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Quercetin 2,3-dioxygenase
Known as:
quercetinase
National Institutes of Health
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1 relation
Broader (1)
Dioxygenases
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
The Behavior of Trispyrazolylborato-Metal(II)-Flavonolate Complexes as Functional Models for Bacterial Quercetinase-Assessment of the Metal Impact.
S. Hoof
,
C. Limberg
Inorganic Chemistry
2019
Corpus ID: 202406857
A series of five compounds TpMesMFla (TpMes = hydrotris(3-mesityl)pyrazolylborate; M = Mn, Fe, Co, Ni, Zn; Fla = 3…
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2009
2009
Theoretical investigations of the role played by quercetinase enzymes upon the flavonoids oxygenolysis mechanism.
S. Antonczak
,
S. Fiorucci
,
J. Golebiowski
,
D. Cabrol-Bass
Physical Chemistry, Chemical Physics - PCCP
2009
Corpus ID: 27516820
Quercetinase enzymatic activity consists in the addition of dioxygen onto flavonoids, some natural polyphenol compounds, leading…
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2008
2008
Biochemical and molecular characterization of a quercetinase from Penicillium olsonii.
S. Tranchimand
,
Gisela Ertel
,
V. Gaydou
,
C. Gaudin
,
T. Tron
,
G. Iacazio
Biochimie
2008
Corpus ID: 205994127
2006
2006
Molecular simulations reveal a new entry site in quercetin 2,3‐dioxygenase. A pathway for dioxygen?
S. Fiorucci
,
J. Golebiowski
,
D. Cabrol-Bass
,
S. Antonczak
Proteins: Structure, Function, and Bioinformatics
2006
Corpus ID: 28491374
Molecular dynamics simulations performed on quercetin 2,3‐dioxygenase have shown the existence of a channel linking the bulk…
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2004
2004
Evidence for a new metal in a known active site: purification and characterization of an iron-containing quercetin 2,3-dioxygenase from Bacillus subtilis.
B. M. Barney
,
Matthew R. Schaab
,
R. Lobrutto
,
W. A. Francisco
Protein Expression and Purification
2004
Corpus ID: 31268108
1982
1982
A study of the mechanism of quercetin oxygenation by 18O labelling. A comparison of the mechanism with that of haem degradation.
S. B. Brown
,
V. Rajananda
,
J. Holroyd
,
E. Evans
Biochemical Journal
1982
Corpus ID: 31315414
The mechanism of quercetin oxygenation, which is formally analogous to haem degradation, was studied by using 18O labelling. In…
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Highly Cited
1972
Highly Cited
1972
Degradation of rutin by Aspergillus flavus. Studies on specificity, inhibition, and possible reaction mechanism of quercetinase.
T. Oka
,
F. J. Simpson
,
H. Krishnamurty
Canadian Journal of Microbiology (print)
1972
Corpus ID: 23701889
The dioxygenase produced by Aspergillus flavus that oxidizes quercetin contains 2 moles of copper per mole of enzyme and binds at…
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1972
1972
Degradation of rutin by Aspergillus flavus. Quercetinase: isolation of a low molecular-weight form containing less carbohydrate.
T. Oka
,
F. J. Simpson
Canadian Journal of Microbiology (print)
1972
Corpus ID: 23096740
Previous work indicated that quercetinase (a flavonol 2,4-dioxygenase) is a glycoprotein with a molecular weight of 111 000…
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Highly Cited
1971
Highly Cited
1971
Quercetinase, a dioxygenase containing copper.
T. Oka
,
F. J. Simpson
Biochemical and Biophysical Research…
1971
Corpus ID: 30088324
1971
1971
Degradation of rutin by Aspergillus flavus. Purification of the dioxygenase, querecentinase.
T. Oka
,
F. J. Simpson
,
J. J. Child
,
C. Mills
Canadian Journal of Microbiology (print)
1971
Corpus ID: 22537279
Evidence is presented that a single enzyme, quercetinase, is responsible for the degradation of quercetin by Aspergillus flavus…
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