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1
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0242267926
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Deflavination and reconstitution of flavoproteins
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Hefti M.H., Vervoort J., and van Berkel W.J.H. Deflavination and reconstitution of flavoproteins. Eur J Biochem 270 (2003) 4227-4242
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(2003)
Eur J Biochem
, vol.270
, pp. 4227-4242
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Hefti, M.H.1
Vervoort, J.2
van Berkel, W.J.H.3
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2
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33644689024
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Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8α-N1-histidyl FAD
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The 3D structure of glucooligosaccharide oxidase from Acremonium strictum demonstrates the first known double attachment flavinylation. The glucooligosaccharide oxidase possesses an open carbohydrate-binding groove, enabling the accommodation of higher oligosaccharides. A detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.
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Huang C.H., Lai W.L., Lee M.H., Chen C.J., Vasella A., Tsai Y.C., and Liaw S.H. Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8α-N1-histidyl FAD. J Biol Chem 280 (2005) 38831-38838. The 3D structure of glucooligosaccharide oxidase from Acremonium strictum demonstrates the first known double attachment flavinylation. The glucooligosaccharide oxidase possesses an open carbohydrate-binding groove, enabling the accommodation of higher oligosaccharides. A detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.
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(2005)
J Biol Chem
, vol.280
, pp. 38831-38838
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Huang, C.H.1
Lai, W.L.2
Lee, M.H.3
Chen, C.J.4
Vasella, A.5
Tsai, Y.C.6
Liaw, S.H.7
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3
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33746325823
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Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor
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Winkler A., Hartner F., Kutchan T.M., Glieder A., and Macheroux P. Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor. J Biol Chem 281 (2006) 21276-21285
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J Biol Chem
, vol.281
, pp. 21276-21285
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Winkler, A.1
Hartner, F.2
Kutchan, T.M.3
Glieder, A.4
Macheroux, P.5
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4
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33745229673
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Characterization of the flavin association in hexose oxidase from Chondrus crispus
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Rand T., Qvist K.B., Walter C.P., and Poulsen C.H. Characterization of the flavin association in hexose oxidase from Chondrus crispus. FEBS J 273 (2006) 2693-2703
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(2006)
FEBS J
, vol.273
, pp. 2693-2703
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Rand, T.1
Qvist, K.B.2
Walter, C.P.3
Poulsen, C.H.4
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5
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23944437959
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Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans
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Koetter J.W., and Schulz G.E. Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans. J Mol Biol 352 (2005) 418-428
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(2005)
J Mol Biol
, vol.352
, pp. 418-428
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Koetter, J.W.1
Schulz, G.E.2
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6
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17844393348
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Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein
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Controlled expression of the apoenzyme of monomeric sarcosine oxidase (MSOX) in a riboflavin-dependent Escherichia coli strain. Reconstitution experiments provide evidence for autoflavinylation in a reaction that proceeds via a reduced flavin intermediate and requires only apoMSOX and FAD.
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Hassan-Abdallah A., Bruckner R.C., Zhao G., and Jorns M.S. Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein. Biochemistry 44 (2005) 6452-6462. Controlled expression of the apoenzyme of monomeric sarcosine oxidase (MSOX) in a riboflavin-dependent Escherichia coli strain. Reconstitution experiments provide evidence for autoflavinylation in a reaction that proceeds via a reduced flavin intermediate and requires only apoMSOX and FAD.
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(2005)
Biochemistry
, vol.44
, pp. 6452-6462
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Hassan-Abdallah, A.1
Bruckner, R.C.2
Zhao, G.3
Jorns, M.S.4
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7
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33645244308
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Recent advances in oxygenase-catalyzed biotransformations
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Urlacher V.B., and Schmid R.D. Recent advances in oxygenase-catalyzed biotransformations. Curr Opin Chem Biol 10 (2006) 156-161
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(2006)
Curr Opin Chem Biol
, vol.10
, pp. 156-161
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Urlacher, V.B.1
Schmid, R.D.2
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8
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33747624251
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Non-enzymatic regeneration of nicotinamide and flavin cofactors for monooxygenase catalysis
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Hollmann F., Hofstetter K., and Schmid A. Non-enzymatic regeneration of nicotinamide and flavin cofactors for monooxygenase catalysis. Trends Biotechnol 24 (2006) 163-171
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(2006)
Trends Biotechnol
, vol.24
, pp. 163-171
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Hollmann, F.1
Hofstetter, K.2
Schmid, A.3
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9
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33845964503
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Efficient regeneration of NADPH using an engineered phosphite dehydrogenase
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Johannes T.W., Woodyer R.D., and Zhao H. Efficient regeneration of NADPH using an engineered phosphite dehydrogenase. Biotechnol Bioeng 96 (2006) 18-26
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(2006)
Biotechnol Bioeng
, vol.96
, pp. 18-26
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Johannes, T.W.1
Woodyer, R.D.2
Zhao, H.3
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10
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33745991798
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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
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Reclassification of flavoprotein monooxygenases based on fold and function.
