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Caffeoyl shikimate esterase (CSE) is an enzyme in the lignin biosynthetic pathway in Arabidopsis.
Vanholme, Ruben; Cesarino, Igor; Rataj, Katarzyna; Xiao, Yuguo; Sundin, Lisa; Goeminne, Geert; Kim, Hoon; Cross, Joanna; Morreel, Kris; Araujo, Pedro; Welsh, Lydia; Haustraete, Jurgen; McClellan, Christopher; Vanholme, Bartel; Ralph, John; Simpson, Gordon G; Halpin, Claire; Boerjan, Wout.
Affiliation
  • Vanholme R; Department of Plant Systems Biology, VIB (Flanders Institute for Biotechnology), Technologiepark 927, B-9052 Ghent, Belgium.
Science ; 341(6150): 1103-6, 2013 Sep 06.
Article in En | MEDLINE | ID: mdl-23950498
Lignin is a major component of plant secondary cell walls. Here we describe caffeoyl shikimate esterase (CSE) as an enzyme central to the lignin biosynthetic pathway. Arabidopsis thaliana cse mutants deposit less lignin than do wild-type plants, and the remaining lignin is enriched in p-hydroxyphenyl units. Phenolic metabolite profiling identified accumulation of the lignin pathway intermediate caffeoyl shikimate in cse mutants as compared to caffeoyl shikimate levels in the wild type, suggesting caffeoyl shikimate as a substrate for CSE. Accordingly, recombinant CSE hydrolyzed caffeoyl shikimate into caffeate. Associated with the changes in lignin, the conversion of cellulose to glucose in cse mutants increased up to fourfold as compared to that in the wild type upon saccharification without pretreatment. Collectively, these data necessitate the revision of currently accepted models of the lignin biosynthetic pathway.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carboxylic Ester Hydrolases / Arabidopsis / Arabidopsis Proteins / Lignin Language: En Journal: Science Year: 2013 Document type: Article Affiliation country: Belgium Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carboxylic Ester Hydrolases / Arabidopsis / Arabidopsis Proteins / Lignin Language: En Journal: Science Year: 2013 Document type: Article Affiliation country: Belgium Country of publication: United States