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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/24/16156 |
| _version_ | 1797457209524748288 |
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| author | Xuanhao Zhang Yi Liu Asma Ayaz Huayan Zhao Shiyou Lü |
| author_facet | Xuanhao Zhang Yi Liu Asma Ayaz Huayan Zhao Shiyou Lü |
| author_sort | Xuanhao Zhang |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-09T16:18:54Z |
| format | Article |
| id | doaj.art-89721e6dfdb74531a3a36cb18a38fb6b |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T16:18:54Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-89721e6dfdb74531a3a36cb18a38fb6b2023-11-24T15:33:57ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0123241615610.3390/ijms232416156The Plant Fatty Acyl ReductasesXuanhao Zhang0Yi Liu1Asma Ayaz2Huayan Zhao3Shiyou Lü4State Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, ChinaState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, ChinaState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, ChinaState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, ChinaState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, ChinaFatty 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.https://www.mdpi.com/1422-0067/23/24/16156fatty acyl reductasescuticular waxtaproot waxsuberinsporopolleninbiosynthesis |
| spellingShingle | Xuanhao Zhang Yi Liu Asma Ayaz Huayan Zhao Shiyou Lü The Plant Fatty Acyl Reductases International Journal of Molecular Sciences fatty acyl reductases cuticular wax taproot wax suberin sporopollenin biosynthesis |
| 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 | fatty acyl reductases cuticular wax taproot wax suberin sporopollenin biosynthesis |
| url | https://www.mdpi.com/1422-0067/23/24/16156 |
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