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Article: Two divergent members of 4-coumarate: Coenzyme a ligase from salvia miltiorrhiza bunge: cDNA cloning and functional study

TitleTwo divergent members of 4-coumarate: Coenzyme a ligase from salvia miltiorrhiza bunge: cDNA cloning and functional study
Authors
Keywords4-coumarate:Coenzyme A ligase (4CL)
cDNA cloning
Danshen(Salvia miltiorrhiza)
Enzymatic kinetic assays
Water-soluble phenolic acids
Issue Date2006
PublisherBlackwell Publishing Ltd.
Citation
Journal Of Integrative Plant Biology, 2006, v. 48 n. 11, p. 1355-1364 How to Cite?
Abstract4-Coumarate: coenzyme A ligase (4CL) is one of the key enzymes in phenylpropanoid metabolism leading to series of phenolics, including water-soluble phenolic acids, which are important compounds determining the medicinal quality of Danshen (Salvia miltiorrhiza Bunge), a traditional Chinese medicinal herb. To investigate the function of 4CL in the biosynthesis of water-soluble phenolic acid in Danshen, we have cloned two cDNAs (Sm4CL1 and Sm4CL2) encoding divergent 4CL members by applying nested reverse transcription-polymerase chain reaction (RT-PCR) with degenerate primers followed by 5′/3′ rapid amplification of cDNA ends (RACE) (Note, these sequence data have been submitted to the GenBank database under accession numbers AY237163 and AY237164). Either of the coding regions was inserted into a pRSET vector and a kinetic assay was performed with purified recombinant proteins. The substrate utilization profile of Sm4CL1 was distinct from that of Sm4CL2. The K m values of Sm4CL1 and Sm4CL2 to 4-coumaric acid were (72.20±4.10) and (6.50±1.45) μmol/L, respectively. These results, in conjunction with Northern blotting and other information, imply that Sm4CL2 may play an important role in the biosynthesis of water-soluble phenolic compounds, whereas Sm4CL1 may play a minor role in the pathway. Southern blotting analysis suggested that both Sm4CL1 and Sm4CL2 genes are present as a single copy and are located at different sites in the genome. © 2006 Institute of Botany, Chinese Academy of Sciences.
Persistent Identifierhttp://hdl.handle.net/10722/84812
ISSN
2015 Impact Factor: 3.67
2015 SCImago Journal Rankings: 1.674
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhao, SJen_HK
dc.contributor.authorHu, ZBen_HK
dc.contributor.authorLiu, Den_HK
dc.contributor.authorLeung, FCCen_HK
dc.date.accessioned2010-09-06T08:57:24Z-
dc.date.available2010-09-06T08:57:24Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of Integrative Plant Biology, 2006, v. 48 n. 11, p. 1355-1364en_HK
dc.identifier.issn1672-9072en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84812-
dc.description.abstract4-Coumarate: coenzyme A ligase (4CL) is one of the key enzymes in phenylpropanoid metabolism leading to series of phenolics, including water-soluble phenolic acids, which are important compounds determining the medicinal quality of Danshen (Salvia miltiorrhiza Bunge), a traditional Chinese medicinal herb. To investigate the function of 4CL in the biosynthesis of water-soluble phenolic acid in Danshen, we have cloned two cDNAs (Sm4CL1 and Sm4CL2) encoding divergent 4CL members by applying nested reverse transcription-polymerase chain reaction (RT-PCR) with degenerate primers followed by 5′/3′ rapid amplification of cDNA ends (RACE) (Note, these sequence data have been submitted to the GenBank database under accession numbers AY237163 and AY237164). Either of the coding regions was inserted into a pRSET vector and a kinetic assay was performed with purified recombinant proteins. The substrate utilization profile of Sm4CL1 was distinct from that of Sm4CL2. The K m values of Sm4CL1 and Sm4CL2 to 4-coumaric acid were (72.20±4.10) and (6.50±1.45) μmol/L, respectively. These results, in conjunction with Northern blotting and other information, imply that Sm4CL2 may play an important role in the biosynthesis of water-soluble phenolic compounds, whereas Sm4CL1 may play a minor role in the pathway. Southern blotting analysis suggested that both Sm4CL1 and Sm4CL2 genes are present as a single copy and are located at different sites in the genome. © 2006 Institute of Botany, Chinese Academy of Sciences.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd.en_HK
dc.relation.ispartofJournal of Integrative Plant Biologyen_HK
dc.rightsJournal of Integrative Plant Biology. Copyright © Blackwell Publishing Ltd.en_HK
dc.subject4-coumarate:Coenzyme A ligase (4CL)en_HK
dc.subjectcDNA cloningen_HK
dc.subjectDanshen(Salvia miltiorrhiza)en_HK
dc.subjectEnzymatic kinetic assaysen_HK
dc.subjectWater-soluble phenolic acidsen_HK
dc.titleTwo divergent members of 4-coumarate: Coenzyme a ligase from salvia miltiorrhiza bunge: cDNA cloning and functional studyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1672-9072&volume=48&spage=1355&epage=1364&date=2006&atitle=Two+Divergent+Members+of+4-Coumarate:+Coenzyme+A+Ligase+from+Salvia+miltiorrhiza+Bunge:+cDNA+Cloning+and+Functional+Studyen_HK
dc.identifier.emailLeung, FCC: fcleung@hkucc.hku.hken_HK
dc.identifier.authorityLeung, FCC=rp00731en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1744-7909.2006.00302.xen_HK
dc.identifier.scopuseid_2-s2.0-33845528420en_HK
dc.identifier.hkuros133520en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845528420&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume48en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1355en_HK
dc.identifier.epage1364en_HK
dc.identifier.isiWOS:000241736600013-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridZhao, SJ=15521675200en_HK
dc.identifier.scopusauthoridHu, ZB=7404211433en_HK
dc.identifier.scopusauthoridLiu, D=55367643500en_HK
dc.identifier.scopusauthoridLeung, FCC=7103078633en_HK
dc.identifier.citeulike926887-

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