ArticleMolecular biotechnology2017
Ability of T1 Lipase to Degrade Amorphous P(3HB): Structural and Functional Study.
Article in Molecular biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Biodegradable plastics: mechanisms of degradation and generated bio microplastic impact on soil health.Biodegradation · 2024Review
- Knotting terminal ends of mutant T1 lipase with disulfide bond improved structure rigidity and stability.Applied microbiology and biotechnology · 2023Article
- Polymer-Degrading Enzymes ofInternational journal of molecular sciences · 2023Article
- Characterization of Polymer Degrading Lipases, LIP1 and LIP2 FromFrontiers in bioengineering and biotechnology · 2022Article
- Comparative Genomics of Marine Bacteria from a Historically Defined Plastic Biodegradation Consortium with the Capacity to Biodegrade Polyhydroxyalkanoates.Microorganisms · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An enzyme with broad substrate specificity would be an asset for industrial application. T1 lipase apparently has the same active site residues as polyhydroxyalkanoates (PHA) depolymerase. Sequences of both enzymes were studied and compared, and a conserved lipase box pentapeptide region around the nucleophilic serine was detected. The alignment of 3-D structures for both enzymes showed their active site residues were well aligned with an RMSD value of 1.981 Å despite their sequence similarity of only 53.8%. Docking of T1 lipase with P(3HB) gave forth high binding energy of 5.4 kcal/mol, with the distance of 4.05 Å between serine hydroxyl (OH) group of TI lipase to the carbonyl carbon of the substrate, similar to the native PhaZ7
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Registered trials
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