Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity

MicrobiologyOpen

Jonatan Cristian Campillo-Brocal¹  Patricia Lucas-Elio¹ 

[1] Department of Genetics and Microbiology, University of Murcia, Murcia, Spain

关键词: Glycine oxidase;    hydrogen peroxide;    Marinomonas mediterranea;    quinoprotein.;   

DOI  :  10.1002/mbo3.107

来源: Wiley

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 The Authors. Microbiology Open published by John Wiley & Sons Ltd.

Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.