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...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of molecular sciences Vol. 23; no. 24; p. 16156
Main Authors Zhang, Xuanhao, Liu, Yi, Ayaz, Asma, Zhao, Huayan, Lü, Shiyou
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 18.12.2022
MDPI
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms232416156