Cargando…
The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme
The marine environment is a rich source of antimicrobial compounds with promising pharmaceutical and biotechnological applications. The Pseudoalteromonas genus harbors one of the highest proportions of bacterial species producing antimicrobial molecules. For decades, the presence of proteins with L-...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316408/ https://www.ncbi.nlm.nih.gov/pubmed/30545033 http://dx.doi.org/10.3390/md16120499 |
_version_ | 1783384522876780544 |
---|---|
author | Andreo-Vidal, Andrés Sanchez-Amat, Antonio Campillo-Brocal, Jonatan C. |
author_facet | Andreo-Vidal, Andrés Sanchez-Amat, Antonio Campillo-Brocal, Jonatan C. |
author_sort | Andreo-Vidal, Andrés |
collection | PubMed |
description | The marine environment is a rich source of antimicrobial compounds with promising pharmaceutical and biotechnological applications. The Pseudoalteromonas genus harbors one of the highest proportions of bacterial species producing antimicrobial molecules. For decades, the presence of proteins with L-amino acid oxidase (LAAO) and antimicrobial activity in Pseudoalteromonas luteoviolacea has been known. Here, we present for the first time the identification, cloning, characterization and phylogenetic analysis of Pl-LAAO, the enzyme responsible for both LAAO and antimicrobial activity in P. luteoviolacea strain CPMOR-2. Pl-LAAO is a flavoprotein of a broad substrate range, in which the hydrogen peroxide generated in the LAAO reaction is responsible for the antimicrobial activity. So far, no protein with a sequence similarity to Pl-LAAO has been cloned or characterized, with this being the first report on a flavin adenine dinucleotide (FAD)-containing LAAO with antimicrobial activity from a marine microorganism. Our results revealed that 20.4% of the sequenced Pseudoalteromonas strains (specifically, 66.6% of P. luteoviolacea strains) contain Pl-laao similar genes, which constitutes a well-defined phylogenetic group. In summary, this work provides insights into the biological significance of antimicrobial LAAOs in the Pseudoalteromonas genus and shows an effective approach for the detection of novel LAAOs, whose study may be useful for biotechnological applications. |
format | Online Article Text |
id | pubmed-6316408 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63164082019-01-10 The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme Andreo-Vidal, Andrés Sanchez-Amat, Antonio Campillo-Brocal, Jonatan C. Mar Drugs Article The marine environment is a rich source of antimicrobial compounds with promising pharmaceutical and biotechnological applications. The Pseudoalteromonas genus harbors one of the highest proportions of bacterial species producing antimicrobial molecules. For decades, the presence of proteins with L-amino acid oxidase (LAAO) and antimicrobial activity in Pseudoalteromonas luteoviolacea has been known. Here, we present for the first time the identification, cloning, characterization and phylogenetic analysis of Pl-LAAO, the enzyme responsible for both LAAO and antimicrobial activity in P. luteoviolacea strain CPMOR-2. Pl-LAAO is a flavoprotein of a broad substrate range, in which the hydrogen peroxide generated in the LAAO reaction is responsible for the antimicrobial activity. So far, no protein with a sequence similarity to Pl-LAAO has been cloned or characterized, with this being the first report on a flavin adenine dinucleotide (FAD)-containing LAAO with antimicrobial activity from a marine microorganism. Our results revealed that 20.4% of the sequenced Pseudoalteromonas strains (specifically, 66.6% of P. luteoviolacea strains) contain Pl-laao similar genes, which constitutes a well-defined phylogenetic group. In summary, this work provides insights into the biological significance of antimicrobial LAAOs in the Pseudoalteromonas genus and shows an effective approach for the detection of novel LAAOs, whose study may be useful for biotechnological applications. MDPI 2018-12-12 /pmc/articles/PMC6316408/ /pubmed/30545033 http://dx.doi.org/10.3390/md16120499 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Andreo-Vidal, Andrés Sanchez-Amat, Antonio Campillo-Brocal, Jonatan C. The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title | The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title_full | The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title_fullStr | The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title_full_unstemmed | The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title_short | The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme |
title_sort | pseudoalteromonas luteoviolacea l-amino acid oxidase with antimicrobial activity is a flavoenzyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316408/ https://www.ncbi.nlm.nih.gov/pubmed/30545033 http://dx.doi.org/10.3390/md16120499 |
work_keys_str_mv | AT andreovidalandres thepseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme AT sanchezamatantonio thepseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme AT campillobrocaljonatanc thepseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme AT andreovidalandres pseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme AT sanchezamatantonio pseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme AT campillobrocaljonatanc pseudoalteromonasluteoviolacealaminoacidoxidasewithantimicrobialactivityisaflavoenzyme |