The active site structure of manganese-containing Brassica rapa auxin-amidohydrolase BrILL2 (CROSBI ID 627475)
Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Grabar Branilović, Marina ; Smolko, Ana ; Šupljika, Filip ; Salopek-Sondi, Branka ; Piantanida, Ivo ; Tomić, Sanja
engleski
The active site structure of manganese-containing Brassica rapa auxin-amidohydrolase BrILL2
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.
auxin-amidohydrolase ; Brassica rapa ; manganese ions ; Cys ; interdisciplinary study
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Podaci o prilogu
210-210.
2015.
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objavljeno
10.1107/S2053273315096849
Podaci o matičnoj publikaciji
Acta crystallographica. Section A, Foundations and advances
2053-2733
Podaci o skupu
The 29th European Crystallographic Meeting
poster
23.08.2015-28.08.2015
Rovinj, Hrvatska
Povezanost rada
Fizika, Kemija, Biologija