Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus

Polygonum minus (syn. Persicaria minor) is a herbal plant that is well known for producing sesquiterpenes, which contribute to its flavour and fragrance. This study describes the cloning and functional characterisation of PmSTPS1 and PmSTPS2, two sesquiterpene synthase genes that were identified fro...

Full description

Saved in:
Bibliographic Details
Main Authors: Rusdi, Nor Azizun, Goh, Hoe Han, Sabri, Suriana, Ramzi, Ahmad Bazli, Mohd Noor, Normah, Baharum, Syarul Nataqain
Format: Article
Language:English
Published: MDPI 2018
Online Access:http://psasir.upm.edu.my/id/eprint/72804/1/Functional%20characterisation%20of%20new%20sesquiterpene%20synthase%20from%20the%20Malaysian%20herbal%20plant%2C%20Polygonum%20minus.pdf
http://psasir.upm.edu.my/id/eprint/72804/
https://pubmed.ncbi.nlm.nih.gov/29882808/
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Universiti Putra Malaysia
Language: English
id my.upm.eprints.72804
record_format eprints
spelling my.upm.eprints.728042021-02-09T23:06:00Z http://psasir.upm.edu.my/id/eprint/72804/ Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus Rusdi, Nor Azizun Goh, Hoe Han Sabri, Suriana Ramzi, Ahmad Bazli Mohd Noor, Normah Baharum, Syarul Nataqain Polygonum minus (syn. Persicaria minor) is a herbal plant that is well known for producing sesquiterpenes, which contribute to its flavour and fragrance. This study describes the cloning and functional characterisation of PmSTPS1 and PmSTPS2, two sesquiterpene synthase genes that were identified from P. minus transcriptome data mining. The full-length sequences of the PmSTPS1 and PmSTPS2 genes were expressed in the E. coli pQE-2 expression vector. The sizes of PmSTPS1 and PmSTPS2 were 1098 bp and 1967 bp, respectively, with open reading frames (ORF) of 1047 and 1695 bp and encoding polypeptides of 348 and 564 amino acids, respectively. The proteins consist of three conserved motifs, namely, Asp-rich substrate binding (DDxxD), metal binding residues (NSE/DTE), and cytoplasmic ER retention (RxR), as well as the terpene synthase family N-terminal domain and C-terminal metal-binding domain. From the in vitro enzyme assays, using the farnesyl pyrophosphate (FPP) substrate, the PmSTPS1 enzyme produced multiple acyclic sesquiterpenes of β-farnesene, α-farnesene, and farnesol, while the PmSTPS2 enzyme produced an additional nerolidol as a final product. The results confirmed the roles of PmSTPS1 and PmSTPS2 in the biosynthesis pathway of P. minus, to produce aromatic sesquiterpenes. MDPI 2018 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/72804/1/Functional%20characterisation%20of%20new%20sesquiterpene%20synthase%20from%20the%20Malaysian%20herbal%20plant%2C%20Polygonum%20minus.pdf Rusdi, Nor Azizun and Goh, Hoe Han and Sabri, Suriana and Ramzi, Ahmad Bazli and Mohd Noor, Normah and Baharum, Syarul Nataqain (2018) Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus. Molecules, 23 (6). pp. 1-15. ISSN 1420-3049 https://pubmed.ncbi.nlm.nih.gov/29882808/ 10.3390/molecules23061370
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description Polygonum minus (syn. Persicaria minor) is a herbal plant that is well known for producing sesquiterpenes, which contribute to its flavour and fragrance. This study describes the cloning and functional characterisation of PmSTPS1 and PmSTPS2, two sesquiterpene synthase genes that were identified from P. minus transcriptome data mining. The full-length sequences of the PmSTPS1 and PmSTPS2 genes were expressed in the E. coli pQE-2 expression vector. The sizes of PmSTPS1 and PmSTPS2 were 1098 bp and 1967 bp, respectively, with open reading frames (ORF) of 1047 and 1695 bp and encoding polypeptides of 348 and 564 amino acids, respectively. The proteins consist of three conserved motifs, namely, Asp-rich substrate binding (DDxxD), metal binding residues (NSE/DTE), and cytoplasmic ER retention (RxR), as well as the terpene synthase family N-terminal domain and C-terminal metal-binding domain. From the in vitro enzyme assays, using the farnesyl pyrophosphate (FPP) substrate, the PmSTPS1 enzyme produced multiple acyclic sesquiterpenes of β-farnesene, α-farnesene, and farnesol, while the PmSTPS2 enzyme produced an additional nerolidol as a final product. The results confirmed the roles of PmSTPS1 and PmSTPS2 in the biosynthesis pathway of P. minus, to produce aromatic sesquiterpenes.
format Article
author Rusdi, Nor Azizun
Goh, Hoe Han
Sabri, Suriana
Ramzi, Ahmad Bazli
Mohd Noor, Normah
Baharum, Syarul Nataqain
spellingShingle Rusdi, Nor Azizun
Goh, Hoe Han
Sabri, Suriana
Ramzi, Ahmad Bazli
Mohd Noor, Normah
Baharum, Syarul Nataqain
Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
author_facet Rusdi, Nor Azizun
Goh, Hoe Han
Sabri, Suriana
Ramzi, Ahmad Bazli
Mohd Noor, Normah
Baharum, Syarul Nataqain
author_sort Rusdi, Nor Azizun
title Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
title_short Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
title_full Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
title_fullStr Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
title_full_unstemmed Functional characterisation of new sesquiterpene synthase from the Malaysian herbal plant, Polygonum minus
title_sort functional characterisation of new sesquiterpene synthase from the malaysian herbal plant, polygonum minus
publisher MDPI
publishDate 2018
url http://psasir.upm.edu.my/id/eprint/72804/1/Functional%20characterisation%20of%20new%20sesquiterpene%20synthase%20from%20the%20Malaysian%20herbal%20plant%2C%20Polygonum%20minus.pdf
http://psasir.upm.edu.my/id/eprint/72804/
https://pubmed.ncbi.nlm.nih.gov/29882808/
_version_ 1691734446126923776