@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. These
enzymes 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 to
the entries available in the PAZy database (pazy.eu) with the addition of a highly efficient
I. sakaiensis PETase mutant W159H/S238F and analyzed the results. The aligned sequences
included several different well-aligned segments, which were as follows: 18 single-amino acid
segments, 13 two-amino acid segments, 10 three-amino-acid segments, 1 four-amino acid
segment, 1 six-amino acid segment and 1 eight-amino acid segment. Additionally, at position
238, which is adjacent to a highly conserved His237, the most common amino acids were
F,T, S, Y, W, L and G, whereas at position 159, the most common amino acids were W, H, I and
L, flanked by a conserved three- and eight-amino acid region. These positions seem to be
critical for the improvement of the PET hydrolytic activity based on the comparison of
I. sakaiensis PETase mutant W159H/S238F and wt enzyme.
Using AlphaFold 2.0 we have predicted the structures of all enzymes available in the database
whose structures haven't been previously reported and the presence of the α/β hydrolase
motif 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",
pages = "103-103",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5971"
}
