Trapping and structural characterisation of a covalent intermediate in vitamin B 6 biosynthesis catalysed by the Pdx1 PLP synthase - Archive ouverte HAL Access content directly
Journal Articles RSC Chemical Biology Year : 2022

Trapping and structural characterisation of a covalent intermediate in vitamin B 6 biosynthesis catalysed by the Pdx1 PLP synthase

Abstract

The Pdx1 enzyme catalyses 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.
Fichier principal
Vignette du fichier
Rodrigues_RSCChemBiol_2021_Pdx1.3_I333_formatted-online.pdf (2.29 Mo) Télécharger le fichier
Origin : Publisher files allowed on an open archive

Dates and versions

hal-03411231 , version 1 (02-11-2021)

Licence

Attribution - NonCommercial - CC BY 4.0

Identifiers

Cite

Matthew J Rodrigues, Nitai Giri, Antoine Royant, Yang Zhang, Rachel Bolton, et al.. Trapping and structural characterisation of a covalent intermediate in vitamin B 6 biosynthesis catalysed by the Pdx1 PLP synthase. RSC Chemical Biology, 2022, 3 (2), pp.227-230. ⟨10.1039/D1CB00160D⟩. ⟨hal-03411231⟩
37 View
18 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More