biostudies-literatureUnknown3(2)Rodrigues MJThe Pdx1 enzyme catalyses condensation of two carbohydrates and ammonia to form pyridoxal 5-phosphate (PLP) <i>via</i> 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.RSC chemical biology227-230https://www.ebi.ac.uk/biostudies/studies/S-EPMC8827014biostudies-literatureTrapping and structural characterisation of a covalent intermediate in vitamin B₆ biosynthesis catalysed by the Pdx1 PLP synthase.PMC8827014Rodrigues MJGiri NRoyant ABolton RZhang YEalick SEBegley TEvans GTews IfalseTrapping and structural characterisation of a covalent intermediate in vitamin B₆ biosynthesis catalysed by the Pdx1 PLP synthase.The Pdx1 enzyme catalyses condensation of two carbohydrates and ammonia to form pyridoxal 5-phosphate (PLP) <i>via</i> 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.2022-01-01T00:00:00Z2022 Feb2024-12-04T12:00:57.775Z2024-12-04T12:00:57.775ZS-EPMC88270143536088710.1039/d1cb00160d