Naslov
The active site structure of manganese-containing Brassica rapa auxin-amidohydrolase BrILL2

Autori
Grabar Branilović, Marina ; Smolko, Ana ; Šupljika, Filip ; Salopek-Sondi, Branka ; Piantanida, Ivo ; Tomić, Sanja

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

Izvornik
29th European Crystallographic Meeting, Book of Abstracts, Acta Crystallographica A, 71 / - , 2015, 210-210

Skup
The 29th European Crystallographic Meeting

Mjesto i datum
Rovinj, Hrvatska, 23.08.2015. - 28.08.2015

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
auxin-amidohydrolase ; Brassica rapa ; manganese ions ; Cys ; interdisciplinary study

Sažetak
Auxin-amidohydrolase from Brassica rapa (Br), BrILL2, belongs to the M20D metallopeptidase subfamily, related to the amidohydrolase superfamily (M20) of enzymes which hydrolyze a number of different substrates, including amino acids, sugars, nucleic acids, and organophosphate esters. BrILL2 is catalytically the most efficient auxin-amidohydrolase from Br, playing a key role in homeostasis of the plant hormone auxin in a way to hydrolases amino acid conjugates (AACs) of auxins (IAA, IBA, IPA). A large concentration of free auxins, of which the most common is indole-3- acetic acid (IAA), is toxic for plants, so only about 5% of the total concentration of auxin molecules in plants is in the free (active) form, while the rest is stored in inactive forms, mostly as amino acid and sugar conjugates. In order to hydrolyze the amide bond of amino acid conjugated auxins (inactive, torage forms), and release the free auxin, BrILL needs manganese. The aim of our research was to determine number of the manganese ions, Mn2+, in the enzyme active site, and the influence of Cys to Ser mutations on the protein structure and activity. In order to fulfil this aim we conducted an interdisciplinary study combining different experimental and computational approaches: biochemical, spectroscopic, calorimetric and computational.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Kemija, Biologija

POVEZANOST RADA