Works (1)

Updated: July 5th, 2023 15:51

2009 journal article

X-ray structure of ILL2, an auxin-conjugate amidohydrolase from Arabidopsis thaliana


By: E. Bitto*, C. Bingman*, L. Bittova*, N. Houston n, R. Boston n, B. Fox*, G. Phillips*

author keywords: M20D peptidase family; auxin homeostasis; metalloenzyme; X-ray structure
MeSH headings : Amidohydrolases / chemistry; Animals; Arabidopsis / enzymology; Arabidopsis Proteins / chemistry; Bacterial Proteins / chemistry; Binding Sites; Crystallography, X-Ray; Exopeptidases / chemistry; Indoleacetic Acids / chemistry; Metalloproteases / chemistry; Models, Chemical; Protein Structure, Quaternary; Substrate Specificity
TL;DR: The structure of ILL2 suggests that this enzyme likely uses a catalytic mechanism that follows the paradigm established for the other enzymes of the M20 peptidase family, and a hydrophobic pocket nearby the catalytic dimetal center likely recognizes the indolyl moiety of the substrate. (via Semantic Scholar)
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Added: August 6, 2018

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