Recent advances in polyphenol research . Volume 4 / / edited by Annalisa Romani, Vincenzo Lattanzio, Stephane Quideau ; contributors Nickolas A. Anderson [and twenty eight others]

• Record Nr.: UNINA9910812642303321
• Pubbl/distr/stampa: Chichester, England : , : Wiley Blackwell, , 2014; ©2014
• ISBN: 1-118-32963-5; 1-118-32966-X; 1-118-32965-1
• Descrizione fisica: 1 online resource (468 p.)
• Collana: Recent Advances in Polyphenol Research
• Disciplina: 581.192
• Soggetti: Botanical chemistry; Polyphenols
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references at the end of each chapters and index.
• Nota di contenuto: Cover; Title Page; Copyright; Acknowledgments; Contents; Contributors; Preface; Chapter 1 Monolignol Biosynthesis and its Genetic Manipulation: The Good, the Bad, and the Ugly; 1.1 Introduction; 1.2 Function and distribution of lignin in plants; 1.3 Targets for modification of lignin biosynthesis; 1.3.1 Gene targets 1. Biosynthetic enzymes; 1.3.1.1 L-phenylalanine ammonia-lyase (PAL); 1.3.1.2 Cinnamate 4-hydroxylase (C4H); 1.3.1.3 4-coumarate: coenzyme-A ligase (4CL); 1.3.1.4 Enzymes of the coumaroyl shikimate shunt; 1.3.1.5 Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT); 1.3.1.6 Ferulate 5-hydroxylase (F5H)1.3.1.7 Caffeic acid 3-O-methyltransferase (COMT); 1.3.1.8 Cinnamoyl-CoA reductase; 1.3.1.9 Cinnamyl alcohol dehydrogenase (CAD); 1.3.2 Gene targets 2. Transcription factors; 1.4 Impacts of lignin modification through targeting of the monolignol biosynthetic pathway; 1.4.1 L-phenylalanine ammonia-lyase (PAL); 1.4.2 Cinnamate 4-hydroxylase (C4H); 1.4.3 4-coumarate: coenzyme-A ligase (4CL); 1.4.4 Hydroxycinnamoyl-CoA: shikimate hydroxycinnamoyl transferase (HCT); 1.4.5 4-coumaroyl shikimate 3'-hydroxylase (C3'H); 1.4.6 Caffeoyl CoA 3-O-methyltransferase (CCoAOMT)1.4.7 Ferulate 5-hydroxylase (F5H); 1.4.8 Caffeic acid O-methyltransferase (COMT); 1.4.9 Cinnamoyl-CoA reductase (CCR); 1.4.10 Cinnamyl alcohol dehydrogenase (CAD); 1.5 Impacts of lignin modification through targeting of TFs; 1.5.1 NAC master switches; 1.5.2 MYB repressors of monolignol biosynthesis; 1.5.3 WRKY repressors of lignification in pith; 1.6 Monolignol pathway modification and plant growth; 1.7 Conclusions: it isn't all that bad!; References; Chapter 2 Perturbing Lignin Biosynthesis: Metabolic Changes in Response to Manipulation of the Phenylpropanoid Pathway2.1 Introduction; 2.1.1 Cell wall-bound phenylpropanoids; 2.1.2 Soluble phenylpropanoids; 2.2 Changes in metabolism associated with phenylpropanoid-pathway disruptions; 2.2.1 Phenylalanine ammonia-lyase (PAL); 2.2.2 Cinnamate 4-hydroxylase (C4H); 2.2.3 4-coumarate: CoA ligase (4CL); 2.2.4 Hydroxycinnamoyl-coenzyme A: shikimate/quinate hydroxycinnamoyltransferase (HCT)/p-coumaroyl shikimate 3'-hydroxylase (C3'H); 2.2.5 Cinnamoyl CoA reductase (CCR); 2.2.6 Ferulate 5-hydroxylase (F5H)2.2.7 Caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT)/caffeoyl CoA 3-O-methyltransferase (CCoAOMT); 2.2.8 Cinnamyl alcohol dehydrogenases (CAD); 2.3 Atypical lignins; 2.4 Dwarfism; 2.5 Conclusions; References; Chapter 3 Function, Structure, and Evolution of Flavonoid Glycosyltransferases in Plants; 3.1 Introduction; 3.2 UDP-dependent glycosyltransferases; 3.2.1 Functional identification of flavonoid UGTs; 3.2.1.1 Flavonoid 3-O-glycosyltransferases; 3.2.1.2 Flavonoid 7-O-glycosyltransferases; 3.2.1.3 Flavonoid glycosyltransferases that glycosylate the sugar moiety attached to a flavonoid aglycone
• Sommario/riassunto: Plant polyphenols are secondary metabolites that constitute one of the most common and widespread groups of natural products. They express a large and diverse panel of biological activities including beneficial effects on both plants and humans. Many polyphenols, from their structurally simplest representatives to their oligo/polymeric versions (also referred to as vegetable tannins) are notably known as phytoestrogens, plant pigments, potent antioxidants, and protein interacting agents. Sponsored by the scholarly society Groupe Polyphénols, this publication, which is the fourth volume in th