Cargando…

Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin

Pogostone, a compound with various pharmaceutical activities, is a major constituent of the essential oil preparation called Pogostemonis Herba, which is obtained from the plant Pogostemon cablin. The biosynthesis of pogostone has not been elucidated, but 4-methylvaleryl-CoA (4MVCoA) is a likely pre...

Descripción completa

Detalles Bibliográficos
Autores principales: Chen, Jing, Liu, Lang, Wang, Ying, Li, Zhengguo, Wang, Guodong, Kraus, George A, Pichersky, Eran, Xu, Haiyang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8643619/
https://www.ncbi.nlm.nih.gov/pubmed/34255851
http://dx.doi.org/10.1093/pcp/pcab111
_version_ 1784609895198228480
author Chen, Jing
Liu, Lang
Wang, Ying
Li, Zhengguo
Wang, Guodong
Kraus, George A
Pichersky, Eran
Xu, Haiyang
author_facet Chen, Jing
Liu, Lang
Wang, Ying
Li, Zhengguo
Wang, Guodong
Kraus, George A
Pichersky, Eran
Xu, Haiyang
author_sort Chen, Jing
collection PubMed
description Pogostone, a compound with various pharmaceutical activities, is a major constituent of the essential oil preparation called Pogostemonis Herba, which is obtained from the plant Pogostemon cablin. The biosynthesis of pogostone has not been elucidated, but 4-methylvaleryl-CoA (4MVCoA) is a likely precursor. We analyzed the distribution of pogostone in P. cablin using gas chromatography-mass spectrometry (GC-MS) and found that pogostone accumulates at high levels in the main stems and leaves of young plants. A search for the acyl-activating enzyme (AAE) that catalyzes the formation of 4MVCoA from 4-methylvaleric acid was launched, using an RNAseq-based approach to identify 31 unigenes encoding putative AAEs including the PcAAE2, the transcript profile of which shows a strong positive correlation with the distribution pattern of pogostone. The protein encoded by PcAAE2 was biochemically characterized in vitro and shown to catalyze the formation of 4MVCoA from 4-methylvaleric acid. Phylogenetic analysis showed that PcAAE2 is closely related to other AAE proteins in P. cablin and other species that are localized to the peroxisomes. However, PcAAE2 lacks a peroxisome targeting sequence 1 (PTS1) and is localized in the cytosol.
format Online
Article
Text
id pubmed-8643619
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Oxford University Press
record_format MEDLINE/PubMed
spelling pubmed-86436192021-12-06 Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin Chen, Jing Liu, Lang Wang, Ying Li, Zhengguo Wang, Guodong Kraus, George A Pichersky, Eran Xu, Haiyang Plant Cell Physiol Regular Paper Pogostone, a compound with various pharmaceutical activities, is a major constituent of the essential oil preparation called Pogostemonis Herba, which is obtained from the plant Pogostemon cablin. The biosynthesis of pogostone has not been elucidated, but 4-methylvaleryl-CoA (4MVCoA) is a likely precursor. We analyzed the distribution of pogostone in P. cablin using gas chromatography-mass spectrometry (GC-MS) and found that pogostone accumulates at high levels in the main stems and leaves of young plants. A search for the acyl-activating enzyme (AAE) that catalyzes the formation of 4MVCoA from 4-methylvaleric acid was launched, using an RNAseq-based approach to identify 31 unigenes encoding putative AAEs including the PcAAE2, the transcript profile of which shows a strong positive correlation with the distribution pattern of pogostone. The protein encoded by PcAAE2 was biochemically characterized in vitro and shown to catalyze the formation of 4MVCoA from 4-methylvaleric acid. Phylogenetic analysis showed that PcAAE2 is closely related to other AAE proteins in P. cablin and other species that are localized to the peroxisomes. However, PcAAE2 lacks a peroxisome targeting sequence 1 (PTS1) and is localized in the cytosol. Oxford University Press 2021-07-13 /pmc/articles/PMC8643619/ /pubmed/34255851 http://dx.doi.org/10.1093/pcp/pcab111 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Regular Paper
Chen, Jing
Liu, Lang
Wang, Ying
Li, Zhengguo
Wang, Guodong
Kraus, George A
Pichersky, Eran
Xu, Haiyang
Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title_full Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title_fullStr Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title_full_unstemmed Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title_short Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin
title_sort characterization of a cytosolic acyl-activating enzyme catalyzing the formation of 4-methylvaleryl-coa for pogostone biosynthesis in pogostemon cablin
topic Regular Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8643619/
https://www.ncbi.nlm.nih.gov/pubmed/34255851
http://dx.doi.org/10.1093/pcp/pcab111
work_keys_str_mv AT chenjing characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT liulang characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT wangying characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT lizhengguo characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT wangguodong characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT krausgeorgea characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT picherskyeran characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin
AT xuhaiyang characterizationofacytosolicacylactivatingenzymecatalyzingtheformationof4methylvalerylcoaforpogostonebiosynthesisinpogostemoncablin