Document Detail


Novel hydroxycinnamoyl-coenzyme A quinate transferase genes from artichoke are involved in the synthesis of chlorogenic acid.
MedLine Citation:
PMID:  20431089     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Artichoke (Cynara cardunculus subsp. scolymus) extracts have high antioxidant capacity, due primarily to flavonoids and phenolic acids, particularly chlorogenic acid (5-caffeoylquinic acid [CGA]), dicaffeoylquinic acids, and caffeic acid, which are abundant in flower bracts and bioavailable to humans in the diet. The synthesis of CGA can occur following different routes in plant species, and hydroxycinnamoyl-coenzyme A transferases are important enzymes in these pathways. Here, we report on the isolation and characterization of two novel genes both encoding hydroxycinnamoyl-coenzyme A quinate transferases (HQT) from artichoke. The recombinant proteins (HQT1 and HQT2) were assayed after expression in Escherichia coli, and both showed higher affinity for quinate over shikimate. Their preferences for acyl donors, caffeoyl-coenzyme A or p-coumaroyl-coenzyme A, were examined. Modeling and docking analyses were used to propose possible pockets and residues involved in determining substrate specificities in the HQT enzyme family. Quantitative real-time polymerase chain reaction analysis of gene expression indicated that HQT1 might be more directly associated with CGA content. Transient and stable expression of HQT1 in Nicotiana resulted in a higher production of CGA and cynarin (1,3-dicaffeoylquinic acid). These findings suggest that several isoforms of HQT contribute to the synthesis of CGA in artichoke according to physiological needs and possibly following various metabolic routes.
Authors:
Gabriella Sonnante; Rosalinda D'Amore; Emanuela Blanco; Ciro L Pierri; Monica De Palma; Jie Luo; Marina Tucci; Cathie Martin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-29
Journal Detail:
Title:  Plant physiology     Volume:  153     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-02     Completed Date:  2010-10-07     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1224-38     Citation Subset:  IM    
Affiliation:
Institute of Plant Genetics, National Research Council, 70126 Bari, Italy. gabriella.sonnante@igv.cnr.it
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AM690438;  EU442190;  EU697935;  EU839580;  FM244907
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MeSH Terms
Descriptor/Qualifier:
Acyltransferases / chemistry,  genetics*,  metabolism
Amino Acid Sequence
Base Sequence
Binding Sites
Chlorogenic Acid / metabolism*
Cynara scolymus / enzymology*,  genetics*
DNA, Complementary / genetics,  isolation & purification
Enzyme Assays
Escherichia coli / metabolism
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Genes, Plant / genetics*
Kinetics
Models, Biological
Models, Molecular
Molecular Sequence Data
Organ Specificity / genetics
Phylogeny
Plant Proteins / chemistry,  genetics*,  metabolism
Plants, Genetically Modified
Sequence Analysis, DNA
Structural Homology, Protein
Tobacco / genetics
Grant Support
ID/Acronym/Agency:
//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/Plant Proteins; 327-97-9/Chlorogenic Acid; EC 2.3.-/Acyltransferases; EC 2.3.1.-/hydroxycinnamoyl-CoA-quinate transferase
Comments/Corrections

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