-
1
-
-
33745115647
-
The 50th anniversary of the discovery of oxygenases
-
Yamamoto S. The 50th anniversary of the discovery of oxygenases. IUBMB Life 2006, 58:248-250.
-
(2006)
IUBMB Life
, vol.58
, pp. 248-250
-
-
Yamamoto, S.1
-
2
-
-
0345492036
-
Mechanism of aromatic amino acid hydroxylation
-
Fitzpatrick P.F. Mechanism of aromatic amino acid hydroxylation. Biochemistry 2003, 42:14083-14091.
-
(2003)
Biochemistry
, vol.42
, pp. 14083-14091
-
-
Fitzpatrick, P.F.1
-
3
-
-
27544440222
-
Alpha-dioxygenases
-
Hamberg M., Ponce de Leon I., Rodriguez M.J., Castresana C. Alpha-dioxygenases. Biochem Biophys Res Commun 2005, 338:169-174.
-
(2005)
Biochem Biophys Res Commun
, vol.338
, pp. 169-174
-
-
Hamberg, M.1
Ponce de Leon, I.2
Rodriguez, M.J.3
Castresana, C.4
-
4
-
-
80054052917
-
Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease
-
Haeggstrom J.Z., Funk C.D. Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease. Chem Rev 2011, 111:5866-5898.
-
(2011)
Chem Rev
, vol.111
, pp. 5866-5898
-
-
Haeggstrom, J.Z.1
Funk, C.D.2
-
5
-
-
84959227665
-
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases
-
Frandsen K.E., Simmons T.J., Dupree P., Poulsen J.C., Hemsworth G.R., Ciano L., Johnston E.M., Tovborg M., Johansen K.S., von Freiesleben P., et al. The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nat Chem Biol 2016, 12:298-303.
-
(2016)
Nat Chem Biol
, vol.12
, pp. 298-303
-
-
Frandsen, K.E.1
Simmons, T.J.2
Dupree, P.3
Poulsen, J.C.4
Hemsworth, G.R.5
Ciano, L.6
Johnston, E.M.7
Tovborg, M.8
Johansen, K.S.9
von Freiesleben, P.10
-
6
-
-
0347986903
-
Carotene oxygenases: a new family of double bond cleavage enzymes
-
Wyss A. Carotene oxygenases: a new family of double bond cleavage enzymes. J Nutr 2004, 134:246S-250S.
-
(2004)
J Nutr
, vol.134
, pp. 246S-250S
-
-
Wyss, A.1
-
7
-
-
0037358282
-
Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
-
Myllyharju J. Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol 2003, 22:15-24.
-
(2003)
Matrix Biol
, vol.22
, pp. 15-24
-
-
Myllyharju, J.1
-
8
-
-
4644275807
-
Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes
-
Meunier B., de Visser S.P., Shaik S. Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes. Chem Rev 2004, 104:3947-3980.
-
(2004)
Chem Rev
, vol.104
, pp. 3947-3980
-
-
Meunier, B.1
de Visser, S.P.2
Shaik, S.3
-
9
-
-
33750460925
-
Oxygenases and dehalogenases: molecular approaches to efficient degradation of chlorinated environmental pollutants
-
Furukawa K. Oxygenases and dehalogenases: molecular approaches to efficient degradation of chlorinated environmental pollutants. Biosci Biotechnol Biochem 2006, 70:2335-2348.
-
(2006)
Biosci Biotechnol Biochem
, vol.70
, pp. 2335-2348
-
-
Furukawa, K.1
-
10
-
-
0242500462
-
Practical issues in the application of oxygenases
-
van Beilen J.B., Duetz W.A., Schmid A., Witholt B. Practical issues in the application of oxygenases. Trends Biotechnol 2003, 21:170-177.
-
(2003)
Trends Biotechnol
, vol.21
, pp. 170-177
-
-
van Beilen, J.B.1
Duetz, W.A.2
Schmid, A.3
Witholt, B.4
-
12
-
-
34247534094
-
2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
-
2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 2007, 316:453-457.
-
(2007)
Science
, vol.316
, pp. 453-457
-
-
Kovaleva, E.G.1
Lipscomb, J.D.2
-
13
-
-
0043022281
-
Dioxygenase enzymes: catalytic mechanism and chemical models
-
Bugg T.D.H. Dioxygenase enzymes: catalytic mechanism and chemical models. Tetrahedron 2003, 59:7075-7101.
