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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1996-7-30
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pubmed:abstractText |
An enormous variety of metabolic processes are characterized by enzyme complexes, which are likely to play important roles in directing the efficient operation and specificity of cellular metabolism. In many cases membranes or cytoskeletal elements provide scaffolding for these highly ordered assemblies of enzymes. Biochemical and immunocytochemical studies indicate that the flavonoid biosynthetic pathway of higher plants involves a complex of sequentially-acting enzymes localized at the cytoplasmic face of the endoplasmic reticulum. This paper describes preliminary efforts to define the organization of this putative flavonoid biosynthetic complex and elucidate its role in controlling the synthesis of different flavonoid end-products in the model plant, Arabidopsis thaliana.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavonoids,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/chalcone isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/dihydroflavanol 4-reductase,
http://linkedlifedata.com/resource/pubmed/chemical/flavanone 3-dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/flavanone synthetase
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pubmed:status |
MEDLINE
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pubmed:issn |
1052-6781
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-36
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8652129-Acyltransferases,
pubmed-meshheading:8652129-Alcohol Oxidoreductases,
pubmed-meshheading:8652129-Arabidopsis,
pubmed-meshheading:8652129-Binding Sites,
pubmed-meshheading:8652129-DNA,
pubmed-meshheading:8652129-DNA-Binding Proteins,
pubmed-meshheading:8652129-Endoplasmic Reticulum,
pubmed-meshheading:8652129-Flavonoids,
pubmed-meshheading:8652129-Fungal Proteins,
pubmed-meshheading:8652129-Intramolecular Lyases,
pubmed-meshheading:8652129-Isomerases,
pubmed-meshheading:8652129-Mixed Function Oxygenases,
pubmed-meshheading:8652129-Multienzyme Complexes,
pubmed-meshheading:8652129-Recombinant Fusion Proteins,
pubmed-meshheading:8652129-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8652129-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
Are flavonoids synthesized by a multi-enzyme complex?
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pubmed:affiliation |
Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg 24061-0406, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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