Biochemical and molecular characterization of a quercetinase from Penicillium olsonii

Tranchimand, Sylvain; Ertel, Gisela; Gaydou, Vincent; Gaudin, Christian; Tron, Thierry; Iacazio, Gilles

doi:10.1016/j.biochi.2007.12.004

Cited by 32 publications

(66 citation statements)

References 38 publications

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“…The lowest K m (in the micromolar range) are found for flavonols bearing one or two hydroxy substitutions on ring A (7-OH and 5,7-diOH) and none, one or two hydroxy substitutions on ring B (4 0 -OH and 3 0 ,4 0 -diOH). Similar conclusions could be drawn from a recent study on purified P. olsonii quercetinase (Tranchimand et al 2008). In the latter the nitrogen equivalent of flavonol (i.e.…”

Section: Substrate Specificitysupporting

confidence: 81%

“…The inhibition caused by ethylxanthate was found to be competitive (K i = 2.7 9 10 -7 M). Using purified A. niger quercetinase similar results were obtained with the first three inhibitors listed above (Hund et al 1999) and DDC inhibited totally P. olsonii quercetinase at 100 nM concentration (Tranchimand et al 2008). With A. flavus quercetinase, nitrogen bases with chelating capacities such as 8-hydroxy quinoline, o-phenantroline and a,a 0 -dipyridyl were found more potent inhibitors that non-chelating bases such as a-naphtoquinoline, quinoline and pyridine .…”

Section: Quercetinase Inhibitionmentioning

confidence: 62%

“…of copper found by atomic absorption spectroscopy (Kooter et al 2002). Recently, using the same technique, a copper content of 0.9 ± 0.1 atom per monomer was found for P. olsonii quercetinase (Tranchimand et al 2008). Thus actually mould quercetinases are thought to all have one cuprous ion per molecule as cofactor.…”

Section: Metal Contentmentioning

confidence: 96%

“…Purification and characterisation of the enzyme Up to date the purification and characterisation of five mould quercetinases [A. flavus , A. niger (Hund et al 1999), P. decumbens (Mamma et al 2004), A. japonicus (Fusetti et al 2002;Kooter et al 2002) and P. olsonii (Tranchimand et al 2008)] have been reported. The enzyme is easily purified by classical chromatographic procedures (ion exchange chromatography and gel filtration).…”

Section: Products Of the Reactionmentioning

confidence: 99%

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The rutin catabolic pathway with special emphasis on quercetinase

Tranchimand¹,

Brouant²,

Iacazio³

2010

Biodegradation

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The aim of this review is to give a general account on the oxidative microbial degradation of flavonols. Since now 50 years, various research groups have deciphered the way microorganisms aerobically deal with this important class of flavonoids. Flavonols such as rutin and quercetin are abundantly found in vegetal tissues and exudates, and it was thus patent that various microorganisms will bear the enzymatic machinery necessary to cope with these vegetal secondary metabolites. After initial studies focussed on the general metabolic capacity of various microorganisms towards flavonols, the so called rutin catabolic pathway was rapidly established in moulds. Enzymes of the path as well as substrates and products were known at the beginning of the seventies. Then during 30 years, only sporadic studies were focused on this pathway, before a new burst of interest at the beginning of the new century arose with structural, genomic and theoretical studies mainly conducted towards quercetinase. This is the goal of this work to relate this 50 years journey at the crossroads of microbiology, biochemistry, genetic and chemistry. Some mention of the potential usefulness of the enzymes of the path as well as micro-organisms bearing the whole rutin catabolic pathway is also discussed.

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Section: Substrate Specificitysupporting

confidence: 81%

Section: Quercetinase Inhibitionmentioning

confidence: 62%

Section: Metal Contentmentioning

confidence: 96%

Section: Products Of the Reactionmentioning

confidence: 99%

See 2 more Smart Citations

The rutin catabolic pathway with special emphasis on quercetinase

Tranchimand¹,

Brouant²,

Iacazio³

2010

Biodegradation

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“…The reactivity of quercetinases from Aspergillus japonicus, other Aspergillus species, and Penicillium olsonii depends on a mononuclear Cu II center (49,61,70,95,122). In the crystal structure of quercetinase of A. japonicus, the copper ion is mainly coordinated by three His residues and a water molecule in a distorted tetrahedral geometry; in a minor form, the metal is penta-coordinated by three His, a glutamate, and an aquo ligand in a trigonal bipyramidal geometry.…”

Section: Flavonol 24-dioxygenases (Quercetinases)mentioning

confidence: 99%

Ring-Cleaving Dioxygenases with a Cupin Fold

Fetzner

2012

Appl Environ Microbiol

166

141

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ABSTRACTRing-cleaving dioxygenases catalyze key reactions in the aerobic microbial degradation of aromatic compounds. Many pathways converge to catecholic intermediates, which are subject toorthoormetacleavage by intradiol or extradiol dioxygenases, respectively. However, a number of degradation pathways proceed via noncatecholic hydroxy-substituted aromatic carboxylic acids like gentisate, salicylate, 1-hydroxy-2-naphthoate, or aminohydroxybenzoates. The ring-cleaving dioxygenases active toward these compounds belong to the cupin superfamily, which is characterized by a six-stranded β-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. Most cupin-type ring cleavage dioxygenases use an FeIIcenter for catalysis, and the proposed mechanism is very similar to that of the canonical (type I) extradiol dioxygenases. The metal ion is presumed to act as an electron conduit for single electron transfer from the metal-bound substrate anion to O2, resulting in activation of both substrates to radical species. The family of cupin-type dioxygenases also involves quercetinase (flavonol 2,4-dioxygenase), which opens up two C-C bonds of the heterocyclic ring of quercetin, a wide-spread plant flavonol. Remarkably, bacterial quercetinases are capable of using different divalent metal ions for catalysis, suggesting that the redox properties of the metal are relatively unimportant for the catalytic reaction. The major role of the active-site metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer. The tentative hypothesis that quercetinase catalysis involves direct electron transfer from metal-bound flavonolate to O2is supported by model chemistry.

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Biological Aspects of Metal Enolates

Ming

2010

Patai's Chemistry of Functional Groups

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Biochemical and molecular characterization of a quercetinase from Penicillium olsonii

Cited by 32 publications

References 38 publications

The rutin catabolic pathway with special emphasis on quercetinase

The rutin catabolic pathway with special emphasis on quercetinase

Ring-Cleaving Dioxygenases with a Cupin Fold

Biological Aspects of Metal Enolates

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