ArticleThe Journal of biological chemistry2021
Phylogenetic analysis and in-depth characterization of functionally and structurally diverse CE5 cutinases.
Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Phylogenetic analysis of xylan-degrading hemicellulases fromFrontiers in microbiology · 2026Article
- Genomic and Functional Analysis of Carbohydrate Esterases in the Maize PathogenMicroorganisms · 2025Article
- Biochemical Characterization and Polyester-Binding/Degrading Capability of Two Cutinases fromMicroorganisms · 2025Article
- Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes inBioengineering (Basel, Switzerland) · 2025Review
- Review
- The Multifaceted Roles of Fungal Cutinases during Infection.Journal of fungi (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cutinases are esterases that release fatty acids from the apoplastic layer in plants. As they accept bulky and hydrophobic substrates, cutinases could be used in many applications, ranging from valorization of bark-rich side streams to plastic recycling. Advancement of these applications, however, requires deeper knowledge of cutinases' biodiversity and structure-function relationships. Here, we mined over 3000 members from carbohydrate esterase family 5 for putative cutinases and condensed it to 151 genes from known or putative lignocellulose-targeting organisms. The 151 genes were subjected to a phylogenetic analysis, which showed that cutinases with available crystal structures were phylogenetically closely related. We then selected nine phylogenic diverse cutinases for recombinant production and characterized their kinetic activity against para-nitrophenol substrates esterified with consecutively longer alkyl chains (pNP-C
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.