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van Berkel W.J.H., Kamerbeek N.M., and Fraaije M.W. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J Biotechnol 124 (2006) 670-689. Reclassification of flavoprotein monooxygenases based on fold and function.
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(2006)
J Biotechnol
, vol.124
, pp. 670-689
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van Berkel, W.J.H.1
Kamerbeek, N.M.2
Fraaije, M.W.3
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11
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33845205401
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Occurence and biocatalytic potential of carbohydrate oxidases
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van Hellemond E.W., Leferink N.G.H., Heuts D.P.H.M., Fraaije M.W., and van Berkel W.J.H. Occurence and biocatalytic potential of carbohydrate oxidases. Adv Appl Microbiol 60 (2006) 17-54
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(2006)
Adv Appl Microbiol
, vol.60
, pp. 17-54
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van Hellemond, E.W.1
Leferink, N.G.H.2
Heuts, D.P.H.M.3
Fraaije, M.W.4
van Berkel, W.J.H.5
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13
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29044440810
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Applications of oxidoreductases: recent progress
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Xu F. Applications of oxidoreductases: recent progress. Ind Biotechnol 1 (2005) 38-50
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(2005)
Ind Biotechnol
, vol.1
, pp. 38-50
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Xu, F.1
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14
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34047180214
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New frontiers in structural flavoenzymology
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De Colibus L., and Mattevi A. New frontiers in structural flavoenzymology. Curr Opin Struct Biol 16 (2006) 722-728
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(2006)
Curr Opin Struct Biol
, vol.16
, pp. 722-728
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De Colibus, L.1
Mattevi, A.2
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15
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33645986474
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Preparative deracemization of unnatural amino acids
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Description of how flavoprotein oxidases can be used in a chemoenzymatic process to prepare enantiomerically pure l- and d-amino acids in high yield by deracemization of racemic starting materials.
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Fotheringham I., Archer I., Carr R., Speight R., and Turner N.J. Preparative deracemization of unnatural amino acids. Biochem Soc Trans 34 (2006) 287-290. Description of how flavoprotein oxidases can be used in a chemoenzymatic process to prepare enantiomerically pure l- and d-amino acids in high yield by deracemization of racemic starting materials.
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(2006)
Biochem Soc Trans
, vol.34
, pp. 287-290
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Fotheringham, I.1
Archer, I.2
Carr, R.3
Speight, R.4
Turner, N.J.5
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16
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33745012843
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Maximization of production of his-tagged glycine oxidase and its M261 mutant proteins
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Martinez-Martinez I., Navarro-Fernandez J., Lozada-Ramirez J.D., Garcia-Carmona F., and Sanchez-Ferrer A. Maximization of production of his-tagged glycine oxidase and its M261 mutant proteins. Biotechnol Prog 22 (2006) 647-652
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(2006)
Biotechnol Prog
, vol.22
, pp. 647-652
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Martinez-Martinez, I.1
Navarro-Fernandez, J.2
Lozada-Ramirez, J.D.3
Garcia-Carmona, F.4
Sanchez-Ferrer, A.5
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17
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14644432391
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Molecular analysis of the rebeccamycin l-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
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Nishizawa T., Aldrich C.C., and Sherman D.H. Molecular analysis of the rebeccamycin l-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J Bacteriol 187 (2005) 2084-2092
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(2005)
J Bacteriol
, vol.187
, pp. 2084-2092
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Nishizawa, T.1
Aldrich, C.C.2
Sherman, D.H.3
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18
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0344583742
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Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the l-amino oxidase family
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Sobrado P., and Fitzpatrick P.F. Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the l-amino oxidase family. Biochemistry 42 (2003) 13826-13832
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(2003)
Biochemistry
, vol.42
, pp. 13826-13832
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Sobrado, P.1
Fitzpatrick, P.F.2
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19
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33745862395
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Crystal structure and mechanism of human lysine-specific demethylase-1
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Stavropoulos P., Blobel G., and Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol 13 (2006) 626-632
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(2006)
Nat Struct Mol Biol
, vol.13
, pp. 626-632
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Stavropoulos, P.1
Blobel, G.2
Hoelz, A.3
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20
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33746435258
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Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
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The crystal structure of the LSD1-CoREST complex shows an elongated structure with a long stalk connecting the catalytic domain of LSD1 and the CoREST SANT2 domain. The shape and dimension of LSD1-CoREST suggest its bivalent binding to nucleosomes, enabling efficient H3-K4 demethylation.
