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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

Grabar Branilović, Marina ; Smolko, Ana ; Šupljika, Filip ; Salopek-Sondi, Branka ; Piantanida, Ivo ; Tomić, Sanja The active site structure of manganese-containing Brassica rapa auxin-amidohydrolase BrILL2 // Acta crystallographica. Section A, Foundations and advances. 2015. str. 210-210 doi: 10.1107/S2053273315096849

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

Poveznice
Indeksiranost