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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Campillo‐Brocal, Jonatan C. | - |
dc.contributor.author | Lucas‐Elio, Patricia | - |
dc.contributor.author | Sanchez‐Amat, Antonio | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Genética y Microbiología | es |
dc.date.accessioned | 2024-02-08T11:33:04Z | - |
dc.date.available | 2024-02-08T11:33:04Z | - |
dc.date.issued | 2013 | - |
dc.identifier.citation | Microbiology Open 2013; 2(4): 684–694 | es |
dc.identifier.issn | Electronic: 2045-8827 | - |
dc.identifier.uri | http://hdl.handle.net/10201/138983 | - |
dc.description | ª 2013 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. | es |
dc.description.abstract | A novel enzyme with lysine-epsilon oxidase activity was previously described in the marine bacterium Marinomonas mediterranea. This enzyme differs from other l-amino acid oxidases in not being a flavoprotein but containing a quinone cofactor. It is encoded by an operon with two genes lodA and lodB. The first one codes for the oxidase, while the second one encodes a protein required for the expression of the former. Genome sequencing of M. mediterranea has revealed that it contains two additional operons encoding proteins with sequence similarity to LodA. In this study, it is shown that the product of one of such genes, Marme_1655, encodes a protein with glycine oxidase activity. This activity shows important differences in terms of substrate range and sensitivity to inhibitors to other glycine oxidases previously described which are flavoproteins synthesized by Bacillus. The results presented in this study indicate that the products of the genes with different degrees of similarity to lodA detected in bacterial genomes could constitute a reservoir of different oxidases. | es |
dc.format | application/pdf | es |
dc.format.extent | 11 | es |
dc.language | eng | es |
dc.publisher | WILEY | es |
dc.relation | This work has been supported by grants BIO2010-15226 (Ministerio de Ciencia e Innovacion, Spain) and 11867/PI/09 (Fundacion Seneca, CARM, Spain) Cofinanced by the European Commission, FEDER funds | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Glycine oxidase | es |
dc.subject | Hydrogen peroxide | es |
dc.subject | Marinomonas mediterranea | es |
dc.subject | Quinoprotein | es |
dc.subject.other | CDU::5 - Ciencias puras y naturales::57 - Biología::579 - Microbiología | es |
dc.title | Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity | es |
dc.type | info:eu-repo/semantics/article | es |
dc.identifier.doi | https://doi.org/10.1002/mbo3.107 | - |
Aparece en las colecciones: | Artículos: Genética y Microbiología |
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MicrobiologyOpen - 2013 - Campillo‐Brocal - Identification in Marinomonas mediterranea of a novel quinoprotein with glycine.pdf | 769,04 kB | Adobe PDF | Visualizar/Abrir |
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