8hea: Difference between revisions
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==Esterase2 (EaEst2) from Exiguobacterium antarcticum== | |||
<StructureSection load='8hea' size='340' side='right'caption='[[8hea]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8hea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Exiguobacterium_antarcticum_B7 Exiguobacterium antarcticum B7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HEA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</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> | |||
== 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8hea" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Exiguobacterium antarcticum B7]] | |||
[[Category: Large Structures]] | |||
[[Category: Hwang J]] | |||
[[Category: Lee JH]] | |||
Latest revision as of 17:43, 20 September 2023
Esterase2 (EaEst2) from Exiguobacterium antarcticumEsterase2 (EaEst2) from Exiguobacterium antarcticum
Structural highlights
FunctionPublication Abstract from PubMedThis 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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