8ian: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ian FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ian OCA], [https://pdbe.org/8ian PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ian RCSB], [https://www.ebi.ac.uk/pdbsum/8ian PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ian ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ian FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ian OCA], [https://pdbe.org/8ian PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ian RCSB], [https://www.ebi.ac.uk/pdbsum/8ian PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ian ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
Using enzymes to hydrolyze and recycle poly(ethylene terephthalate) (PET) is an attractive eco-friendly approach to manage the ever-increasing PET wastes, while one major challenge to realize the commercial application of enzyme-based PET degradation is to establish large-scale production methods to produce PET hydrolytic enzyme. To achieve this goal, we exploited the industrial strain Pichia pastoris to express a PET hydrolytic enzyme from Caldimonas taiwanensis termed CtPL-DM. In contrast to the protein expressed in Escherichia coli, CtPL-DM expressed in P. pastoris is inactive in PET degradation. Structural analysis indicates that a putative N-glycosylation site N181 could restrain the conformational change of a substrate-binding Trp and hamper the enzyme action. We thus constructed N181A to remove the N-glycosylation and found that the PET hydrolytic activity of this variant was restored. The performance of N181A was further enhanced via molecular engineering. These results are of valuable in terms of PET hydrolytic enzyme production in industrial strains in the future. | |||
Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris.,Li X, Shi B, Huang JW, Zeng Z, Yang Y, Zhang L, Min J, Chen CC, Guo RT Bioresour Bioprocess. 2023 Apr 6;10(1):26. doi: 10.1186/s40643-023-00648-1. PMID:38647782<ref>PMID:38647782</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 8ian" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 15:02, 30 October 2024
Crystal structure of CtPL-H210S/F214I mutantCrystal structure of CtPL-H210S/F214I mutant
Structural highlights
Publication Abstract from PubMedUsing enzymes to hydrolyze and recycle poly(ethylene terephthalate) (PET) is an attractive eco-friendly approach to manage the ever-increasing PET wastes, while one major challenge to realize the commercial application of enzyme-based PET degradation is to establish large-scale production methods to produce PET hydrolytic enzyme. To achieve this goal, we exploited the industrial strain Pichia pastoris to express a PET hydrolytic enzyme from Caldimonas taiwanensis termed CtPL-DM. In contrast to the protein expressed in Escherichia coli, CtPL-DM expressed in P. pastoris is inactive in PET degradation. Structural analysis indicates that a putative N-glycosylation site N181 could restrain the conformational change of a substrate-binding Trp and hamper the enzyme action. We thus constructed N181A to remove the N-glycosylation and found that the PET hydrolytic activity of this variant was restored. The performance of N181A was further enhanced via molecular engineering. These results are of valuable in terms of PET hydrolytic enzyme production in industrial strains in the future. Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris.,Li X, Shi B, Huang JW, Zeng Z, Yang Y, Zhang L, Min J, Chen CC, Guo RT Bioresour Bioprocess. 2023 Apr 6;10(1):26. doi: 10.1186/s40643-023-00648-1. PMID:38647782[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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