Details

Autor(en) / Beteiligte

• Yan, Xiaoguang
• Qin, Xiaoyu
• Li, Weiguo
• Liang, Dongmei
• Qiao, Jianjun
• Li, Yanni

Titel

Functional characterization and catalytic activity improvement of BAHD acyltransferase from Celastrus angulatus Maxim

Ist Teil von

• Planta, 2020-07, Vol.252 (1), p.6-6, Article 6

Ort / Verlag

Berlin/Heidelberg: Springer Berlin Heidelberg

Erscheinungsjahr

2020

Quelle

MEDLINE

Beschreibungen/Notizen

• Main Conclusion A BAHD terpene alcohol acyltransferase, CaAT20, was identified from Celastrus angulatus Maxim, expressed in E. coli and functionally characterized. S405A mutant of CaAT20 increased the enzyme activity. Acylation is a diversely physiological process in the biosynthesis of plant secondary metabolites. Plant BAHD acyltransferases play an important role in the modification of volatile esters with biological activities. In this research, a BAHD acyltransferase (CaAT20) was identified from Celastrus angulatus Maxim and the function of this enzyme was characterized. CaAT20 could convert geraniol to geranyl esters by using benzoyl-CoA and acetyl-CoA as the acyl donors respectively. Furthermore, the catalytic activity of CaAT20 for benzoyl-CoA was higher than that of acetyl-CoA. Site-directed mutation of CaAT20 was carried out based on the results of molecular simulation. In vitro site-directed mutant S405A of CaAT20 increased the volume of binding cavity so as to facilitate the entry of geraniol, indicating a more efficient acylation for geraniol and benzoyl-CoA. Our research provides new insight for the catalytic functions of CaAT20.