Biochemical and molecular characterization of a quercetinase from Penicillium olsonii

Biochimie
Sylvain TranchimandGilles Iacazio

Abstract

Quercetinase (quercetin 2,3-dioxygenase, EC 1.13.11.24) is produced by various filamentous fungi when grown on rutin as the sole carbon and energy source. From a rutin based liquid culture of Penicillium olsonii, we purified a quercetinase with a specific activity of 175U mg(-1). The enzyme is a monomeric glycoprotein of approximately 55 kDa, containing 0.9+/-0.1 copper atoms per protein. Its substrate specificity is restricted to the flavonol family of flavonoids. It is completely inhibited by diethyldithiocarbamate at a concentration of 100 nM and 1H-2-benzyl-3-hydroxy-4-oxoquinolin is a competitive inhibitor with a K(I) of 4 microM. The cDNA poquer1 was cloned and sequenced. It encodes a 365 amino acids long enzyme with a strong sequence identity with the Aspergillus japonicus quercetinase (Q7SIC2). Like the enzyme from A. japonicus, only one of the two cupin domains of the Penicillium olsonii quercetinase is able to bind a metal atom.

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Citations

Apr 27, 2010·Biodegradation·Sylvain TranchimandGilles Iacazio
Feb 26, 2009·Physical Chemistry Chemical Physics : PCCP·Serge AntonczakDaniel Cabrol-Bass
Jan 31, 2012·Applied and Environmental Microbiology·Susanne Fetzner
Mar 5, 2014·Chemical Reviews·Edward I SolomonLi Tian
Feb 25, 2015·Biotechnology Advances·Marcel KarabinPavel Dostalek
Aug 7, 2008·FEMS Microbiology Letters·Hedda Merkens, Susanne Fetzner
Jul 22, 2017·Chemical Reviews·Aditi R DeshpandeDagmar Ringe
Jun 6, 2018·Physical Chemistry Chemical Physics : PCCP·Wen-Juan WangRong-Zhen Liao
May 23, 2019·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Hyunuk Eom, Woon Ju Song
May 18, 2021·Frontiers in Plant Science·Nathaniel M WestrickMehdi Kabbage

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