Site-directed mutagenesis around the CuA site of a polyphenol oxidase from Coreopsis grandiflora (cgAUS1)

Author(s)
Cornelia Kaintz, Rupert L. Mayer, Franz Jirsa, Heidi Halbwirth, Annette Rompel
Abstract

Abstract Aurone synthase from Coreopsis grandiflora (cgAUS1), catalyzing conversion of butein to sulfuretin in a type-3 copper center, is a rare example of a polyphenol oxidase involved in anabolism. Site-directed mutagenesis around the CuA site of AUS1 was performed, and recombinant enzymes were analyzed by mass spectrometry. Replacement of the coordinating CuA histidines with alanine resulted in the presence of a single copper and loss of diphenolase activity. The thioether bridge-building cysteine and a phenylalanine over the CuA site, exchanged to alanine, have no influence on copper content but appear to play an important role in substrate binding.

Organisation(s)
Department of Biophysical Chemistry, Department of Analytical Chemistry, Department of Inorganic Chemistry
External organisation(s)
Technische Universität Wien
Journal
FEBS Letters
Volume
589
Pages
789-797
No. of pages
9
ISSN
0014-5793
DOI
https://doi.org/10.1016/j.febslet.2015.02.009
Publication date
03-2015
Peer reviewed
Yes
Austrian Fields of Science 2012
104004 Chemical biology, 106023 Molecular biology, 103006 Chemical physics
Keywords
ASJC Scopus subject areas
Genetics, Molecular Biology, Biophysics, Structural Biology, Biochemistry, Cell Biology
Portal url
https://ucrisportal.univie.ac.at/en/publications/sitedirected-mutagenesis-around-the-cua-site-of-a-polyphenol-oxidase-from-coreopsis-grandiflora-cgaus1(e89f1cea-72ce-4adf-a41c-4df008c345f5).html