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The Plant Fatty Acyl Reductases
Fatty acyl reductase (FAR) is a crucial enzyme that catalyzes the NADPH-dependent reduction of fatty acyl-CoA or acyl-ACP substrates to primary fatty alcohols, which in turn acts as intermediate metabolites or metabolic end products to participate in the formation of plant extracellular lipid protec...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9783961/ https://www.ncbi.nlm.nih.gov/pubmed/36555796 http://dx.doi.org/10.3390/ijms232416156 |
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author | Zhang, Xuanhao Liu, Yi Ayaz, Asma Zhao, Huayan Lü, Shiyou |
author_facet | Zhang, Xuanhao Liu, Yi Ayaz, Asma Zhao, Huayan Lü, Shiyou |
author_sort | Zhang, Xuanhao |
collection | PubMed |
description | Fatty acyl reductase (FAR) is a crucial enzyme that catalyzes the NADPH-dependent reduction of fatty acyl-CoA or acyl-ACP substrates to primary fatty alcohols, which in turn acts as intermediate metabolites or metabolic end products to participate in the formation of plant extracellular lipid protective barriers (e.g., cuticular wax, sporopollenin, suberin, and taproot wax). FARs are widely present across plant evolution processes and play conserved roles during lipid synthesis. In this review, we provide a comprehensive view of FAR family enzymes, including phylogenetic analysis, conserved structural domains, substrate specificity, subcellular localization, tissue-specific expression patterns, their varied functions in lipid biosynthesis, and the regulation mechanism of FAR activity. Finally, we pose several questions to be addressed, such as the roles of FARs in tryphine, the interactions between transcription factors (TFs) and FARs in various environments, and the identification of post-transcriptional, translational, and post-translational regulators. |
format | Online Article Text |
id | pubmed-9783961 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97839612022-12-24 The Plant Fatty Acyl Reductases Zhang, Xuanhao Liu, Yi Ayaz, Asma Zhao, Huayan Lü, Shiyou Int J Mol Sci Review Fatty acyl reductase (FAR) is a crucial enzyme that catalyzes the NADPH-dependent reduction of fatty acyl-CoA or acyl-ACP substrates to primary fatty alcohols, which in turn acts as intermediate metabolites or metabolic end products to participate in the formation of plant extracellular lipid protective barriers (e.g., cuticular wax, sporopollenin, suberin, and taproot wax). FARs are widely present across plant evolution processes and play conserved roles during lipid synthesis. In this review, we provide a comprehensive view of FAR family enzymes, including phylogenetic analysis, conserved structural domains, substrate specificity, subcellular localization, tissue-specific expression patterns, their varied functions in lipid biosynthesis, and the regulation mechanism of FAR activity. Finally, we pose several questions to be addressed, such as the roles of FARs in tryphine, the interactions between transcription factors (TFs) and FARs in various environments, and the identification of post-transcriptional, translational, and post-translational regulators. MDPI 2022-12-18 /pmc/articles/PMC9783961/ /pubmed/36555796 http://dx.doi.org/10.3390/ijms232416156 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 | Review Zhang, Xuanhao Liu, Yi Ayaz, Asma Zhao, Huayan Lü, Shiyou The Plant Fatty Acyl Reductases |
title | The Plant Fatty Acyl Reductases |
title_full | The Plant Fatty Acyl Reductases |
title_fullStr | The Plant Fatty Acyl Reductases |
title_full_unstemmed | The Plant Fatty Acyl Reductases |
title_short | The Plant Fatty Acyl Reductases |
title_sort | plant fatty acyl reductases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9783961/ https://www.ncbi.nlm.nih.gov/pubmed/36555796 http://dx.doi.org/10.3390/ijms232416156 |
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