ArticleBiotechnology and bioengineering2022
Structure-function analysis of two closely related cutinases from Thermobifida cellulosilytica.
Article in Biotechnology and bioengineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- Reporter Group-Labeled Synthetic Cellulose: Structural Characterization and Utilization in Mapping the Cellulose Chain-Cleavage Modes of Cellulases.Biomacromolecules · 2026Article
- Comparison of Polyethylene Terephthalate (PET) Degrading Cutinases from Bacteria and Fungi: Structural Characterization and Molecular Docking Analysis.Applied biochemistry and biotechnology · 2025Article
- Discovery of two novel cutinases from a gut yeast of plastic-eating mealworm for polyester depolymerization.Applied and environmental microbiology · 2025Article
- Perspectives on the microorganisms with the potentials of PET-degradation.Frontiers in microbiology · 2025Review
- Exploring biodegradable alternatives: microorganism-mediated plastic degradation and environmental policies for sustainable plastic management.Archives of microbiology · 2024Review
- Characterization and engineering of plastic-degrading polyesterases jmPE13 and jmPE14 fromFrontiers in bioengineering and biotechnology · 2024Article
- Construction of Fusion Protein with Carbohydrate-Binding Module and Leaf-Branch Compost Cutinase to Enhance the Degradation Efficiency of Polyethylene Terephthalate.International journal of molecular sciences · 2023Article
- Mechanism-Based Design of Efficient PET Hydrolases.ACS catalysis · 2022Review
- Structure-function analysis of two closely related cutinases from Thermobifida cellulosilytica.Biotechnology and bioengineering · 2022Article
- Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.Frontiers in bioengineering and biotechnology · 2022Article
- Catalytic Features and Thermal Adaptation Mechanisms of a Deep Sea Bacterial Cutinase-Type Poly(Ethylene Terephthalate) Hydrolase.Frontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cutinases can play a significant role in a biotechnology-based circular economy. However, relatively little is known about the structure-function relationship of these enzymes, knowledge that is vital to advance optimized, engineered enzyme candidates. Here, two almost identical cutinases from Thermobifida cellulosilytica DSM44535 (Thc_Cut1 and Thc_Cut2) with only 18 amino acids difference were used for a rigorous biochemical characterization of their ability to hydrolyze poly(ethylene terephthalate) (PET), PET-model substrates, and cutin-model substrates. Kinetic parameters were compared with detailed in silico docking studies of enzyme-ligand interactions. The two enzymes interacted with, and hydrolyzed PET differently, with Thc_Cut1 generating smaller PET-degradation products. Thc_Cut1 also showed higher catalytic efficiency on long-chain aliphatic substrates, an effect likely caused by small changes in the binding architecture. Thc_Cut2, in contrast, showed improved binding and catalytic efficiency when approaching the glass transition temperature of PET, an effect likely caused by longer amino acid residues in one area at the enzyme's surface. Finally, the position of the single residue Q93 close to the active site, rotated out in Thc_Cut2, influenced the ligand position of a trimeric PET-model substrate. In conclusion, we illustrate that even minor sequence differences in cutinases can affect their substrate binding, substrate specificity, and catalytic efficiency drastically.
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