Publication: Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity
Loading...
Date
2013
Authors
Campillo‐Brocal, Jonatan C. ; Lucas‐Elio, Patricia ; Sanchez‐Amat, Antonio
item.page.secondaryauthor
item.page.director
Publisher
WILEY
publication.page.editor
publication.page.department
DOI
https://doi.org/10.1002/mbo3.107
item.page.type
info:eu-repo/semantics/article
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.
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.
publication.page.subject
Citation
Microbiology Open 2013 2(4): 684–694
item.page.embargo
Collections
Ir a Estadísticas
Este ítem está sujeto a una licencia Creative Commons. http://creativecommons.org/licenses/by-nc-nd/4.0/