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Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase
Flavonol synthase was classified as a 2-oxoglutarate-dependent dioxygenase converting natural (2 R,3 R)-dihydroflavonols, i.e. dihydrokaempferol, to the corresponding flavonols (kaempferol). Flavonol synthase from Citrus unshiu (Satsuma mandarin), expressed in Escherichia coli and purified to homoge...
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| Published in: | Phytochemistry (Oxford) 2003-02, Vol.62 (3), p.287-292 |
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| Main Authors: | , , , , |
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| cites | cdi_FETCH-LOGICAL-c540t-ca4f380ae4306dbabbaa4ace39382458210eb0117b5609eb17b6affed14211f13 |
| container_end_page | 292 |
| container_issue | 3 |
| container_start_page | 287 |
| container_title | Phytochemistry (Oxford) |
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| creator | Lukačin, Richard Wellmann, Frank Britsch, Lothar Martens, Stefan Matern, Ulrich |
| description | Flavonol synthase was classified as a 2-oxoglutarate-dependent dioxygenase converting natural (2
R,3
R)-dihydroflavonols, i.e. dihydrokaempferol, to the corresponding flavonols (kaempferol). Flavonol synthase from
Citrus unshiu (Satsuma mandarin), expressed in
Escherichia coli and purified to homogeneity, was shown to accept also (2
S)-naringenin as a substrate, producing kaempferol in high yield and assigning sequential flavanone 3β-hydroxylase and flavonol synthase activities to the enzyme. In contrast, dihydrokaempferol was identified as the predominant product from assays performed with the unnatural (2
R)-naringenin as substrate. The product which was not converted any further on repeated incubations was identified by
1H NMR and CD spectroscopies as (−)-
trans-dihydrokaempferol. The data demonstrate that
Citrus flavonol synthase encompasses an additional non-specific activity
trans-hydroxylating the flavanones (2
S)-naringenin as well as the unnatural (2
R)-naringenin at C-3.
The recombinant flavonol sythase also catalyzes the 3-hydroxylation of (±) naringenin. |
| doi_str_mv | 10.1016/S0031-9422(02)00567-8 |
| format | article |
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R,3
R)-dihydroflavonols, i.e. dihydrokaempferol, to the corresponding flavonols (kaempferol). Flavonol synthase from
Citrus unshiu (Satsuma mandarin), expressed in
Escherichia coli and purified to homogeneity, was shown to accept also (2
S)-naringenin as a substrate, producing kaempferol in high yield and assigning sequential flavanone 3β-hydroxylase and flavonol synthase activities to the enzyme. In contrast, dihydrokaempferol was identified as the predominant product from assays performed with the unnatural (2
R)-naringenin as substrate. The product which was not converted any further on repeated incubations was identified by
1H NMR and CD spectroscopies as (−)-
trans-dihydrokaempferol. The data demonstrate that
Citrus flavonol synthase encompasses an additional non-specific activity
trans-hydroxylating the flavanones (2
S)-naringenin as well as the unnatural (2
R)-naringenin at C-3.
