ArticleInternational journal of molecular sciences2018
Expression and Interaction Analysis among Saffron ALDHs and Crocetin Dialdehyde.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Montbretia flowers as a source of bioactive crocins: Biotechnology tools and delivery systems.Biotechnology reports (Amsterdam, Netherlands) · 2025Article
- Research progress on the pharmacological activity, biosynthetic pathways, and biosynthesis of crocins.Beilstein journal of organic chemistry · 2024Review
- Fortification and bioaccessibility of saffron apocarotenoids in potato tubers.Frontiers in nutrition · 2022Article
- A New Glycosyltransferase Enzyme from Family 91, UGT91P3, Is Responsible for the Final Glucosylation Step of Crocins in Saffron (International journal of molecular sciences · 2021Article
- Review
- Genome-wide characterization of ALDH Superfamily in Brassica rapa and enhancement of stress tolerance in heterologous hosts by BrALDH7B2 expression.Scientific reports · 2019Article
- Multi-species transcriptome analyses for the regulation of crocins biosynthesis in Crocus.BMC genomics · 2019Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In saffron, the cleavage of zeaxanthin by means of CCD2 generates crocetin dialdehyde, which is then converted by an unknown aldehyde dehydrogenase to crocetin. A proteome from saffron stigma was released recently and, based on the expression pattern and correlation analyses, five aldehyde dehydrogenases (ALDHs) were suggested as possible candidates to generate crocetin from crocetin dialdehydes. We selected four of the suggested ALDHs and analyzed their expression in different tissues, determined their activity over crocetin dialdehyde, and performed structure modeling and docking calculation to find their specificity. All the ALDHs were able to convert crocetin dialdehyde to crocetin, but two of them were stigma tissue-specific. Structure modeling and docking analyses revealed that, in all cases, there was a high coverage of residues in the models. All of them showed a very close conformation, indicated by the low root-mean-square deviation (RMSD) values of backbone atoms, which indicate a high similarity among them. However, low affinity between the enzymes and the crocetin dialdehyde were observed. Phylogenetic analysis and binding affinities calculations, including some ALDHs from
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Registered trials
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