English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/99618
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
DC FieldValueLanguage
dc.contributor.authorIturbe-Ormaetxe, Iñaki-
dc.contributor.authorHeras, Begoña-
dc.contributor.authorMatamoros Galindo, Manuel Ángel-
dc.contributor.authorRamos Escribano, Javier-
dc.contributor.authorMorán, José F.-
dc.contributor.authorBecana Ausejo, Manuel-
dc.date.accessioned2014-07-08T10:45:10Z-
dc.date.available2014-07-08T10:45:10Z-
dc.date.issued2002-05-
dc.identifierdoi: 10.1034/j.1399-3054.2002.1150107.x-
dc.identifierissn: 0031-9317-
dc.identifier.citationPhysiologia Plantarum 115 (1): 69-73 (2002)-
dc.identifier.urihttp://hdl.handle.net/10261/99618-
dc.description16 Pags.- 2 Figs. The definitive version, with all 3 Figs., is available at: http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1399-3054-
dc.description.abstractThe thiol tripeptide glutathione (GSH; γGlu-Cys-Gly) is very abundant in legume nodules where it performs multiple functions that are critical for optimal nitrogen fixation. Some legume nodules contain another tripeptide, homoglutathione (hGSH; γGlu-Cys-βAla), in addition to or instead of GSH. We have isolated from a pea (Pisum sativum L.) nodule library a cDNA, GSHS2, that is expressed in nodules but not in leaves. This cDNA was overexpressed in insect cells and its protein product was identified as a highly active and specific hGSH synthetase. The enzyme, the first of this type to be completely purified, is predicted to be a homodimeric cytosolic protein. It shows a specific activity of 3400 nmol hGSH min-1 mg-1 protein with a standard substrate concentration (5 mM β-alanine) and Km values of 1.9 mM for β-alanine and 104 mM for glycine. The specificity constant (Vmax/Km) shows that the pure enzyme is 57.3-fold more specific for β-alanine than for glycine. Southern blot analysis revealed that the gene is present as a single copy in the pea genome and that there are homologous genes in other legumes. We conclude that the synthesis of hGSH in pea nodules is catalysed by a specific hGSH synthetase and not by a GSH synthetase with broad substrate specificity.-
dc.description.sponsorshipM.A.M. was the recipient of a predoctoral fellowship from the Basque Government (Spain). This work was supported by grant no. 2FD97-1101 from the Comisión Interministerial de Ciencia y Tecnología and the European Union and by grant no. PB98-0522 from the Dirección General de Investigación Científica (Spain).-
dc.publisherBlackwell Publishing-
dc.relation.isversionofPostprint-
dc.rightsopenAccess-
dc.titleCloning and functional characterization of a homoglutathione synthetase from pea nodules-
dc.typeartículo-
dc.identifier.doi10.1034/j.1399-3054.2002.1150107.x-
dc.relation.publisherversionhttp://dx.doi.org/10.1034/j.1399-3054.2002.1150107.x-
dc.date.updated2014-07-08T10:45:10Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
Appears in Collections:(EEAD) Artículos
Files in This Item:
File Description SizeFormat 
BecanaM_PhysiolPlant_a_2002.pdf173,53 kBAdobe PDFThumbnail
View/Open
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.