The recombinant flavonol sythase also catalyzes the 3-hydroxylation of (±) naringenin.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/S0031-9422(02)00567-8</identifier><identifier>PMID: 12620339</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Bifunctional dioxygenase ; Biological and medical sciences ; Chromatography, Thin Layer ; Circular Dichroism ; Citrus ; Citrus - enzymology ; Citrus unshiu ; Dihydroflavonol hydroxylase ; Escherichia coli ; Escherichia coli - metabolism ; Flavanones ; Flavonoid biosynthesis ; Flavonoids - biosynthesis ; Flavonoids - chemistry ; Flavonoids - metabolism ; Flavonol synthase ; Fundamental and applied biological sciences. Psychology ; Kaempferols ; Metabolism ; Metabolism. Physicochemical requirements ; Mixed Function Oxygenases - metabolism ; Oxidoreductases - metabolism ; Oxygenases - metabolism ; Plant physiology and development ; Plant Proteins ; Quercetin - analogs & derivatives ; Quercetin - biosynthesis ; Rutaceae ; Stereoisomerism</subject><ispartof>Phytochemistry (Oxford), 2003-02, Vol.62 (3), p.287-292</ispartof><rights>2003 Elsevier Science Ltd</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-ca4f380ae4306dbabbaa4ace39382458210eb0117b5609eb17b6affed14211f13</citedby><cites>FETCH-LOGICAL-c540t-ca4f380ae4306dbabbaa4ace39382458210eb0117b5609eb17b6affed14211f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14478750$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12620339$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lukačin, Richard</creatorcontrib><creatorcontrib>Wellmann, Frank</creatorcontrib><creatorcontrib>Britsch, Lothar</creatorcontrib><creatorcontrib>Martens, Stefan</creatorcontrib><creatorcontrib>Matern, Ulrich</creatorcontrib><title>Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase</title><title>Phytochemistry (Oxford)</title><addtitle>Phytochemistry</addtitle><description>Flavonol synthase was classified as a 2-oxoglutarate-dependent dioxygenase converting natural (2
R,3
R)-dihydroflavonols, i.e. dihydrokaempferol, to the corresponding flavonols (kaempferol). Flavonol synthase from
Citrus unshiu (Satsuma mandarin), expressed in
Escherichia coli and purified to homogeneity, was shown to accept also (2
S)-naringenin as a substrate, producing kaempferol in high yield and assigning sequential flavanone 3β-hydroxylase and flavonol synthase activities to the enzyme. In contrast, dihydrokaempferol was identified as the predominant product from assays performed with the unnatural (2
R)-naringenin as substrate. The product which was not converted any further on repeated incubations was identified by
1H NMR and CD spectroscopies as (−)-
trans-dihydrokaempferol. The data demonstrate that
Citrus flavonol synthase encompasses an additional non-specific activity
trans-hydroxylating the flavanones (2
S)-naringenin as well as the unnatural (2
R)-naringenin at C-3.
The recombinant flavonol sythase also catalyzes the 3-hydroxylation of (±) naringenin.</description><subject>Bifunctional dioxygenase</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Thin Layer</subject><subject>Circular Dichroism</subject><subject>Citrus</subject><subject>Citrus - enzymology</subject><subject>Citrus unshiu</subject><subject>Dihydroflavonol hydroxylase</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Flavanones</subject><subject>Flavonoid biosynthesis</subject><subject>Flavonoids - biosynthesis</subject><subject>Flavonoids - chemistry</subject><subject>Flavonoids - metabolism</subject><subject>Flavonol synthase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kaempferols</subject><subject>Metabolism</subject><subject>Metabolism. Physicochemical requirements</subject><subject>Mixed Function Oxygenases - metabolism</subject><subject>Oxidoreductases - metabolism</subject><subject>Oxygenases - metabolism</subject><subject>Plant physiology and development</subject><subject>Plant Proteins</subject><subject>Quercetin - analogs & derivatives</subject><subject>Quercetin - biosynthesis</subject><subject>Rutaceae</subject><subject>Stereoisomerism</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqF0EFvFCEUwHHSaNq19iPUzMVGD6OPgYGZU1M3Vk2aeFDP5A3zsDSz0MJM4357WXdjj01I4PB7QP6MnXP4wIGrjz8ABK972TTvoHkP0Cpdd0dsxTstaqEBXrDVf3LCXuV8B0W1Sh2zE96oBoToV-zT9YSPMcSpytsw32KmyqW4qdZ-TkuulpBv_VL5XGE1eLcEO_sYcKpGH_9sf1MoA6_ZS4dTprPDfsp-XX_-uf5a33z_8m19dVPbVsJcW5ROdIAkBahxwGFAlGhJ9KJrZNs1HGgAzvXQKuhpKAeFztHIZcO54-KUXezvvU_xYaE8m43PlqYJA8UlGy1A973Wz0Lea9UppQps99CmmHMiZ-6T32DaGg5mV9n8q2x2CQ2UtatsujL35vDAMmxofJo6ZC3g7QFgtji5hMH6_OSk1J1uobjLvaPS7dFTMtl6CpZGn8jOZoz-ma_8BUYSmQA</recordid><startdate>20030201</startdate><enddate>20030201</enddate><creator>Lukačin, Richard</creator><creator>Wellmann, Frank</creator><creator>Britsch, Lothar</creator><creator>Martens, Stefan</creator><creator>Matern, Ulrich</creator><general>Elsevier