First description of betalains biosynthesis in an aquatic organism: characterization of 4,5‐DOPA‐extradiol‐dioxygenase activity in the cyanobacteria Anabaena cylindrica

This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the m...

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Published inMicrobial biotechnology Vol. 13; no. 6; pp. 1948 - 1959
Main Authors Guerrero‐Rubio, María Alejandra, García‐Carmona, Francisco, Gandía‐Herrero, Fernando
Format Journal Article
LanguageEnglish
Published United States John Wiley & Sons, Inc 01.11.2020
John Wiley and Sons Inc
Wiley
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Summary:This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. The discovery of this novel dioxygenase in the phylum cyanobacteria shows that betalains' formation is more diverse than expected. Summary The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them.
Bibliography:Funding information
This work was supported by ‘Ministerio de Ciencia e Innovación’, project AGL2017‐86526‐P (MCI/AEI/FEDER, UE) and by ‘Programa de Ayudas a Grupos de Excelencia de la Región de Murcia, Fundación Séneca, Agencia de Ciencia y Tecnología de la Región de Murcia’ (Project 19893/GERM/15). M.A.G.‐R. holds a contract financed by MEC‐FSE (Spain).
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ISSN:1751-7915
1751-7915
DOI:10.1111/1751-7915.13641