Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/81788
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Uncovering the Lactobacillus plantarum WCFS1 gallate decarboxylase involved in tannin degradation |
Autor: | Jiménez, Natalia CSIC; Curiel, José Antonio CSIC ORCID ; Reverón, Inés CSIC; Rivas, Blanca de las CSIC ORCID; Muñoz, Rosario CSIC ORCID | Fecha de publicación: | jul-2013 | Editor: | American Society for Microbiology | Citación: | Applied and Environmental Microbiology 79(14): 4253-4263 (2013) | Resumen: | Lactobacillus plantarum is a lactic acid bacterium able to degrade tannins by the subsequent action of tannase and gallate decarboxylase enzymes. the gene encoding tannase had previously been identified, whereas the gene encoding gallate decarboxylase is unknown. sodium dodecyl sulfate-polyacrylamide gel electrophoresis (sds-page) of gallic-acid induced l. plantarum extracts showed a 54-kda protein which was absent in the uninduced cells. this protein was identified as lp_2945, putatively annotated ubid. homology searches identified ubid-like genes located within three-gene operons which encoded the three subunits of nonoxidative aromatic acid decarboxylases. l. plantarum is the only bacterium in which the lpdc (lp_2945) gene and the lpdb and lpdd (lp_0271 and lp_0272) genes are separated in the chromosome. combination of extracts from recombinant escherichia coli cells expressing the lpdb, lpdc, and lpdc genes demonstrated that lpdc is the only protein required to yield gallate decarboxylase activity. however, the disruption of these genes in l. plantarum revealed that the lpdb and lpdc gene products are essential for gallate decarboxylase activity. similar to l. plantarum tannase, which exhibited activity only in esters derived from gallic and protocatechuic acids, purified his6-lpdc protein from e. coli showed decarboxylase activity against gallic and protocatechuic acids. in contrast to the tannase activity, gallate decarboxylase activity is widely present among lactic acid bacteria. this study constitutes the first genetic characterization of a gallate decarboxylase enzyme and provides new insights into the role of the different subunits of bacterial nonoxidative aromatic acid decarboxylases. © 2013, American Society for Microbiology. | Versión del editor: | http://dx.doi.org/10.1128/AEM.00840-13 | URI: | http://hdl.handle.net/10261/81788 | DOI: | 10.1128/AEM.00840-13 | Identificadores: | issn: 0099-2240 |
Aparece en las colecciones: | (ICTAN) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
WCFS1_gallate_decarboxylase_Jimenez.pdf | 1,13 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
35
checked on 26-abr-2024
SCOPUSTM
Citations
72
checked on 10-may-2024
WEB OF SCIENCETM
Citations
66
checked on 24-feb-2024
Page view(s)
358
checked on 13-may-2024
Download(s)
374
checked on 13-may-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.