-
(2003)
Tetrahedron
, vol.59
, pp. 7075-7101
-
-
Bugg, T.D.H.1
-
14
-
-
77950626884
-
Cofactor-independent oxidases and oxygenases
-
Fetzner S., Steiner R.A. Cofactor-independent oxidases and oxygenases. Appl Microbiol Biotechnol 2010, 86:791-804.
-
(2010)
Appl Microbiol Biotechnol
, vol.86
, pp. 791-804
-
-
Fetzner, S.1
Steiner, R.A.2
-
15
-
-
76249120623
-
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
-
Steiner R.A., Janssen H.J., Roversi P., Oakley A.J., Fetzner S. Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold. Proc Natl Acad Sci U S A 2010, 107:657-662.
-
(2010)
Proc Natl Acad Sci U S A
, vol.107
, pp. 657-662
-
-
Steiner, R.A.1
Janssen, H.J.2
Roversi, P.3
Oakley, A.J.4
Fetzner, S.5
-
16
-
-
34249084726
-
Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis
-
Widboom P.F., Fielding E.N., Liu Y., Bruner S.D. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 2007, 447:342-345.
-
(2007)
Nature
, vol.447
, pp. 342-345
-
-
Widboom, P.F.1
Fielding, E.N.2
Liu, Y.3
Bruner, S.D.4
-
17
-
-
37049015634
-
Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC
-
Fielding E.N., Widboom P.F., Bruner S.D. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 2007, 46:13994-14000.
-
(2007)
Biochemistry
, vol.46
, pp. 13994-14000
-
-
Fielding, E.N.1
Widboom, P.F.2
Bruner, S.D.3
-
18
-
-
0037439266
-
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
-
Sciara G., Kendrew S.G., Miele A.E., Marsh N.G., Federici L., Malatesta F., Schimperna G., Savino C., Vallone B. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J 2003, 22:205-215.
-
(2003)
EMBO J
, vol.22
, pp. 205-215
-
-
Sciara, G.1
Kendrew, S.G.2
Miele, A.E.3
Marsh, N.G.4
Federici, L.5
Malatesta, F.6
Schimperna, G.7
Savino, C.8
Vallone, B.9
-
19
-
-
35948997680
-
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis
-
Loening A.M., Fenn T.D., Gambhir S.S. Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis. J Mol Biol 2007, 374:1017-1028.
-
(2007)
J Mol Biol
, vol.374
, pp. 1017-1028
-
-
Loening, A.M.1
Fenn, T.D.2
Gambhir, S.S.3
-
20
-
-
13444252278
-
Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole
-
Schultz L.W., Liu L., Cegielski M., Hastings J.W. Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. Proc Natl Acad Sci U S A 2005, 102:1378-1383.
-
(2005)
Proc Natl Acad Sci U S A
, vol.102
, pp. 1378-1383
-
-
Schultz, L.W.1
Liu, L.2
Cegielski, M.3
Hastings, J.W.4
-
21
-
-
84956590341
-
Crystal structure of nanoKAZ: the mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine
-
Tomabechi Y., Hosoya T., Ehara H., Sekine S., Shirouzu M., Inouye S. Crystal structure of nanoKAZ: the mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine. Biochem Biophys Res Commun 2016, 470:88-93.
-
(2016)
Biochem Biophys Res Commun
, vol.470
, pp. 88-93
-
-
Tomabechi, Y.1
Hosoya, T.2
Ehara, H.3
Sekine, S.4
Shirouzu, M.5
Inouye, S.6
-
22
-
-
84922650052
-
Functional and structural characterization of an unusual cofactor-independent oxygenase
-
Baas B.J., Poddar H., Geertsema E.M., Rozeboom H.J., de Vries M.P., Permentier H.P., Thunnissen A.M., Poelarends G.J. Functional and structural characterization of an unusual cofactor-independent oxygenase. Biochemistry 2015, 54:1219-1232.
-
(2015)
Biochemistry
, vol.54
, pp. 1219-1232
-
-
Baas, B.J.1
Poddar, H.2
Geertsema, E.M.3
Rozeboom, H.J.4
de Vries, M.P.5
Permentier, H.P.6
Thunnissen, A.M.7
Poelarends, G.J.8
-
23
-
-
0029767386
-
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 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. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur J Biochem 1996, 240:576-583.
