Type : Quinoline
Chemical_Nomenclature : 3-hydroxy-2-methyl-1H-quinolin-4-one
Canonical SMILES : CC1=C(C(=O)C2=CC=CC=C2N1)O
InChI : InChI=1S\/C10H9NO2\/c1-6-9(12)10(13)7-4-2-3-5-8(7)11-6\/h2-5,12H,1H3,(H,11,13)
InChIKey : FSCXZVPPDJYLDD-UHFFFAOYSA-N
Other name(s) : 2-Methylquinoline-3,4-diol, 3-Hydroxy-2-methyl-1H-quinolin-4-one, CHEBI:29216, C06331, QND, 1H-3-hydroxy-4-oxoquinaldine, 1-H-3-hydroxy-4-oxoquinaldine
Families : HOD-cofactorfree-dioxygenase
Title : Evolutionary adaptation from hydrolytic to oxygenolytic catalysis - Bui_2023_bioRxiv__ |
Author(s) : Bui S , Gil-Guerrero S , van der Linden P , Carpentier P , Ceccarelli M , Jambrina PG , Steiner RA |
Ref : Biorxiv , : , 2023 |
Abstract : Bui_2023_bioRxiv__ |
ESTHER : Bui_2023_bioRxiv__ |
PubMedSearch : Bui_2023_bioRxiv__ |
PubMedID: |
Gene_locus related to this paper: artsp-hod |
Title : Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC, a mycobacterial dioxygenase of the alpha\/beta-hydrolase fold family - Wullich_2019_J.Struct.Biol_207_287 |
Author(s) : Wullich SC , Kobus S , Wienhold M , Hennecke U , Smits SHJ , Fetzner S |
Ref : J Struct Biol , 207 :287 , 2019 |
Abstract : Wullich_2019_J.Struct.Biol_207_287 |
ESTHER : Wullich_2019_J.Struct.Biol_207_287 |
PubMedSearch : Wullich_2019_J.Struct.Biol_207_287 |
PubMedID: 31228546 |
Gene_locus related to this paper: mycab-x8en65 |
Title : Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue - Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
Author(s) : Hernandez-Ortega A , Quesne MG , Bui S , Heuts DP , Steiner RA , Heyes DJ , de Visser SP , Scrutton NS |
Ref : Journal of Biological Chemistry , 289 :8620 , 2014 |
Abstract : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
ESTHER : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
PubMedSearch : Hernandez-Ortega_2014_J.Biol.Chem_289_8620 |
PubMedID: 24482238 |
Gene_locus related to this paper: artsp-hod |
Title : Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha\/beta-hydrolase fold - Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
Author(s) : Steiner RA , Janssen HJ , Roversi P , Oakley AJ , Fetzner S |
Ref : Proc Natl Acad Sci U S A , 107 :657 , 2010 |
Abstract : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
ESTHER : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
PubMedSearch : Steiner_2010_Proc.Natl.Acad.Sci.U.S.A_107_657 |
PubMedID: 20080731 |
Gene_locus related to this paper: artsp-hod , psepu-QDO |
Title : Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase - Beermann_2007_Biochemistry_46_4241 |
Author(s) : Beermann B , Guddorf J , Boehm K , Albers A , Kolkenbrock S , Fetzner S , Hinz HJ |
Ref : Biochemistry , 46 :4241 , 2007 |
Abstract : Beermann_2007_Biochemistry_46_4241 |
ESTHER : Beermann_2007_Biochemistry_46_4241 |
PubMedSearch : Beermann_2007_Biochemistry_46_4241 |
PubMedID: 17371045 |
Title : Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase - Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
Author(s) : Frerichs-Deeken U , Fetzner S |
Ref : Curr Microbiol , 51 :344 , 2005 |
Abstract : Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
ESTHER : Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
PubMedSearch : Frerichs-Deeken_2005_Curr.Microbiol_51_344 |
PubMedID: 16187153 |
Gene_locus related to this paper: artsp-hod |
Title : Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion - Frerichs-Deeken_2004_Biochemistry_43_14485 |
Author(s) : Frerichs-Deeken U , Ranguelova K , Kappl R , Huttermann J , Fetzner S |
Ref : Biochemistry , 43 :14485 , 2004 |
Abstract : Frerichs-Deeken_2004_Biochemistry_43_14485 |
ESTHER : Frerichs-Deeken_2004_Biochemistry_43_14485 |
PubMedSearch : Frerichs-Deeken_2004_Biochemistry_43_14485 |
PubMedID: 15533053 |
Gene_locus related to this paper: artsp-hod |
Title : 2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33\/1 - Bauer_1996_Eur.J.Biochem_240_576 |
Author(s) : Bauer I , Max N , Fetzner S , Lingens F |
Ref : European Journal of Biochemistry , 240 :576 , 1996 |
Abstract : Bauer_1996_Eur.J.Biochem_240_576 |
ESTHER : Bauer_1996_Eur.J.Biochem_240_576 |
PubMedSearch : Bauer_1996_Eur.J.Biochem_240_576 |
PubMedID: 8856057 |
Gene_locus related to this paper: artsp-hod , psepu-QDO |