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 in | Microbial biotechnology Vol. 13; no. 6; pp. 1948 - 1959 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
John Wiley & Sons, Inc
01.11.2020
John Wiley and Sons Inc Wiley |
Subjects | |
Online Access | Get full text |
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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. |
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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). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1751-7915 1751-7915 |
DOI: | 10.1111/1751-7915.13641 |