimetics that inhibit protein-protein interactions, as well as functionally selective GABA ligands.Safety of (4-Formyl-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate