ArticleApplied and environmental microbiology2022
A Novel Actinobacterial Cutinase Containing a Noncatalytic Polymer-Binding Domain.
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Enzymatic Degradation of Polycaprolactone by Cutinase-Producing Bacteria Isolated from Plastic-Contaminated Environments.Applied biochemistry and biotechnology · 2026Article
- The peptidoglycan-binding domain regulates antimycobacterial activity of LysB by affecting its transportation and/or catalytic activity.Communications biology · 2026Article
- Molecular Dynamics Insights into the Biodegradation of Synthetic Polymers byJournal of chemical information and modeling · 2026Article
- Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer.Scientific reports · 2025Article
- Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes inBioengineering (Basel, Switzerland) · 2025Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The single putative cutinase-encoding gene from the genome of Kineococcus radiotolerans SRS30216 was cloned and expressed in Escherichia coli as a secreted fusion protein, designated YebF-KrCUT, where YebF is the extracellular carrier protein. The 294-amino-acid sequence of KrCUT is unique among currently characterized cutinases by having a C-terminal extension that consists of a short (Pro-Thr)-rich linker and a 55-amino-acid region resembling the substrate binding domain of poly(hydroxybutyrate) (PHB) depolymerases. Phylogenetically, KrCUT takes a unique position among known cutinases and cutinase-like proteins of bacterial and fungal origins. A modeled structure of KrCUT, although displaying a typical α/β hydrolase fold, shows some unique loops close to the catalytic site. The 39-kDa YebF-KrCUT fusion protein and a truncated variant thereof were purified to electrophoretic homogeneity and functionally characterized. The melting temperatures (
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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.