Reference on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, I.; Max, N.; Fetzner, S.; Lingens, F.
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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
Eur. J. Biochem.
240
576-583
1996
Arthrobacter sp., Arthrobacter sp. Ru61a
Bauer, I.; de Beyer, A.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarboxylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline
FEMS Microbiol. Lett.
117
299-304
1994
Arthrobacter sp., Arthrobacter sp. Ru61a
-
Fischer, F.; Kunne, S.; Fetzner, S.
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases
J. Bacteriol.
181
5725-5733
1999
Arthrobacter sp.
Frerichs-Deeken, U.; Ranguelova, K.; Kappl, R.; Huettermann, J.; Fetzner, S.
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
Biochemistry
43
14485-14499
2004
Paenarthrobacter ilicis, Paenarthrobacter ilicis Ru61a
Frerichs-Deeken, U.; Fetzner, S.
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
Curr. Microbiol.
51
344-352
2005
Paenarthrobacter nitroguajacolicus (Q7WSQ7), Paenarthrobacter nitroguajacolicus R61a (Q7WSQ7), Paenarthrobacter nitroguajacolicus R-61a (Q7WSQ7)
Steiner, R.A.; Frerichs-Deeken, U.; Fetzner, S.
Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rue61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily
Acta Crystallogr. Sect. F
63
382-385
2007
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R61a, Paenarthrobacter nitroguajacolicus Rue61a
Boehm, K.; Guddorf, J.; Albers, A.; Kamiyama, T.; Fetzner, S.; Hinz, H.
Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism
Biochemistry
47
7116-7126
2008
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus (Q7WSQ7), Paenarthrobacter nitroguajacolicus R61a (Q7WSQ7), Paenarthrobacter nitroguajacolicus R-61a
Beermann, B; Guddorf, J.; Boehm, K.; Albers, A.; Kolkenbrock, S.; Fetzner, S.; Hinz, H.-J.
Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Biochemistry
46
4241-4249
2007
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R61a
Pietra, F.
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations
Chem. Biodivers.
11
861-871
2014
Paenarthrobacter nitroguajacolicus (O31266)
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