sh.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Prospecting Biotechnologically-Relevant Monooxygenases from Cold Sediment Metagenomes: An In Silico Approach
Centro para el Estudio de Sistemas Marinos, CONICET, Puerto Madryn, Argentina.
Centro para el Estudio de Sistemas Marinos, CONICET, Puerto Madryn, Argentina.
Universidad Nacional de Rosario, CONICET, Rosario, Argentina.
Instituto Antártico Argentino, Ciudad Autónoma de Buenos Aires, Argentina / CONICET—Universidad de Buenos Aires, Ciudad Autónoma de Buenos Aires, Argentina.
Show others and affiliations
2017 (English)In: Marine Drugs, ISSN 1660-3397, E-ISSN 1660-3397, Vol. 15, no 4, 114Article in journal (Refereed) Published
Abstract [en]

The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo- selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments.

Place, publisher, year, edition, pages
2017. Vol. 15, no 4, 114
Keyword [en]
Baeyer–Villiger monooxygenases, bacterial cytochrome P450, bioprospecting biocatalysts, molecular modeling, phylogenetic analysis
National Category
Environmental Sciences
Research subject
Environmental Studies
Identifiers
URN: urn:nbn:se:sh:diva-32413DOI: 10.3390/md15040114ISI: 000404228300030PubMedID: 28397770Scopus ID: 2-s2.0-85018661660OAI: oai:DiVA.org:sh-32413DiVA: diva2:1088953
Available from: 2017-04-18 Created: 2017-04-18 Last updated: 2017-07-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopusPMC Full text

Search in DiVA

By author/editor
Jansson, Janet K.Sjöling, Sara
By organisation
Environmental Science
In the same journal
Marine Drugs
Environmental Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 47 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf