Evolution of serine carboxypeptidase-like acyltransferases in the monocots
- PMID: 20173416
- PMCID: PMC2884133
- DOI: 10.4161/psb.5.2.11093
Evolution of serine carboxypeptidase-like acyltransferases in the monocots
Abstract
The serine carboxypeptidases are a large family of proteases. in higher plants some members of this family have diversified and adopted new functions as acyltransferases required for the synthesis of natural products. we recently reported the first serine carboxypeptidase-like (scpl) acyltransferase enzyme to be characterized from monocotyledonous plants. This enzyme, AsSCPL1, is required for acylation of antimicrobial terpenes (avenacins) that are produced in the roots of oat (Avena spp.) and that provide protection against soil-borne pathogens. The SCPL acyltransferase enzyme family has undergone substantial expansion following the divergence of monocots and dicots. Here we discuss the evolution of this SCPL enzyme family in monocots, their contribution to metabolic diversity, and the roles of these enzymes in biotic and abiotic stress tolerance.
Figures
Comment on
-
A serine carboxypeptidase-like acyltransferase is required for synthesis of antimicrobial compounds and disease resistance in oats.Plant Cell. 2009 Aug;21(8):2473-84. doi: 10.1105/tpc.109.065870. Epub 2009 Aug 14. Plant Cell. 2009. PMID: 19684243 Free PMC article.
References
-
- D’Auria J. Acyltransferases in plants: a good time to be BAHD. Curr Opin Plant Biol. 2006;9:331–340. - PubMed
-
- Shirley AM, McMichael CM, Chapple C. The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase-like protein sinapoylglucose: choline sinapoyltransferase. Plant J. 2001;28:83–94. - PubMed
Publication types
Grants and funding
LinkOut - more resources
Full Text Sources
Miscellaneous