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Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa

Rehmannia glutinosa is an important medicinal plant that has long been used in Chinese traditional medicine. Acteoside, one of the bioactive components from R. glutinosa, possessed various pharmacological activities for human health; however, the molecular mechanism of acteoside formation is not ful...

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Autores principales: Li, Yuanjun, Wang, Yanan, Huang, Longyu, Chen, Chunrong, An, Na, Zheng, Xiaoke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8912026/
https://www.ncbi.nlm.nih.gov/pubmed/35268735
http://dx.doi.org/10.3390/molecules27051634
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author Li, Yuanjun
Wang, Yanan
Huang, Longyu
Chen, Chunrong
An, Na
Zheng, Xiaoke
author_facet Li, Yuanjun
Wang, Yanan
Huang, Longyu
Chen, Chunrong
An, Na
Zheng, Xiaoke
author_sort Li, Yuanjun
collection PubMed
description Rehmannia glutinosa is an important medicinal plant that has long been used in Chinese traditional medicine. Acteoside, one of the bioactive components from R. glutinosa, possessed various pharmacological activities for human health; however, the molecular mechanism of acteoside formation is not fully understood. In the current study, a novel tyrosine decarboxylase (designated as RgTyDC2) was identified from the R. glutinosa transcriptome. Biochemical analysis of RgTyDC2 showed RgTyDC2 uses tyrosine and dopa as the substrate to produce tyramine and dopamine, respectively, and it displays higher catalytic efficiency toward tyrosine than dopa. Moreover, the transcript level of RgTyDC2 was consistent with the accumulation pattern of acteoside in R. glutinosa, supporting its possible role in the biosynthesis of acteoside in vivo.
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spelling pubmed-89120262022-03-11 Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa Li, Yuanjun Wang, Yanan Huang, Longyu Chen, Chunrong An, Na Zheng, Xiaoke Molecules Article Rehmannia glutinosa is an important medicinal plant that has long been used in Chinese traditional medicine. Acteoside, one of the bioactive components from R. glutinosa, possessed various pharmacological activities for human health; however, the molecular mechanism of acteoside formation is not fully understood. In the current study, a novel tyrosine decarboxylase (designated as RgTyDC2) was identified from the R. glutinosa transcriptome. Biochemical analysis of RgTyDC2 showed RgTyDC2 uses tyrosine and dopa as the substrate to produce tyramine and dopamine, respectively, and it displays higher catalytic efficiency toward tyrosine than dopa. Moreover, the transcript level of RgTyDC2 was consistent with the accumulation pattern of acteoside in R. glutinosa, supporting its possible role in the biosynthesis of acteoside in vivo. MDPI 2022-03-01 /pmc/articles/PMC8912026/ /pubmed/35268735 http://dx.doi.org/10.3390/molecules27051634 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Yuanjun
Wang, Yanan
Huang, Longyu
Chen, Chunrong
An, Na
Zheng, Xiaoke
Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title_full Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title_fullStr Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title_full_unstemmed Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title_short Identification and Functional Characterization of Tyrosine Decarboxylase from Rehmannia glutinosa
title_sort identification and functional characterization of tyrosine decarboxylase from rehmannia glutinosa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8912026/
https://www.ncbi.nlm.nih.gov/pubmed/35268735
http://dx.doi.org/10.3390/molecules27051634
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