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Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2
Pandanus amaryllifolius Roxb. accumulates the highest concentration of the major basmati aroma volatile 2-acetyl-1-pyrroline (2AP) in the plant kingdom. The expression of 2AP is correlated with the presence of a nonfunctional betaine aldehyde dehydrogenase 2(BADH2) in aromatic rice and other plant s...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8269274/ https://www.ncbi.nlm.nih.gov/pubmed/34203477 http://dx.doi.org/10.3390/ijms22136968 |
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author | Bhatt, Vacha Barvkar, Vitthal T. Furtado, Agnelo Henry, Robert J. Nadaf, Altafhusain |
author_facet | Bhatt, Vacha Barvkar, Vitthal T. Furtado, Agnelo Henry, Robert J. Nadaf, Altafhusain |
author_sort | Bhatt, Vacha |
collection | PubMed |
description | Pandanus amaryllifolius Roxb. accumulates the highest concentration of the major basmati aroma volatile 2-acetyl-1-pyrroline (2AP) in the plant kingdom. The expression of 2AP is correlated with the presence of a nonfunctional betaine aldehyde dehydrogenase 2(BADH2) in aromatic rice and other plant species. In the present study, a full-length BADH2 sequence was reconstructed from the transcriptome data of leaf tissue from P. amaryllifolius seedlings. Based on this sequence, a 1509 bp coding sequence was defined that encoded a 54 kD PaBADH2 protein. This revealed the presence of a full-length BADH2 protein in P. amaryllifolius. Moreover, quantitative real-time PCR analysis, combined with BADH2 enzyme activity, confirmed the expression and functionality of the PaBADH2 protein. To understand the apparent structural variation, docking analysis was carried out in which protein showed a good affinity with both betaine aldehyde (BAD) and γ-aminobutyraldehyde (GAB-ald) as substrates. Overall, the analysis showed the presence of a functional BADH2, along with substantial 2AP synthesis (4.38 ppm). Therefore, we conclude that unlike all other plants studied to date, 2AP biosynthesis in P. amaryllifolius is not due to the inactivation of BADH2. |
format | Online Article Text |
id | pubmed-8269274 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-82692742021-07-10 Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 Bhatt, Vacha Barvkar, Vitthal T. Furtado, Agnelo Henry, Robert J. Nadaf, Altafhusain Int J Mol Sci Article Pandanus amaryllifolius Roxb. accumulates the highest concentration of the major basmati aroma volatile 2-acetyl-1-pyrroline (2AP) in the plant kingdom. The expression of 2AP is correlated with the presence of a nonfunctional betaine aldehyde dehydrogenase 2(BADH2) in aromatic rice and other plant species. In the present study, a full-length BADH2 sequence was reconstructed from the transcriptome data of leaf tissue from P. amaryllifolius seedlings. Based on this sequence, a 1509 bp coding sequence was defined that encoded a 54 kD PaBADH2 protein. This revealed the presence of a full-length BADH2 protein in P. amaryllifolius. Moreover, quantitative real-time PCR analysis, combined with BADH2 enzyme activity, confirmed the expression and functionality of the PaBADH2 protein. To understand the apparent structural variation, docking analysis was carried out in which protein showed a good affinity with both betaine aldehyde (BAD) and γ-aminobutyraldehyde (GAB-ald) as substrates. Overall, the analysis showed the presence of a functional BADH2, along with substantial 2AP synthesis (4.38 ppm). Therefore, we conclude that unlike all other plants studied to date, 2AP biosynthesis in P. amaryllifolius is not due to the inactivation of BADH2. MDPI 2021-06-28 /pmc/articles/PMC8269274/ /pubmed/34203477 http://dx.doi.org/10.3390/ijms22136968 Text en © 2021 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 Bhatt, Vacha Barvkar, Vitthal T. Furtado, Agnelo Henry, Robert J. Nadaf, Altafhusain Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title | Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title_full | Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title_fullStr | Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title_full_unstemmed | Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title_short | Fragrance in Pandanus amaryllifolius Roxb. Despite the Presence of a Betaine Aldehyde Dehydrogenase 2 |
title_sort | fragrance in pandanus amaryllifolius roxb. despite the presence of a betaine aldehyde dehydrogenase 2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8269274/ https://www.ncbi.nlm.nih.gov/pubmed/34203477 http://dx.doi.org/10.3390/ijms22136968 |
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