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. Rue61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1

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Eur J Biochem | / 3卷 / 576期

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[1] 2,4-Dioxyenases 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, I
Max, N
Fetzner, S
Lingens, F
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 240 (03): : 576 - 583
[2] Cloning, sequence analysis; and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase
Max, N
Betz, A
Facey, S
Lingens, F
Hauer, B
Fetzner, S
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1999, 1431 (02): : 547 - 552
[3] Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Beermann, Bernd
Guddorf, Jessica
Boehm, Kristian
Albers, Alexander
Kolkenbrock, Stephan
Fetzner, Susanne
Hinz, H. -J.
BIOCHEMISTRY, 2007, 46 (14) : 4241 - 4249
[4] A NOVEL TYPE OF OXYGENOLYTIC RING-CLEAVAGE - 2,4-OXYGENATION AND DECARBONYLATION OF 1H-3-HYDROXY-4-OXOQUINALDINE AND 1H-3-HYDROXY-4-OXOQUINOLINE
BAUER, I
DEBEYER, A
TSHISUAKA, B
FETZNER, S
LINGENS, F
FEMS MICROBIOLOGY LETTERS, 1994, 117 (03) : 299 - 304
[5] Site-directed mutagenesis of potential catalytic residues in 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, and hypothesis on the catalytic mechanism of 2,4-dioxygenolytic ring cleavage
Fischer, F
Fetzner, S
FEMS MICROBIOLOGY LETTERS, 2000, 190 (01) : 21 - 27
[6] Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase:: a cofactor-free oxygenase of the α/β-hydrolase family
Qi, Ruhu
Fetzner, Susanne
Oakley, Aaron J.
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2007, 63 : 378 - 381
[7] Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Ru61a
Betz, A
Facey, SJ
Hauer, B
Tshisuaka, B
Lingens, F
JOURNAL OF BASIC MICROBIOLOGY, 2000, 40 (01) : 7 - 23
[8] Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a:: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily
Steiner, Roberto A.
Frerichs-Deeken, Ursula
Fetzner, Susanne
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2007, 63 : 382 - 385
[9] Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase
Hernandez-Ortega, Aitor
Quesne, Matthew G.
Bui, Soi
Heuts, Dominic P. H. M.
Steiner, Roberto A.
Heyes, Derren J.
de Visser, Sam P.
Scrutton, Nigel S.
JOURNAL OF BIOLOGICAL CHEMISTRY, 2014, 289 (12) : 8620 - 8632
[10] 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, U
Fetzner, S
CURRENT MICROBIOLOGY, 2005, 51 (05) : 344 - 352

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