Analysis of PET degrading enzymes by bioinfomatic tools
Конференцијски прилог (Објављена верзија)
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PET hydrolases are enzymes that have been shown to act upon PET as a substrate. Theseenzymes usually adopt an α/β hydrolase fold and are from the classes of esterases, lipases,cutinases, and hydrolases.Here, we have done sequence alignment by ClustalW of the sequences corresponding tothe entries available in the PAZy database (pazy.eu) with the addition of a highly efficientI. sakaiensis PETase mutant W159H/S238F and analyzed the results. The aligned sequencesincluded several different well-aligned segments, which were as follows: 18 single-amino acidsegments, 13 two-amino acid segments, 10 three-amino-acid segments, 1 four-amino acidsegment, 1 six-amino acid segment and 1 eight-amino acid segment. Additionally, at position238, which is adjacent to a highly conserved His237, the most common amino acids wereF,T, S, Y, W, L and G, whereas at position 159, the most common amino acids were W, H, I andL, flanked by a conserved three- and eight-amino acid region. These positions seem to becr...itical for the improvement of the PET hydrolytic activity based on the comparison ofI. sakaiensis PETase mutant W159H/S238F and wt enzyme.Using AlphaFold 2.0 we have predicted the structures of all enzymes available in the databasewhose structures haven't been previously reported and the presence of the α/β hydrolasemotif has been observed. The sequences were also analyzed by SIAS (imed.med.ucm.es).
Кључне речи:
Recombinant technology / PET hydrolase / SIAS / ClustalW / PAZy / AlphaFold 2.0 / PETaseИзвор:
Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference, 2023Издавач:
- European federation of biotechnology
- Asian federation of biotechnology
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200288 (Иновациони центар Хемијског факултета у Београду доо) (RS-MESTD-inst-2020-200288)
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Hemijski fakultet / Faculty of ChemistryTY - CONF AU - Savić, Aleksa D. AU - Stefanović, Marija AU - Slović, Filip AU - Radosavljević, Jelena PY - 2023 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5972 AB - PET hydrolases are enzymes that have been shown to act upon PET as a substrate. Theseenzymes usually adopt an α/β hydrolase fold and are from the classes of esterases, lipases,cutinases, and hydrolases.Here, we have done sequence alignment by ClustalW of the sequences corresponding tothe entries available in the PAZy database (pazy.eu) with the addition of a highly efficientI. sakaiensis PETase mutant W159H/S238F and analyzed the results. The aligned sequencesincluded several different well-aligned segments, which were as follows: 18 single-amino acidsegments, 13 two-amino acid segments, 10 three-amino-acid segments, 1 four-amino acidsegment, 1 six-amino acid segment and 1 eight-amino acid segment. Additionally, at position238, which is adjacent to a highly conserved His237, the most common amino acids wereF,T, S, Y, W, L and G, whereas at position 159, the most common amino acids were W, H, I andL, flanked by a conserved three- and eight-amino acid region. These positions seem to becritical for the improvement of the PET hydrolytic activity based on the comparison ofI. sakaiensis PETase mutant W159H/S238F and wt enzyme.Using AlphaFold 2.0 we have predicted the structures of all enzymes available in the databasewhose structures haven't been previously reported and the presence of the α/β hydrolasemotif has been observed. The sequences were also analyzed by SIAS (imed.med.ucm.es). PB - European federation of biotechnology PB - Asian federation of biotechnology C3 - Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference T1 - Analysis of PET degrading enzymes by bioinfomatic tools UR - https://hdl.handle.net/21.15107/rcub_cherry_5972 ER -
@conference{ author = "Savić, Aleksa D. and Stefanović, Marija and Slović, Filip and Radosavljević, Jelena", year = "2023", abstract = "PET hydrolases are enzymes that have been shown to act upon PET as a substrate. Theseenzymes usually adopt an α/β hydrolase fold and are from the classes of esterases, lipases,cutinases, and hydrolases.Here, we have done sequence alignment by ClustalW of the sequences corresponding tothe entries available in the PAZy database (pazy.eu) with the addition of a highly efficientI. sakaiensis PETase mutant W159H/S238F and analyzed the results. The aligned sequencesincluded several different well-aligned segments, which were as follows: 18 single-amino acidsegments, 13 two-amino acid segments, 10 three-amino-acid segments, 1 four-amino acidsegment, 1 six-amino acid segment and 1 eight-amino acid segment. Additionally, at position238, which is adjacent to a highly conserved His237, the most common amino acids wereF,T, S, Y, W, L and G, whereas at position 159, the most common amino acids were W, H, I andL, flanked by a conserved three- and eight-amino acid region. These positions seem to becritical for the improvement of the PET hydrolytic activity based on the comparison ofI. sakaiensis PETase mutant W159H/S238F and wt enzyme.Using AlphaFold 2.0 we have predicted the structures of all enzymes available in the databasewhose structures haven't been previously reported and the presence of the α/β hydrolasemotif has been observed. The sequences were also analyzed by SIAS (imed.med.ucm.es).", publisher = "European federation of biotechnology, Asian federation of biotechnology", journal = "Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference", title = "Analysis of PET degrading enzymes by bioinfomatic tools", url = "https://hdl.handle.net/21.15107/rcub_cherry_5972" }
Savić, A. D., Stefanović, M., Slović, F.,& Radosavljević, J.. (2023). Analysis of PET degrading enzymes by bioinfomatic tools. in Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference European federation of biotechnology.. https://hdl.handle.net/21.15107/rcub_cherry_5972
Savić AD, Stefanović M, Slović F, Radosavljević J. Analysis of PET degrading enzymes by bioinfomatic tools. in Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference. 2023;. https://hdl.handle.net/21.15107/rcub_cherry_5972 .
Savić, Aleksa D., Stefanović, Marija, Slović, Filip, Radosavljević, Jelena, "Analysis of PET degrading enzymes by bioinfomatic tools" in Biotechnology for a circular bioeconomy, 28-29 March 2023, AFOB-EFB Virtual Conference (2023), https://hdl.handle.net/21.15107/rcub_cherry_5972 .