Escherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activity

Gandía Herrero, Fernando; García Carmona, Francisco

Publication:
Escherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activity

dc.contributor.author	Gandía Herrero, Fernando
dc.contributor.author	García Carmona, Francisco
dc.contributor.department	Bioquímica y Biología Molecular "A"	es
dc.date.accessioned	2025-06-25T11:25:59Z
dc.date.available	2025-06-25T11:25:59Z
dc.date.issued	2013-05-12
dc.description	©2013, Springer-Verlag Berlin Heidelberg. This manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by/4.0/. This document is the Published version of a Published Work that appeared in final form in Applied Microbiology and Biotechnology. To access the final edited and published work see 10.1007/S00253-013-4961-3	es
dc.description.abstract	Betalamic acid is the structural unit of all the natural pigments betalains. These are nitrogen-containing water soluble compounds with high colorant and bioactive properties, characteristic of plants of the order Caryophyllales. The formation of betalamic acid from the precursor amino acid 3,4-dihydroxy-L-phenylalanine (L-DOPA) by the enzyme 4,5- DOPA-extradiol-dioxygenase was supposed to be restricted to plants of this order and two fungal species. Here, the first case of betalamic acid formation by an enzyme other than eukaryotes is reported with a homolog enzyme from Escherichia coli. The protein YgiD has been cloned, expressed, and purified to carry out its molecular and functional characterization. The enzyme was obtained as a monomeric active protein with a molecular mass of 32 kDa characterized by chromatography, electrophoresis, and MALDI-TOF analysis. Enzyme kinetic properties are characterized in the transformation of the relevant substrate L-DOPA. Reaction was analyzed spectrophotometrically and by HPLC-DAD, electrospray ionization mass spectrometry, and time-of-flight mass spectrometry	es
dc.format	application/pdf	es
dc.format.extent	10	es
dc.identifier.citation	Appl Microbiol Biotechnol (2014) 98:1165–1174
dc.identifier.doi	https://doi.org/10.1007/S00253-013-4961-3
dc.identifier.issn	Print: 0175-7598
dc.identifier.issn	Electronic: 1432-0614
dc.identifier.uri	http://hdl.handle.net/10201/156641
dc.language	eng	es
dc.publisher	Springer
dc.relation	This work was supported by the Ministerio de Ciencia e Innovación (MICINN, FEDER, Spain) (Project AGL2011-25023) and by Programa de Ayudas a Grupos de Excelencia de la Región de Murcia, of the Fundación Séneca, Agencia de Ciencia y Tecnología de la Región de Murcia (Plan Regional de Ciencia y Tecnología 2007/2010). F. Gandía-Herrero holds a contract with the “Programa Ramón y Cajal” (MICINN, FEDER, Spain). The authors are grateful to Dr. Alejandro Torrecillas and to Dr. José Rodriguez (SAI, University of Murcia) for skillful technical assistance in MALDI-TOF and ESI-MS experiments, respectively. Financiadores Fundación Séneca Spain Ministerio de Ciencia e Innovación Spain European Regional Development Fund European Union AGL2011-25023.	es
dc.relation.publisherversion	https://link.springer.com/article/10.1007/s00253-013-4961-3
dc.rights	info:eu-repo/semantics/openAccess	es
dc.rights	Atribución 4.0 Internacional	*
dc.rights.uri	http://creativecommons.org/licenses/by/4.0/	*
dc.subject	Betalain	es
dc.subject	Betalamic acid	es
dc.subject	Dioxygenase	es
dc.subject	Extradiol	es
dc.subject	Plant pigment	es
dc.subject	Prokaryotic	es
dc.subject.other	CDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísica	es
dc.title	Escherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activity	es
dc.type	info:eu-repo/semantics/article	es
dspace.entity.type	Publication	es
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