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dc.contributor.authorGandía Herrero, Fernando-
dc.contributor.authorGarcía Carmona, Francisco-
dc.date.accessioned2025-06-25T11:25:59Z-
dc.date.available2025-06-25T11:25:59Z-
dc.date.issued2013-05-12-
dc.identifier.citationAppl Microbiol Biotechnol (2014) 98:1165–1174es
dc.identifier.issnPrint: 0175-7598-
dc.identifier.issnElectronic: 1432-0614-
dc.identifier.urihttp://hdl.handle.net/10201/156641-
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/S00253-013-4961-3es
dc.description.abstractBetalamic 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 spectrometryes
dc.formatapplication/pdfes
dc.format.extent10es
dc.languageenges
dc.publisherSpringer-
dc.relationThis 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.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectBetalaines
dc.subjectBetalamic acides
dc.subjectDioxygenasees
dc.subjectExtradioles
dc.subjectPlant pigmentes
dc.subjectProkaryotices
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísicaes
dc.titleEscherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activityes
dc.typeinfo:eu-repo/semantics/articlees
dc.relation.publisherversionhttps://link.springer.com/article/10.1007/s00253-013-4961-3-
dc.identifier.doihttps://doi.org/10.1007/S00253-013-4961-3-
dc.contributor.departmentBioquímica y Biología Molecular "A"es
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