Naslov
Esterase active site-inspired design of short catalytic peptides

Autori
Kalafatovic, Daniela

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Skup
EMBO Workshop "Designing functional biomolecular assemblies: Beyond biology"

Mjesto i datum
Bled, Slovenija; online, 28.09.2021. - 01.10.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
catalytic peptides

Sažetak
To accelerate the discovery of new catalytic peptides, we searched for patterns in existing data by statistically analysing 96 esterases (EC 3.1 Hydrolases acting on ester bonds). In this process, 23 enzymes with known catalytic triads were selected for further evaluation. The analysis of angles and distances between the triad members using molecular dynamics and PDB crystallography showed highly conserved site geometries. Based on the primary structure of the selected enzymes, the composition profiles were created for: (1) the full sequence, (2) the “long active site” including the residues between the first and the last active amino acid and (3) the “short active site” containing only active residues (catalytic triad and oxyanion hole). The results showed that shortening the sequence is challenging for the EC3.1 category because the active site residues are spaced-out throughout the sequence.

Izvorni jezik
Engleski

POVEZANOST RADA