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| Line 7: |
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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=8hea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hea OCA], [https://pdbe.org/8hea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hea RCSB], [https://www.ebi.ac.uk/pdbsum/8hea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hea 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=8hea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hea OCA], [https://pdbe.org/8hea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hea RCSB], [https://www.ebi.ac.uk/pdbsum/8hea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hea ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [https://www.uniprot.org/uniprot/K0AFS0_EXIAB K0AFS0_EXIAB]
| |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| This study aimed to elucidate the crystal structure and biochemically characterize the carboxylesterase EaEst2, a thermotolerant biocatalyst derived from Exiguobacterium antarcticum, a psychrotrophic bacterium. Sequence and phylogenetic analyses showed that EaEst2 belongs to the Family XIII group of carboxylesterases. EaEst2 has a broad range of substrate specificities for short-chain p-nitrophenyl (pNP) esters, 1-naphthyl acetate (1-NA), and 1-naphthyl butyrate (1-NB). Its optimal pH is 7.0, losing its enzymatic activity at temperatures above 50 degrees C. EaEst2 showed degradation activity toward bis(2-hydroxyethyl) terephthalate (BHET), a polyethylene terephthalate degradation intermediate. We determined the crystal structure of EaEst2 at a 1.74 A resolution in the ligand-free form to investigate BHET degradation at a molecular level. Finally, the biochemical stability and immobilization of a crosslinked enzyme aggregate (CLEA) were assessed to examine its potential for industrial application. Overall, the structural and biochemical characterization of EaEst2 demonstrates its industrial potency as a biocatalyst.
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| Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic Bacterium Exiguobacterium antarcticum.,Hwang J, Yoo W, Shin SC, Kim KK, Kim HW, Do H, Lee JH Int J Mol Sci. 2023 Jul 27;24(15):12022. doi: 10.3390/ijms241512022. PMID:37569396<ref>PMID:37569396</ref>
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|
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 8hea" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
