Characterization of the Brassica rapa auxin amido-hydrolase, BrILL2 (CROSBI ID 541264)
Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Savić, Bojana ; Ludwig-Müller, Jutta ; Tomić, Sanja ; Magnus, Volker ; Salopek-Sondi, Branka
engleski
Characterization of the Brassica rapa auxin amido-hydrolase, BrILL2
Reversible conjugation with amino acids is used by plants to adjust endogenous auxin levels as required for concerted growth and development. One of the auxin-amidohydrolases included in this regulatory mechanism, BrILL2, was cloned from Chinese cabbage (Brassica rapa L.) and tested for hydrolytic activity towards conjugates of indole-3-acetic acid. We further characterized the enzyme including substrates such as alanine (Ala) conjugates of indole-3-propionic acid (IPA) and indole-3-butyric acid (IBA), both of which are endogenous auxins. Enzymatic activity of purified BrILL2 was tested in the presence of dithiothreitol and Mn++. Progress of the cleavage reaction was monitored by HPLC using absorbance at 284 nm. IPA-ala was hydrolyzed at the highest rate, followed by IBA-ala and IAA-ala, in this order. The 3D structure of Br-ILL2 was modeled by the program Modeller9v2 using the X-ray structure of IAA-aminoacid hydrolase from Arabidopsis thaliana (PDB_id 1XMB) and the Mn++ binding site was determined. Ligands: IBA-Ala, IPA-ala, IAA-Ala and IPA-Asp were docked into the protein using the AutoDock3.05 program. The most populated binding site was selected as the most probable one. The obtain complexes were neutralized by adding Na+ ions, the systems was solvated in the 8 Å ; ; thick water layer and energy minimized using the program AMBER9. To learn more about the complex stability and the substrate binding site we accomplished a series of molecular dynamics simulations.
Auxin amido-hydrolase; BrILL2; Brassica rapa; Amino acid conjugates; Enzymatic activity
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Podaci o prilogu
P01-065-P01-065.
2008.
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objavljeno
Podaci o matičnoj publikaciji
Physiologia plantarum
Vaughan, Hurry
Oxford: Wiley-Blackwell
0031-9317
Podaci o skupu
XVI Congress of the Federation of European Societies of Plant Biology (FESPB)
poster
17.08.2008-22.08.2008
Tampere, Finska