Ltd</general><general>Elsevier</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20030201</creationdate><title>Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase</title><author>Lukačin, Richard ; Wellmann, Frank ; Britsch, Lothar ; Martens, Stefan ; Matern, Ulrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-ca4f380ae4306dbabbaa4ace39382458210eb0117b5609eb17b6affed14211f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Bifunctional dioxygenase</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Thin Layer</topic><topic>Circular Dichroism</topic><topic>Citrus</topic><topic>Citrus - enzymology</topic><topic>Citrus unshiu</topic><topic>Dihydroflavonol hydroxylase</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Flavanones</topic><topic>Flavonoid biosynthesis</topic><topic>Flavonoids - biosynthesis</topic><topic>Flavonoids - chemistry</topic><topic>Flavonoids - metabolism</topic><topic>Flavonol synthase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kaempferols</topic><topic>Metabolism</topic><topic>Metabolism. Physicochemical requirements</topic><topic>Mixed Function Oxygenases - metabolism</topic><topic>Oxidoreductases - metabolism</topic><topic>Oxygenases - metabolism</topic><topic>Plant physiology and development</topic><topic>Plant Proteins</topic><topic>Quercetin - analogs & derivatives</topic><topic>Quercetin - biosynthesis</topic><topic>Rutaceae</topic><topic>Stereoisomerism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lukačin, Richard</creatorcontrib><creatorcontrib>Wellmann, Frank</creatorcontrib><creatorcontrib>Britsch, Lothar</creatorcontrib><creatorcontrib>Martens, Stefan</creatorcontrib><creatorcontrib>Matern, Ulrich</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lukačin, Richard</au><au>Wellmann, Frank</au><au>Britsch, Lothar</au><au>Martens, Stefan</au><au>Matern, Ulrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase</atitle><jtitle>Phytochemistry (Oxford)</jtitle><addtitle>Phytochemistry</addtitle><date>2003-02-01</date><risdate>2003</risdate><volume>62</volume><issue>3</issue><spage>287</spage><epage>292</epage><pages>287-292</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Flavonol synthase was classified as a 2-oxoglutarate-dependent dioxygenase converting natural (2
R,3
R)-dihydroflavonols, i.e. dihydrokaempferol, to the corresponding flavonols (kaempferol). Flavonol synthase from
Citrus unshiu (Satsuma mandarin), expressed in
Escherichia coli and purified to homogeneity, was shown to accept also (2
S)-naringenin as a substrate, producing kaempferol in high yield and assigning sequential flavanone 3β-hydroxylase and flavonol synthase activities to the enzyme. In contrast, dihydrokaempferol was identified as the predominant product from assays performed with the unnatural (2
R)-naringenin as substrate. The product which was not converted any further on repeated incubations was identified by
1H NMR and CD spectroscopies as (−)-
trans-dihydrokaempferol. The data demonstrate that
Citrus flavonol synthase encompasses an additional non-specific activity
trans-hydroxylating the flavanones (2
S)-naringenin as well as the unnatural (2
R)-naringenin at C-3.
The recombinant flavonol sythase also catalyzes the 3-hydroxylation of (±) naringenin.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>12620339</pmid><doi>10.1016/S0031-9422(02)00567-8</doi><tpages>6</tpages></addata></record> |
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| ispartof | Phytochemistry (Oxford), 2003-02, Vol.62 (3), p.287-292 |
| issn | 0031-9422 1873-3700 |
| language | eng |
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| source | ScienceDirect Freedom Collection |
| subjects | Bifunctional dioxygenase Biological and medical sciences Chromatography, Thin Layer Circular Dichroism Citrus Citrus - enzymology Citrus unshiu Dihydroflavonol hydroxylase Escherichia coli Escherichia coli - metabolism Flavanones Flavonoid biosynthesis Flavonoids - biosynthesis Flavonoids - chemistry Flavonoids - metabolism Flavonol synthase Fundamental and applied biological sciences. Psychology Kaempferols Metabolism Metabolism. Physicochemical requirements Mixed Function Oxygenases - metabolism Oxidoreductases - metabolism Oxygenases - metabolism Plant physiology and development Plant Proteins Quercetin - analogs & derivatives Quercetin - biosynthesis Rutaceae Stereoisomerism |
| title | Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase |
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