BAHD or SCPL acyltransferase? What a dilemma for acylation in the world of plant phenolic compounds

被引:166
作者
Bontpart, Thibaut [1 ]
Cheynier, Veronique [1 ]
Ageorges, Agnes [1 ]
Terrier, Nancy [1 ]
机构
[1] INRA, UMR1083, F-34060 Montpellier, France
关键词
acylation; acyltransferase; BAHD; biosynthesis; phenolic compounds; secondary metabolite; Serine CarboxyPeptidase-Like (SCPL); CHLOROGENIC ACID BIOSYNTHESIS; CARBOXYPEPTIDASE-LIKE ACYLTRANSFERASE; QUINATE HYDROXYCINNAMOYL TRANSFERASE; ARABIDOPSIS SERINE CARBOXYPEPTIDASE; SALVIA-SPLENDENS FLOWERS; ATP-BINDING CASSETTE; FUNCTIONAL-CHARACTERIZATION; CDNA CLONING; COENZYME-A; PROANTHOCYANIDIN BIOSYNTHESIS;
D O I
10.1111/nph.13498
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Phenolic compounds are secondary metabolites involved in several plant growth and development processes, including resistance to biotic and abiotic stresses. The biosynthetic pathways leading to the vast diversity of plant phenolic products often include an acylation step, with phenolic compounds being the donor or acceptor molecules. To date, two acyltransferase families using phenolic compounds as acceptor or donor molecules have been described, with each using a different 'energy-rich' acyl donor. BAHD-acyltransferases, named after the first four biochemically characterized enzymes of the group, use acyl-CoA thioesters as donor molecules, whereas SCPL (Serine CarboxyPeptidase Like)-acyltransferases use 1-O-beta-glucose esters. Here, common and divergent specifications found in the literature for both enzyme families were analyzed to answer the following questions. Are both acyltransferases involved in the synthesis of the same molecule (or same group of molecules)? Are both acyltransferases recruited in the same plant? How does the subcellular localization of these enzymes impact metabolite trafficking in plant cells?
引用
收藏
页码:695 / 707
页数:13
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