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

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 I(333) intermediate characterised here using structural, UV-vis absorption spectroscopy and mass spectrometry analyses rationalises...

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Autores principales: Rodrigues, Matthew J., Giri, Nitai, Royant, Antoine, Zhang, Yang, Bolton, Rachel, Evans, Gwyndaf, Ealick, Steve E., Begley, Tadhg, Tews, Ivo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8827014/
https://www.ncbi.nlm.nih.gov/pubmed/35360887
http://dx.doi.org/10.1039/d1cb00160d
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author Rodrigues, Matthew J.
Giri, Nitai
Royant, Antoine
Zhang, Yang
Bolton, Rachel
Evans, Gwyndaf
Ealick, Steve E.
Begley, Tadhg
Tews, Ivo
author_facet Rodrigues, Matthew J.
Giri, Nitai
Royant, Antoine
Zhang, Yang
Bolton, Rachel
Evans, Gwyndaf
Ealick, Steve E.
Begley, Tadhg
Tews, Ivo
author_sort Rodrigues, Matthew J.
collection PubMed
description 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 I(333) 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.
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spelling pubmed-88270142022-03-30 Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase Rodrigues, Matthew J. Giri, Nitai Royant, Antoine Zhang, Yang Bolton, Rachel Evans, Gwyndaf Ealick, Steve E. Begley, Tadhg Tews, Ivo RSC Chem Biol Chemistry 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 I(333) 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 2021-10-25 /pmc/articles/PMC8827014/ /pubmed/35360887 http://dx.doi.org/10.1039/d1cb00160d Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Rodrigues, Matthew J.
Giri, Nitai
Royant, Antoine
Zhang, Yang
Bolton, Rachel
Evans, Gwyndaf
Ealick, Steve E.
Begley, Tadhg
Tews, Ivo
Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title_full Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title_fullStr Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title_full_unstemmed Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title_short Trapping and structural characterisation of a covalent intermediate in vitamin B(6) biosynthesis catalysed by the Pdx1 PLP synthase
title_sort trapping and structural characterisation of a covalent intermediate in vitamin b(6) biosynthesis catalysed by the pdx1 plp synthase
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8827014/
https://www.ncbi.nlm.nih.gov/pubmed/35360887
http://dx.doi.org/10.1039/d1cb00160d
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