-
(1996)
Eur J Biochem
, vol.240
, pp. 576-583
-
-
Bauer, I.1
Max, N.2
Fetzner, S.3
Lingens, F.4
-
25
-
-
11844304935
-
The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)
-
Gopal B., Madan L.L., Betz S.F., Kossiakoff A.A. The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s). Biochemistry 2005, 44:193-201.
-
(2005)
Biochemistry
, vol.44
, pp. 193-201
-
-
Gopal, B.1
Madan, L.L.2
Betz, S.F.3
Kossiakoff, A.A.4
-
26
-
-
0037168426
-
Crystal structures of anaerobic enzyme·substrate complexes provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
-
Steiner R.A., Kalk K.H., Dijkstra B.W. Crystal structures of anaerobic enzyme·substrate complexes provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc Natl Acad Sci U S A 2002, 99:16625-16630.
-
(2002)
Proc Natl Acad Sci U S A
, vol.99
, pp. 16625-16630
-
-
Steiner, R.A.1
Kalk, K.H.2
Dijkstra, B.W.3
-
27
-
-
0032784276
-
Alpha/beta hydrolase fold enzymes: the family keeps growing
-
Nardini M., Dijkstra B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 1999, 9:732-737.
-
(1999)
Curr Opin Struct Biol
, vol.9
, pp. 732-737
-
-
Nardini, M.1
Dijkstra, B.W.2
-
28
-
-
84946059736
-
Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa quinolone signal degradation and virulence factor attenuation
-
Muller C., Birmes F.S., Ruckert C., Kalinowski J., Fetzner S. Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa quinolone signal degradation and virulence factor attenuation. Appl Environ Microbiol 2015, 81:7720-7729.
-
(2015)
Appl Environ Microbiol
, vol.81
, pp. 7720-7729
-
-
Muller, C.1
Birmes, F.S.2
Ruckert, C.3
Kalinowski, J.4
Fetzner, S.5
-
29
-
-
0344172698
-
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases
-
Fischer F., Künne 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 1999, 181:5725-5733.
-
(1999)
J Bacteriol
, vol.181
, pp. 5725-5733
-
-
Fischer, F.1
Künne, S.2
Fetzner, S.3
-
30
-
-
84943155664
-
How the same core catalytic machinery catalyzes 17 different reactions: the serine-histidine-aspartate catalytic triad of α/β-hydrolase fold enzymes
-
Rauwerdink A., Kazlauskas R.J. How the same core catalytic machinery catalyzes 17 different reactions: the serine-histidine-aspartate catalytic triad of α/β-hydrolase fold enzymes. ACS Catal 2015, 5:6153-6176.
-
(2015)
ACS Catal
, vol.5
, pp. 6153-6176
-
-
Rauwerdink, A.1
Kazlauskas, R.J.2
-
31
-
-
0037210467
-
Oxygenases without requirement for cofactors or metal ions
-
Fetzner S. Oxygenases without requirement for cofactors or metal ions. Appl Microbiol Biotechnol 2002, 60:243-257.
-
(2002)
Appl Microbiol Biotechnol
, vol.60
, pp. 243-257
-
-
Fetzner, S.1
-
32
-
-
8544222809
-
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 U., Ranguelova K., Kappl R., Huttermann 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 2004, 43:14485-14499.
-
(2004)
Biochemistry
, vol.43
, pp. 14485-14499
-
-
Frerichs-Deeken, U.1
Ranguelova, K.2
Kappl, R.3
Huttermann, J.4
Fetzner, S.5
-
33
-
-
84896922255
-
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 A., Quesne M.G., Bui S., Heuts D.P., Steiner R.A., Heyes D.J., de Visser S.P., Scrutton N.S. 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. J Biol Chem 2014, 289:8620-8632.
-
(2014)
J Biol Chem
, vol.289
, pp. 8620-8632
-
-
Hernandez-Ortega, A.1
Quesne, M.G.2
Bui, S.3
Heuts, D.P.4
Steiner, R.A.5
Heyes, D.J.6
de Visser, S.P.7
Scrutton, N.S.8
-
34
-
-
0028108347
-
Activation of molecular oxygen by flavins and flavoproteins
-
Massey V. Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 1994, 269:22459-22462.
