Naslov
Structure-dynamics-function relationship of the methylaspartase ammonia-lyase

Autori
Sanader Maršić, Željka ; Lambrughi, Matteo ; Papaleo, Elena ; Saez-Jimenez, Veronica ; Mapelli, Valeria ; Olsson, Lisbeth

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

Skup
Interdisciplinary Endeavour in Technology at Nanoscale, Water and Environment

Mjesto i datum
Split, Hrvatska, 09.10.2019. - 11.10.2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
methylaspartase ammonia-lyase ; molecular dynamics ; green production of adipic acid

Sažetak
Ammonia lyases (AL) are enzymes of interest for the bio-based production of adipic acid that is widely used for nylon production. Using microsecond molecular dynamics, we investigated the conformational changes in the proximity of the active site of a 3-methylaspartate ammonia lyase (MAL). We identified two regulatory structural elements in the MAL structure: the β5-α2 loop and the helix-hairpin-loop subdomain whose rearrangement changes the accessibility of the active site (e.g. from 'closed' to 'open' states). The β5-α2 loop and the helix-hairpin-loop subdomain modulate the formation of tunnels from the protein surface to the substrate binding site, making the active site more accessible to the substrate when they are in an open state. Our data suggest that protein dynamics need to be considered in the design of new AL variants for protein engineering.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biotehnologija

POVEZANOST RADA