An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of
Citronella ( Cymbopogon winterianus ) is one of the richest sources of high-value isoprenoid aromatic compounds used as flavour, fragrance, and therapeutic elements. These isoprenoid compounds are synthesized by 2 independent pathways: mevalonate pathway and 2-C-methyl- d -erythritol-4-phosphate pat...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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SAGE Publishing
2017-03-01
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| Series: | Bioinformatics and Biology Insights |
| Online Access: | https://doi.org/10.1177/1177932217701735 |
| _version_ | 1828746136714739712 |
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| author | Kamalakshi Devi Lochana Patar Mahendra K Modi Priyabrata Sen |
| author_facet | Kamalakshi Devi Lochana Patar Mahendra K Modi Priyabrata Sen |
| author_sort | Kamalakshi Devi |
| collection | DOAJ |
| description | Citronella ( Cymbopogon winterianus ) is one of the richest sources of high-value isoprenoid aromatic compounds used as flavour, fragrance, and therapeutic elements. These isoprenoid compounds are synthesized by 2 independent pathways: mevalonate pathway and 2-C-methyl- d -erythritol-4-phosphate pathway. Evidence suggests that 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) is a rate-controlling enzyme for the synthesis of variety of isoprenoids. This study reports the isolation, characterization, and tissue-specific expression analysis of HMGR from citronella. The modelled HMGR is a class I type of HMGR enzyme with 3-domain architecture. The active site comprises a cofactor (nicotinamide adenine dinucleotide phosphate) and the substrate-binding motifs. The real-time and quantitative reverse transcription-polymerase chain reaction results revealed equal expression level in both leaf sheath and root tissue. The results from our study shall be a valuable resource for future molecular intervention to alter the metabolic flux towards improvement of key active ingredient in this important medicinal plant. |
| first_indexed | 2024-04-14T04:17:49Z |
| format | Article |
| id | doaj.art-c8261aeaf10b45cdaafa4aa9fcfc4c9d |
| institution | Directory Open Access Journal |
| issn | 1177-9322 |
| language | English |
| last_indexed | 2024-04-14T04:17:49Z |
| publishDate | 2017-03-01 |
| publisher | SAGE Publishing |
| record_format | Article |
| series | Bioinformatics and Biology Insights |
| spelling | doaj.art-c8261aeaf10b45cdaafa4aa9fcfc4c9d2022-12-22T02:12:46ZengSAGE PublishingBioinformatics and Biology Insights1177-93222017-03-011110.1177/117793221770173510.1177_1177932217701735An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase ofKamalakshi Devi0Lochana Patar1Mahendra K Modi2Priyabrata Sen3Distributed Information Centre (DIC), Assam Agricultural University, Jorhat, IndiaDistributed Information Centre (DIC), Assam Agricultural University, Jorhat, IndiaDistributed Information Centre (DIC), Assam Agricultural University, Jorhat, IndiaDepartment of Agricultural Biotechnology, Assam Agricultural University, Jorhat, IndiaCitronella ( Cymbopogon winterianus ) is one of the richest sources of high-value isoprenoid aromatic compounds used as flavour, fragrance, and therapeutic elements. These isoprenoid compounds are synthesized by 2 independent pathways: mevalonate pathway and 2-C-methyl- d -erythritol-4-phosphate pathway. Evidence suggests that 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) is a rate-controlling enzyme for the synthesis of variety of isoprenoids. This study reports the isolation, characterization, and tissue-specific expression analysis of HMGR from citronella. The modelled HMGR is a class I type of HMGR enzyme with 3-domain architecture. The active site comprises a cofactor (nicotinamide adenine dinucleotide phosphate) and the substrate-binding motifs. The real-time and quantitative reverse transcription-polymerase chain reaction results revealed equal expression level in both leaf sheath and root tissue. The results from our study shall be a valuable resource for future molecular intervention to alter the metabolic flux towards improvement of key active ingredient in this important medicinal plant.https://doi.org/10.1177/1177932217701735 |
| spellingShingle | Kamalakshi Devi Lochana Patar Mahendra K Modi Priyabrata Sen An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of Bioinformatics and Biology Insights |
| title | An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of |
| title_full | An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of |
| title_fullStr | An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of |
| title_full_unstemmed | An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of |
| title_short | An Insight Into Structure, Function, and Expression Analysis of 3-Hydroxy-3-Methylglutaryl-CoA Reductase of |
| title_sort | insight into structure function and expression analysis of 3 hydroxy 3 methylglutaryl coa reductase of |
| url | https://doi.org/10.1177/1177932217701735 |
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