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Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M., Otwinowski Z., and Yu H. Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell 23 (2006) 377-387. The crystal structure of the LSD1-CoREST complex shows an elongated structure with a long stalk connecting the catalytic domain of LSD1 and the CoREST SANT2 domain. The shape and dimension of LSD1-CoREST suggest its bivalent binding to nucleosomes, enabling efficient H3-K4 demethylation.
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(2006)
Mol Cell
, vol.23
, pp. 377-387
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Yang, M.1
Gocke, C.B.2
Luo, X.3
Borek, D.4
Tomchick, D.R.5
Machius, M.6
Otwinowski, Z.7
Yu, H.8
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21
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33845935787
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A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1
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In vivo and in vitro experiments to characterize the substrate specificity and recognition by human lysine-specific demethylase (LSD1). It is concluded that epigenetic modifications on histone H3 need to be removed before Lys4 demethylation can efficiently occur.
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Forneris F., Binda C., Dall'aglio A., Fraaije M.W., Battaglioli E., and Mattevi A. A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1. J Biol Chem 281 (2006) 35289-35295. In vivo and in vitro experiments to characterize the substrate specificity and recognition by human lysine-specific demethylase (LSD1). It is concluded that epigenetic modifications on histone H3 need to be removed before Lys4 demethylation can efficiently occur.
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(2006)
J Biol Chem
, vol.281
, pp. 35289-35295
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Forneris, F.1
Binda, C.2
Dall'aglio, A.3
Fraaije, M.W.4
Battaglioli, E.5
Mattevi, A.6
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22
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33646348711
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To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes
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A survey of known 3D structures of flavin-dependent oxidases and dehydrogenases and the correlation with their functional properties indicates that there are no structural rules that enable prediction of whether or how a flavoenzyme reacts with oxygen.
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Mattevi A. To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem Sci 31 (2006) 276-283. A survey of known 3D structures of flavin-dependent oxidases and dehydrogenases and the correlation with their functional properties indicates that there are no structural rules that enable prediction of whether or how a flavoenzyme reacts with oxygen.
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(2006)
Trends Biochem Sci
, vol.31
, pp. 276-283
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Mattevi, A.1
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23
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19644376590
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Purification and characterization of intracellular and extracellular, thermostable and alkali-tolerant alcohol oxidases produced by a thermophilic fungus, Thermoascus aurantiacus NBRC 31693
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Ko H.S., Yokoyama Y., Ohno N., Okadome M., Amachi S., Shinoyama H., and Fujii T. Purification and characterization of intracellular and extracellular, thermostable and alkali-tolerant alcohol oxidases produced by a thermophilic fungus, Thermoascus aurantiacus NBRC 31693. J Biosci Bioeng 99 (2005) 348-353
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(2005)
J Biosci Bioeng
, vol.99
, pp. 348-353
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Ko, H.S.1
Yokoyama, Y.2
Ohno, N.3
Okadome, M.4
Amachi, S.5
Shinoyama, H.6
Fujii, T.7
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27
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31544467044
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Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover
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Nagpal A., Valley M.P., Fitzpatrick P.F., and Orville A.M. Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover. Biochemistry 45 (2006) 1138-1150
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(2006)
Biochemistry
, vol.45
, pp. 1138-1150
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Nagpal, A.1
Valley, M.P.2
Fitzpatrick, P.F.3
Orville, A.M.4
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28
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33845930584
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Structural basis for substrate binding and regioselective oxidation of monosaccharides at C3 by pyranose 2-oxidase
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Kujawa M., Ebner H., Leitner C., Hallberg B.M., Prongjit M., Sucharitakul J., Ludwig R., Rudsander U., Peterbauer C., Chaiyen P., et al. Structural basis for substrate binding and regioselective oxidation of monosaccharides at C3 by pyranose 2-oxidase. J Biol Chem 281 (2006) 35104-35115
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(2006)
J Biol Chem
, vol.281
, pp. 35104-35115
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Kujawa, M.1
Ebner, H.2
Leitner, C.3
Hallberg, B.M.4
Prongjit, M.5
Sucharitakul, J.6
Ludwig, R.7
Rudsander, U.8
Peterbauer, C.9
Chaiyen, P.10
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29
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33646688670
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Multidomain flavin-dependent sulfhydryl oxidases
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Review about origin and properties of quiescin sulfhydryl oxidases (QSOX). The structure and mechanism of QSOX proteins is compared with their smaller stand-alone cousins: yeast ERV1p and ERV2p, the mammalian augmenter of liver regeneration (ALR), and the viral ALR homologues.
