Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/186025
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Cold-induced aldimine bond cleavage by Tris in: Bacillus subtilis alanine racemase |
Autor: | Bernardo-García, Noelia CSIC; Sánchez-Murcia, Pedro A. CSIC ORCID; Espaillat, Akbar; Martínez-Caballero, Siseth ; Cava, Felipe CSIC ORCID; Hermoso, Juan A. CSIC ORCID; Gago, Federico CSIC ORCID | Fecha de publicación: | 2019 | Editor: | Royal Society of Chemistry (UK) | Citación: | Organic and Biomolecular Chemistry 17: 4350-4358 (2019) | Resumen: | Pyridoxal 5′-phosphate (PLP) is a versatile cofactor involved in a large variety of enzymatic processes. Most of PLP-catalysed reactions, such as those of alanine racemases (AlaRs), present a common resting state in which the PLP is covalently bound to an active-site lysine to form an internal aldimine. The crystal structure of BsAlaR grown in the presence of Tris lacks this covalent linkage and the PLP cofactor appears deformylated. However, loss of activity in a Tris buffer only occurred after the solution was frozen prior to carrying out the enzymatic assay. This evidence strongly suggests that Tris can access the active site at subzero temperatures and behave as an alternate racemase substrate leading to mechanism-based enzyme inactivation, a hypothesis that is supported by additional X-ray structures and theoretical results from QM/MM calculations. Taken together, our findings highlight a possibly underappreciated role for a common buffer component widely used in biochemical and biophysical experiments. | Versión del editor: | http://dx.doi.org/10.1039/c9ob00223e | URI: | http://hdl.handle.net/10261/186025 | DOI: | 10.1039/c9ob00223e | Identificadores: | doi: 10.1039/c9ob00223e issn: 1477-0520 e-issn: 1477-0539 |
Aparece en las colecciones: | (IQM) Artículos (IQF) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
2
checked on 11-abr-2024
WEB OF SCIENCETM
Citations
2
checked on 28-feb-2024
Page view(s)
239
checked on 23-abr-2024
Download(s)
29
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.