Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains

Betalains are water-soluble pigments with high antiradical capacity which bestow bright colors to flowers, fruits and other parts of most plants of the order Caryophyllales. The formation of the structural unit of all betalains, betalamic acid from the precursor amino acid 4,5-dihydroxyphenylalanine...

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Bibliographic Details
Published in:Planta 2012-07, Vol.236 (1), p.91-100
Main Authors: Gandía-Herrero, Fernando, García-Carmona, Francisco
Format: Article
Language:English
Subjects:
Agriculture
Amino acids
Beta vulgaris
Beta vulgaris - enzymology
Beta vulgaris - genetics
Betacyanins
Betalains
Betalains - metabolism
Betaxanthins
Biological and medical sciences
Biomedical and Life Sciences
Biosynthesis
Caryophyllales
Dioxygenases - metabolism
E coli
Ecology
Enzymes
Escherichia coli
Forestry
Fundamental and applied biological sciences. Psychology
Gels
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Genes, Plant
Life Sciences
Original Article
Oxygenases - isolation & purification
Pigments
Pigments, Biological - biosynthesis
Plant Proteins - metabolism
Plant Sciences
Plants
Plasmids
Recombinant Proteins
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Summary:Betalains are water-soluble pigments with high antiradical capacity which bestow bright colors to flowers, fruits and other parts of most plants of the order Caryophyllales. The formation of the structural unit of all betalains, betalamic acid from the precursor amino acid 4,5-dihydroxyphenylalanine is catalyzed by the enzyme 4,5-DOPAextradiol-dioxygenase followed by intramolecular cyclization of the 4,5-secodopa intermediate. This paper describes the purification and the molecular and functional characterization of an active 4,5-DOPA-extradiol-dioxygenase from the best-known source of betalains—Beta vulgaris —after heterologous expression in Escherichia coli. The enzyme is a monomeric protein with a molecular mass of 32 kDa characterized by chromatography, electrophoresis and MALDITOF analysis. Enzyme kinetic properties are characterized in the production of betalamic acid, the structural, chromophoric and bioactive unit of plant pigment betalains.
ISSN:0032-0935
1432-2048
DOI:10.1007/s00425-012-1593-2