ArticleJournal of experimental botany2012
Phylogeny and structure of the cinnamyl alcohol dehydrogenase gene family in Brachypodium distachyon.
Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 58 citations in OpenAlex.
- Benzyl alcohol biosynthesis and its subcellular compartmentalization enable scent formation and salicylic acid production.Nature communications · 2026Article
- Allelic Expression Dynamics of Regulatory Factors During Embryogenic Callus Induction in ABB Banana (Plants (Basel, Switzerland) · 2025Article
- Systematic Analysis of Cinnamyl Alcohol Dehydrogenase Family in Cassava and Validation ofInternational journal of molecular sciences · 2024Article
- Genome-wide characterization and expression analysis of the CINNAMYL ALCOHOL DEHYDROGENASE gene family in Triticum aestivum.BMC genomics · 2024Article
- Genome-wide identification and expression analysis of the ADH gene family under diverse stresses in tobacco (Nicotiana tabacum L.).BMC genomics · 2024Article
- Genome-wide identification of thePeerJ · 2024Article
- Genome-wide identification of theFrontiers in plant science · 2024Article
- Genome-wide analysis of the3 Biotech · 2022Article
- Transcriptome Mining Provides Insights into Cell Wall Metabolism and Fiber Lignification inPlants (Basel, Switzerland) · 2022Article
- Cloning and in silico characterization of cinnamyl alcohol dehydrogenase gene involved in lignification of Tall fescue (Festuca arundinacea Schreb.).Molecular genetics and genomics : MGG · 2022Article
- Molecular breeding of barley for quality traits and resilience to climate change.Frontiers in genetics · 2022Review
- Article
- Homo- and Hetero-Dimers of CAD Enzymes Regulate Lignification and Abiotic Stress Response in Moso Bamboo.International journal of molecular sciences · 2021Article
- Identification of genes from the general phenylpropanoid and monolignol-specific metabolism in two sugarcane lignin-contrasting genotypes.Molecular genetics and genomics : MGG · 2020Article
- Isolation, cloning and expression analysis of cinnamyl alcohol dehydrogenase (CAD) involved in phenylpropanoid pathway of3 Biotech · 2020Article
- Biochemical Characterization of the Rice Cinnamyl Alcohol Dehydrogenase Gene Family.Molecules (Basel, Switzerland) · 2018Article
- Characterization and analysis ofBiology open · 2017Article
- Transcriptome-wide identification and characterization of CAD isoforms specific for podophyllotoxin biosynthesis from Podophyllum hexandrum.Plant molecular biology · 2016Article
- The Alcohol Dehydrogenase Gene Family in Melon (Cucumis melo L.): Bioinformatic Analysis and Expression Patterns.Frontiers in plant science · 2016Article
- Map-based cloning and expression analysis of BMR-6 in sorghum.Journal of genetics · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cinnamyl alcohol dehydrogenase (CAD) catalyses the final step of the monolignol biosynthesis, the conversion of cinnamyl aldehydes to alcohols, using NADPH as a cofactor. Seven members of the CAD gene family were identified in the genome of Brachypodium distachyon and five of these were isolated and cloned from genomic DNA. Semi-quantitative reverse-transcription PCR revealed differential expression of the cloned genes, with BdCAD5 being expressed in all tissues and highest in root and stem while BdCAD3 was only expressed in stem and spikes. A phylogenetic analysis of CAD-like proteins placed BdCAD5 on the same branch as bona fide CAD proteins from maize (ZmCAD2), rice (OsCAD2), sorghum (SbCAD2) and Arabidopsis (AtCAD4, 5). The predicted three-dimensional structures of both BdCAD3 and BdCAD5 resemble that of AtCAD5. However, the amino-acid residues in the substrate-binding domains of BdCAD3 and BdCAD5 are distributed symmetrically and BdCAD3 is similar to that of poplar sinapyl alcohol dehydrogenase (PotSAD). BdCAD3 and BdCAD5 expressed and purified from Escherichia coli both showed a temperature optimum of about 50 °C and molar weight of 49 kDa. The optimal pH for the reduction of coniferyl aldehyde were pH 5.2 and 6.2 and the pH for the oxidation of coniferyl alcohol were pH 8 and 9.5, for BdCAD3 and BdCAD5 respectively. Kinetic parameters for conversion of coniferyl aldehyde and coniferyl alcohol showed that BdCAD5 was clearly the most efficient enzyme of the two. These data suggest that BdCAD5 is the main CAD enzyme for lignin biosynthesis and that BdCAD3 has a different role in Brachypodium. All CAD enzymes are cytosolic except for BdCAD4, which has a putative chloroplast signal peptide adding to the diversity of CAD functions.
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