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Coppock D.L., and Thorpe C. Multidomain flavin-dependent sulfhydryl oxidases. Antioxid Redox Signal 8 (2006) 300-311. Review about origin and properties of quiescin sulfhydryl oxidases (QSOX). The structure and mechanism of QSOX proteins is compared with their smaller stand-alone cousins: yeast ERV1p and ERV2p, the mammalian augmenter of liver regeneration (ALR), and the viral ALR homologues.
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(2006)
Antioxid Redox Signal
, vol.8
, pp. 300-311
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Coppock, D.L.1
Thorpe, C.2
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30
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33745861722
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Conservation and diversity of the cellular disulfide bond formation pathways
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Sevier C.S., and Kaiser C.A. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid Redox Signal 8 (2006) 797-811
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(2006)
Antioxid Redox Signal
, vol.8
, pp. 797-811
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Sevier, C.S.1
Kaiser, C.A.2
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31
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33747352990
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Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
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Chimeras of yeast and plant enzymes support the view that the ERV/ALR sulfhydryl oxidase domain is a versatile module adapted for catalysis of disulfide bond formation in various organelles and biological settings.
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Vitu E., Bentzur M., Lisowsky T., Kaiser C.A., and Fass D. Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J Mol Biol 362 (2006) 89-101. Chimeras of yeast and plant enzymes support the view that the ERV/ALR sulfhydryl oxidase domain is a versatile module adapted for catalysis of disulfide bond formation in various organelles and biological settings.
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(2006)
J Mol Biol
, vol.362
, pp. 89-101
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Vitu, E.1
Bentzur, M.2
Lisowsky, T.3
Kaiser, C.A.4
Fass, D.5
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32
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9744270010
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Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase
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Entsch B., Cole L.J., and Ballou D.P. Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. Arch Biochem Biophys 433 (2005) 297-311
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(2005)
Arch Biochem Biophys
, vol.433
, pp. 297-311
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Entsch, B.1
Cole, L.J.2
Ballou, D.P.3
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33
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33744962771
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Real-time enzyme dynamics illustrated with fluorescence spectroscopy of p-hydroxybenzoate hydroxylase
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Nice demonstration of how single-molecule fluorescence correlation spectroscopy can be used for the detection of fast relaxation processes in flavoenzyme catalysis.
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Westphal A.H., Matorin A., Hink M.A., Borst J.W., van Berkel W.J.H., and Visser A.J. Real-time enzyme dynamics illustrated with fluorescence spectroscopy of p-hydroxybenzoate hydroxylase. J Biol Chem 281 (2006) 11074-11081. Nice demonstration of how single-molecule fluorescence correlation spectroscopy can be used for the detection of fast relaxation processes in flavoenzyme catalysis.
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(2006)
J Biol Chem
, vol.281
, pp. 11074-11081
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Westphal, A.H.1
Matorin, A.2
Hink, M.A.3
Borst, J.W.4
van Berkel, W.J.H.5
Visser, A.J.6
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34
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28044470079
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High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule
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The first 3D structure of a eukaryotic flavoprotein hydroxylase stresses the importance of protein dynamics in this class of flavoenzymes. Distinctive structural features highlight putative protein-binding sites in suitable proximity to the active site entrance. The unusual juxtaposition of the hydroxylase activity with a multiprotein-binding scaffold represents a unique combination of functionality to mediate signalling.
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Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., Stuart D.I., Terman J.R., Kolodkin A.L., Pasterkamp R.J., and Jones E.Y. High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule. Proc Natl Acad Sci USA 102 (2005) 16836-16841. The first 3D structure of a eukaryotic flavoprotein hydroxylase stresses the importance of protein dynamics in this class of flavoenzymes. Distinctive structural features highlight putative protein-binding sites in suitable proximity to the active site entrance. The unusual juxtaposition of the hydroxylase activity with a multiprotein-binding scaffold represents a unique combination of functionality to mediate signalling.