-
(1994)
J Biol Chem
, vol.269
, pp. 22459-22462
-
-
Massey, V.1
-
35
-
-
33646348711
-
To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes
-
Mattevi A. To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem Sci 2006, 31:276-283.
-
(2006)
Trends Biochem Sci
, vol.31
, pp. 276-283
-
-
Mattevi, A.1
-
37
-
-
84934957696
-
Catalytic mechanism of cofactor-free dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates
-
Hernandez-Ortega A., Quesne M.G., Bui S., Heyes D.J., Steiner R.A., Scrutton N.S., de Visser S.P. Catalytic mechanism of cofactor-free dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates. J Am Chem Soc 2015, 137:7474-7487.
-
(2015)
J Am Chem Soc
, vol.137
, pp. 7474-7487
-
-
Hernandez-Ortega, A.1
Quesne, M.G.2
Bui, S.3
Heyes, D.J.4
Steiner, R.A.5
Scrutton, N.S.6
de Visser, S.P.7
-
38
-
-
0030663655
-
Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution
-
Colloc'h N., El Hajji M., Bachet B., L'Hermite G., Schiltz M., Prange T., Castro B., Mornon J.P. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat Struct Biol 1997, 4:947-952.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 947-952
-
-
Colloc'h, N.1
El Hajji, M.2
Bachet, B.3
L'Hermite, G.4
Schiltz, M.5
Prange, T.6
Castro, B.7
Mornon, J.P.8
-
39
-
-
0032544185
-
Spectroscopic characterization of intermediates in the urate oxidase reaction
-
Kahn K., Tipton P.A. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 1998, 37:11651-11659.
-
(1998)
Biochemistry
, vol.37
, pp. 11651-11659
-
-
Kahn, K.1
Tipton, P.A.2
-
40
-
-
0037446748
-
General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad
-
Imhoff R.D., Power N.P., Borrok M.J., Tipton P.A. General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad. Biochemistry 2003, 42:4094-4100.
-
(2003)
Biochemistry
, vol.42
, pp. 4094-4100
-
-
Imhoff, R.D.1
Power, N.P.2
Borrok, M.J.3
Tipton, P.A.4
-
41
-
-
84899805626
-
The neutron structure of urate oxidase resolves a long-standing mechanistic conundrum and reveals unexpected changes in protonation
-
Oksanen E., Blakeley M.P., El-Hajji M., Ryde U., Budayova-Spano M. The neutron structure of urate oxidase resolves a long-standing mechanistic conundrum and reveals unexpected changes in protonation. PLOS ONE 2014, 9:e86651.
-
(2014)
PLOS ONE
, vol.9
-
-
Oksanen, E.1
Blakeley, M.P.2
El-Hajji, M.3
Ryde, U.4
Budayova-Spano, M.5
-
42
-
-
84919347015
-
Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase
-
Bui S., von Stetten D., Jambrina P.G., Prange T., Colloc'h N., de Sanctis D., Royant A., Rosta E., Steiner R.A. Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase. Angew Chem Int Ed Engl 2014, 53:13710-13714.
-
(2014)
Angew Chem Int Ed Engl
, vol.53
, pp. 13710-13714
-
-
Bui, S.1
von Stetten, D.2
Jambrina, P.G.3
Prange, T.4
Colloc'h, N.5
de Sanctis, D.6
Royant, A.7
Rosta, E.8
Steiner, R.A.9
-
43
-
-
84899648566
-
Functional relevance of the internal hydrophobic cavity of urate oxidase
-
Colloc'h N., Prange T. Functional relevance of the internal hydrophobic cavity of urate oxidase. FEBS Lett 2014, 588:1715-1719.
-
(2014)
FEBS Lett
, vol.588
, pp. 1715-1719
-
-
Colloc'h, N.1
Prange, T.2
-
44
-
-
84944272891
-
Oxygen diffusion pathways in a cofactor-independent dioxygenase
-
Di Russo N.V., Condurso H.L., Li K., Bruner S.D., Roitberg A.E. Oxygen diffusion pathways in a cofactor-independent dioxygenase. Chem Sci 2015, 6:6341-6348.
-
(2015)
Chem Sci
, vol.6
, pp. 6341-6348
-
-
Di Russo, N.V.1
Condurso, H.L.2
Li, K.3
Bruner, S.D.4
Roitberg, A.E.5
|