The rutin catabolic pathway with special emphasis on quercetinase

  title={The rutin catabolic pathway with special emphasis on quercetinase},
  author={Sylvain Tranchimand and Pierre Brouant and Gilles Iacazio},
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… 
Cu‐Dependent Quercetin Dioxygenase
In this review article, the available structural and functional information and mechanistic proposals for this unique dioxygenase are explored and discussed.
Structure-dependent modulation of substrate binding and biodegradation activity of Pirin proteins towards plant flavonols.
It is found that both Pirin catalyze the oxidative degradation of a wide spectrum of flavonol analogues, and release carbon monoxide (CO) in the process, which shows that Pirin acts on a broad range of substrates and could represent a novel dietary source of CO in vivo.
Rutinosidase from Aspergillus niger: Crystal structure and insight into the enzymatic activity.
Unexpectedly, quercetin 3-O-glucoside was found to be a better substrate than rutin, and thus AnRut cannot be considered a typical diglycosidase.
Pirin-Like Protein from Pseudomonas stutzeri Zobell:Gene Cloning, Heterologous Expression, and Its Quercetinase Activity
The pirin-like protein of a marine most respected denitrifier bacteria, Pseudomonas stutzeri Zobell, is examined by managing the gene cloning, protein expression, enzyme assay and mutagenesis, with the essential intention in ions dependency by a variety of bimetal compound supplementations and catalytic activity to other flavonols.
Sclerotinia sclerotiorum Circumvents Flavonoid Defenses by Catabolizing Flavonol Glycosides and Aglycones1[OPEN]
Investigating how Sclerotinia sclerotiorum, a necrotrophic fungal pathogen that causes disease in a range of economically important crop species, is able to successfully infect flavonol-rich tissues of Arabidopsis found a quercetin dioxygenase gene (QDO) and characterized the encoded protein, which catalyzed cleavage of the Flavonol carbon skeleton.


Theoretical investigations of the role played by quercetinase enzymes upon the flavonoids oxygenolysis mechanism.
It is proposed here that deformations of the substrate induced by the enzyme could originate the differences in the degradation rates experimentally observed, and the role of the enzyme, in terms of structural and electronic effects, can not be neglected.
The Degradation of Flavonols by Pullularia fermentans var. candida
Flavonols belong to a group of flavonoids which are widely distributed in the plant world mostly as glycosides. Numerous studies have been reported on the chemical nature and distribution of these
A number of molds and bacteria were screened for their ability to degrade quercitrin. The molds, but not the bacteria, were particularly active and produced carbon monoxide. The degradation of
Microbial and enzymatic transformations of flavonoids.
In the present review, biotransformations of numerous flavonoids catalyzed mainly by microbes and few plant enzymes are described in four different flavonoid classes, viz., chalcones, isoflavones, catechins, and flavones.
Elucidation of the Flavonoid Catabolism Pathway in Pseudomonas putida PML2 by Comparative Metabolic Profiling
Comparative metabolic profiling of the compounds in the wild-type and mutant strains allowed us to understand the degradation events and to identify six metabolic intermediates, including the first report on quercetin dehydroxylation in aerobic conditions leading to naringenin accumulation.
Rhizobia catabolize nod gene-inducing flavonoids via C-ring fission mechanisms
The initial structural modification of nod gene-inducing flavonoids by rhizobia can generate chalcones, whose open C-ring system may have implications for the binding of inducers to the nodD gene product.
Biochemical Characterization of the Multi-enzyme System Produced by Penicillium decumbens Grown on Rutin
Penicillium decumbens produced a set of enzymes, including a monoxygenase and two glycosidases, which degrade rutin, a nontoxic flavonoid glycoside, to water-soluble products, which were purified to electrophoretic homogeneity.
Degradation of rutin by Aspergillus flavus. Purification and characterization of rutinase.
Rutinase, after partial purification, is relatively stable when stored at −20 °C, and is most stable and most active at pH 5.6.
Degradation of rutin by Aspergillus flavus. Studies with oxygen 18 on the action of a dioxygenase on quercetin.
The enzyme quercetinase, an oxygenase produced by Aspergillus flavus, yield carbon monoxide and a depside, 2-protocatechuoyl-phloroglucinolcarboxylic acid, which is likely to be a dioxygenase.