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(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 16836-16841
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-
Siebold, C.1
Berrow, N.2
Walter, T.S.3
Harlos, K.4
Owens, R.J.5
Stuart, D.I.6
Terman, J.R.7
Kolodkin, A.L.8
Pasterkamp, R.J.9
Jones, E.Y.10
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35
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33751105570
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Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site
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The protein fold of the catalytic domains and the active-site architecture of 3-hydroxybenzoate hydroxylase are similar to those of 4-hydroxybenzoate hydroxylase and phenol hydroxylase. However, a large tunnel connecting the substrate-binding pocket to the protein surface serves for substrate and possibly oxygen transport in this enzyme.
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Hiromoto T., Fujiwara S., Hosokawa K., and Yamaguchi H. Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site. J Mol Biol 364 (2006) 878-896. The protein fold of the catalytic domains and the active-site architecture of 3-hydroxybenzoate hydroxylase are similar to those of 4-hydroxybenzoate hydroxylase and phenol hydroxylase. However, a large tunnel connecting the substrate-binding pocket to the protein surface serves for substrate and possibly oxygen transport in this enzyme.
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(2006)
J Mol Biol
, vol.364
, pp. 878-896
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Hiromoto, T.1
Fujiwara, S.2
Hosokawa, K.3
Yamaguchi, H.4
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36
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25444453735
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Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase
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van den Heuvel R.H., Tahallah N., Kamerbeek N.M., Fraaije M.W., van Berkel W.J.H., Janssen D.B., and Heck A.J. Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase. J Biol Chem 280 (2005) 32115-32121
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(2005)
J Biol Chem
, vol.280
, pp. 32115-32121
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van den Heuvel, R.H.1
Tahallah, N.2
Kamerbeek, N.M.3
Fraaije, M.W.4
van Berkel, W.J.H.5
Janssen, D.B.6
Heck, A.J.7
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37
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33646140803
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Pseudomonad cyclopentadecanone monooxygenase displaying an uncommon spectrum of Baeyer-Villiger oxidations of cyclic ketones
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Iwaki H., Wang S., Grosse S., Bergeron H., Nagahashi A., Lertvorachon J., Yang J., Konishi Y., Hasegawa Y., and Lau P.C. Pseudomonad cyclopentadecanone monooxygenase displaying an uncommon spectrum of Baeyer-Villiger oxidations of cyclic ketones. Appl Environ Microbiol 72 (2006) 2707-2720
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(2006)
Appl Environ Microbiol
, vol.72
, pp. 2707-2720
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Iwaki, H.1
Wang, S.2
Grosse, S.3
Bergeron, H.4
Nagahashi, A.5
Lertvorachon, J.6
Yang, J.7
Konishi, Y.8
Hasegawa, Y.9
Lau, P.C.10
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38
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12144285047
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Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining
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Fraaije M.W., Wu J., Heuts D.P., van Hellemond E.W., Spelberg J.H., and Janssen D.B. Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl Microbiol Biotechnol 66 (2005) 393-400
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(2005)
Appl Microbiol Biotechnol
, vol.66
, pp. 393-400
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Fraaije, M.W.1
Wu, J.2
Heuts, D.P.3
van Hellemond, E.W.4
Spelberg, J.H.5
Janssen, D.B.6
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39
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33845756367
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Cloning, expression, and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas fluorescens DSM 50106 in E. coli
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Kirschner A., Altenbuchner J., and Bornscheuer U.T. Cloning, expression, and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas fluorescens DSM 50106 in E. coli. Appl Microbiol Biotechnol 73 (2007) 1065-1072
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(2007)
Appl Microbiol Biotechnol
, vol.73
, pp. 1065-1072
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Kirschner, A.1
Altenbuchner, J.2
Bornscheuer, U.T.3
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40
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33646462587
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Microbial Baeyer-Villiger oxidation: stereopreference and substrate acceptance of cyclohexanone monooxygenase mutants prepared by directed evolution
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Mihovilovic M.D., Rudroff F., Winninger A., Schneider T., Schulz F., and Reetz M.T. Microbial Baeyer-Villiger oxidation: stereopreference and substrate acceptance of cyclohexanone monooxygenase mutants prepared by directed evolution. Org Lett 8 (2006) 1221-1224
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(2006)
Org Lett
, vol.8
, pp. 1221-1224
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Mihovilovic, M.D.1
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