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...
Autores principales: | , , , , , , , |
---|---|
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 |