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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| Veröffentlicht in: | Planta 2012-07, Vol.236 (1), p.91-100 |
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| description | 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. |
| doi_str_mv | 10.1007/s00425-012-1593-2 |
| format | Article |
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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.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-012-1593-2</identifier><identifier>PMID: 22270561</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>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</subject><ispartof>Planta, 2012-07, Vol.236 (1), p.91-100</ispartof><rights>Springer-Verlag 2012</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-81678166dac79da79e78315973cb8738f43a97a1c4c6b16c0a76a4b13ed0a9993</citedby><cites>FETCH-LOGICAL-c523t-81678166dac79da79e78315973cb8738f43a97a1c4c6b16c0a76a4b13ed0a9993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/43564702$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/43564702$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27923,27924,41487,42556,51318,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26099433$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22270561$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gandía-Herrero, Fernando</creatorcontrib><creatorcontrib>García-Carmona, Francisco</creatorcontrib><title>Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains</title><title>Planta</title><addtitle>Planta</addtitle><addtitle>Planta</addtitle><description>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.</description><subject>Agriculture</subject><subject>Amino acids</subject><subject>Beta vulgaris</subject><subject>Beta vulgaris - enzymology</subject><subject>Beta vulgaris - genetics</subject><subject>Betacyanins</subject><subject>Betalains</subject><subject>Betalains - metabolism</subject><subject>Betaxanthins</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Caryophyllales</subject><subject>Dioxygenases - metabolism</subject><subject>E coli</subject><subject>Ecology</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Forestry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genes, Plant</subject><subject>Life Sciences</subject><subject>Original Article</subject><subject>Oxygenases - isolation & purification</subject><subject>Pigments</subject><subject>Pigments, Biological - biosynthesis</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Sciences</subject><subject>Plants</subject><subject>Plasmids</subject><subject>Recombinant Proteins</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkU2LFDEQhoMo7rj6AzwoDSJ4MJqv7nSO6_gJC-tBz011Oj2boSdZk_Sy46-3xh5XEcRDkoJ66q2qvIQ85uwVZ0y_zowpUVPGBeW1kVTcISuupKCCqfYuWTGGMTOyPiEPct4yhkmt75MTIYRmdcNXpKwvIYEtLvnvUHwMVRyr5Gzc9T5AKNUbV6C6nqcNJJ8r9bKmby8-n1F3UxIMPk4Ur5v9xgXIrkIhf-0qH6py6arex7wPGGWsRNkepSbwIT8k90aYsnt0fE_J1_fvvqw_0vOLD5_WZ-fU1kIW2vJG42kGsNoMoI3TrcRFtbR9q2U7KglGA7fKNj1vLAPdgOq5dAMDY4w8JS8W3asUv80ul27ns3XTBMHFOXdcCM4Vr7Hbf1EmBP6daVpEn_2FbuOcAi7yk-Koxw69-ULZFHNObuyukt9B2iPUHdzrFvc6dK87uNcdhnh6VJ77nRtuK37ZhcDzIwDZwjQmCNbn31zDjFFSIicWLmMqbFz6c8R_d3-yFG1zielWVMm6UZoJ-QMq_boM</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Gandía-Herrero, Fernando</creator><creator>García-Carmona, Francisco</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20120701</creationdate><title>Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains</title><author>Gandía-Herrero, Fernando ; García-Carmona, Francisco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-81678166dac79da79e78315973cb8738f43a97a1c4c6b16c0a76a4b13ed0a9993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Agriculture</topic><topic>Amino acids</topic><topic>Beta vulgaris</topic><topic>Beta vulgaris - enzymology</topic><topic>Beta vulgaris - genetics</topic><topic>Betacyanins</topic><topic>Betalains</topic><topic>Betalains - metabolism</topic><topic>Betaxanthins</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Caryophyllales</topic><topic>Dioxygenases - metabolism</topic><topic>E coli</topic><topic>Ecology</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Forestry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genes, Plant</topic><topic>Life Sciences</topic><topic>Original Article</topic><topic>Oxygenases - isolation & purification</topic><topic>Pigments</topic><topic>Pigments, Biological - biosynthesis</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Sciences</topic><topic>Plants</topic><topic>Plasmids</topic><topic>Recombinant Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gandía-Herrero, Fernando</creatorcontrib><creatorcontrib>García-Carmona, Francisco</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gandía-Herrero, Fernando</au><au>García-Carmona, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains</atitle><jtitle>Planta</jtitle><stitle>Planta</stitle><addtitle>Planta</addtitle><date>2012-07-01</date><risdate>2012</risdate><volume>236</volume><issue>1</issue><spage>91</spage><epage>100</epage><pages>91-100</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>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.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>22270561</pmid><doi>10.1007/s00425-012-1593-2</doi><tpages>10</tpages></addata></record> |
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| 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 |
| title | Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains |
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