-
3
-
-
0014690503
-
6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine
-
6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine J. Biol. Chem. 244 1969 2577 2584
-
(1969)
J. Biol. Chem.
, vol.244
, pp. 2577-2584
-
-
Sundaram, T.K.1
Snell, E.E.2
-
4
-
-
0036559818
-
Purification, molecular cloning, and characterization of pyridoxine 4-oxidase from Microbacterium luteolum
-
Y. Kaneda, K. Ohnishi, and T. Yagi Purification, molecular cloning, and characterization of pyridoxine 4-oxidase from Microbacterium luteolum Biosci. Biotechnol. Biochem. 66 2002 1022 1031
-
(2002)
Biosci. Biotechnol. Biochem.
, vol.66
, pp. 1022-1031
-
-
Kaneda, Y.1
Ohnishi, K.2
Yagi, T.3
-
6
-
-
0026544690
-
GMC oxidoreductases: A newly defined family of homologous proteins with diverse catalytic activities
-
D.R. Cavener GMC oxidoreductases: A newly defined family of homologous proteins with diverse catalytic activities J. Mol. Biol. 223 1992 811 814
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 811-814
-
-
Cavener, D.R.1
-
7
-
-
0034854206
-
Sequence-structure analysis of FAD-containing proteins
-
O. Dym, and D. Eisenberg Sequence-structure analysis of FAD-containing proteins Protein Sci. 10 2001 1712 1728
-
(2001)
Protein Sci.
, vol.10
, pp. 1712-1728
-
-
Dym, O.1
Eisenberg, D.2
-
8
-
-
0021111537
-
Kinetic properties of pyridoxamine (pyridoxine)-5′-phosphate oxidase from rabbit liver
-
J.D. Choi, M. Bowers-Komro, M.D. Davis, D.E. Edmondson, and D.B. McCormick Kinetic properties of pyridoxamine (pyridoxine)-5′-phosphate oxidase from rabbit liver J. Biol. Chem. 258 1983 840 845
-
(1983)
J. Biol. Chem.
, vol.258
, pp. 840-845
-
-
Choi, J.D.1
Bowers-Komro, M.2
Davis, M.D.3
Edmondson, D.E.4
Mccormick, D.B.5
-
9
-
-
0036308637
-
Active site structure and stereospecificity of Escherichia coli pyridoxine-5′-phosphate oxidase
-
M.L. Di Salvo, T.-P. Ko, F.N. Musayev, S. Raboni, V. Schirch, and M.K. Safo Active site structure and stereospecificity of Escherichia coli pyridoxine-5′-phosphate oxidase J. Mol. Biol. 315 2002 385 397
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 385-397
-
-
Di Salvo, M.L.1
Ko, T.-P.2
Musayev, F.N.3
Raboni, S.4
Schirch, V.5
Safo, M.K.6
-
10
-
-
34547843594
-
Pyridoxal phosphate prevents progression of diabetic nephropathy
-
S. Nakamura, H. Li, A. Adijiang, M. Pischetsrieder, and T. Niwa Pyridoxal phosphate prevents progression of diabetic nephropathy Nephrol. Dial. Transplant. 22 2007 2165 2174
-
(2007)
Nephrol. Dial. Transplant.
, vol.22
, pp. 2165-2174
-
-
Nakamura, S.1
Li, H.2
Adijiang, A.3
Pischetsrieder, M.4
Niwa, T.5
-
11
-
-
20244367772
-
Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5′-phosphate oxidase
-
P.B. Mills, R.A.H. Surtees, M.P. Champion, C.E. Beesley, N. Dalton, P.J. Scambler, S.J.R. Heales, A. Briddon, I. Scheimberg, G.F. Hoffmann, J. Zschocke, and P.T. Clayton Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5′-phosphate oxidase Hum. Mol. Genet. 14 2005 1077 1086
-
(2005)
Hum. Mol. Genet.
, vol.14
, pp. 1077-1086
-
-
Mills, P.B.1
Surtees, R.A.H.2
Champion, M.P.3
Beesley, C.E.4
Dalton, N.5
Scambler, P.J.6
Heales, S.J.R.7
Briddon, A.8
Scheimberg, I.9
Hoffmann, G.F.10
Zschocke, J.11
Clayton, P.T.12
-
12
-
-
84855983010
-
Crystallization and preliminary X-ray analysis of pyridoxine 4-oxidase, the first enzyme in pyridoxine degradation pathway I
-
A.N. Mugo, J. Kobayashi, B. Mikami, K. Ohnishi, and T. Yagi Crystallization and preliminary X-ray analysis of pyridoxine 4-oxidase, the first enzyme in pyridoxine degradation pathway I Acta Crystallogr. F Struct. Biol. Cryst. Commun. 68 2012 66 68
-
(2012)
Acta Crystallogr. F Struct. Biol. Cryst. Commun.
, vol.68
, pp. 66-68
-
-
Mugo, A.N.1
Kobayashi, J.2
Mikami, B.3
Ohnishi, K.4
Yagi, T.5
-
13
-
-
0026640258
-
Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP
-
T. Mizobata, Y. Akiyama, N. Yumoto, and Y. Kawata Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP J. Biol. Chem. 267 1992 17773 17779
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 17773-17779
-
-
Mizobata, T.1
Akiyama, Y.2
Yumoto, N.3
Kawata, Y.4
-
14
-
-
74549194551
-
Molecular replacement with MOLREP
-
A. Vagin, and A. Teplyakov Molecular replacement with MOLREP Acta Crystallogr. D66 2010 22 25
-
(2010)
Acta Crystallogr.
, vol.66 D
, pp. 22-25
-
-
Vagin, A.1
Teplyakov, A.2
-
15
-
-
79953737180
-
Overview of the CCP4 suite and current developments
-
M.D. Winn, C.C. Ballard, K.D. Cowtan, E.J. Dodson, P. Emsley, P.R. Evans, R.M. Keegan, E.B. Krissinel, A.G.W. Leslie, A. McCoy, S.J. McNicholas, G.N. Murshudov, N.S. Pannu, E.A. Potterton, H.R. Powell, R.J. Read, A. Vagin, and K.S. Wilson Overview of the CCP4 suite and current developments Acta Crystallogr. D67 2011 235 242
-
(2011)
Acta Crystallogr.
, vol.67 D
, pp. 235-242
-
-
Winn, M.D.1
Ballard, C.C.2
Cowtan, K.D.3
Dodson, E.J.4
Emsley, P.5
Evans, P.R.6
Keegan, R.M.7
Krissinel, E.B.8
Leslie, A.G.W.9
Mccoy, A.10
Mcnicholas, S.J.11
Murshudov, G.N.12
Pannu, N.S.13
Potterton, E.A.14
Powell, H.R.15
Read, R.J.16
Vagin, A.17
Wilson, K.S.18
-
16
-
-
0030924992
-
Refinement of macromolecular structures by the maximum-likelihood method
-
G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D53 1997 240 255
-
(1997)
Acta Crystallogr.
, vol.53 D
, pp. 240-255
-
-
Murshudov, G.N.1
Vagin, A.A.2
Dodson, E.J.3
-
17
-
-
13244281317
-
Coot: Model-building tools for molecular graphics
-
P. Emsley, and K. Cowtan Coot: Model-building tools for molecular graphics Acta Crystallogr. D60 2004 2126 2132
-
(2004)
Acta Crystallogr.
, vol.60 D
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
-
18
-
-
14244272868
-
PHENIX: Building new software for automated crystallographic structure determination
-
P.D. Adams, R.W. Grosse-Kunstleve, L.-W. Hung, T.R. Ioerger, A.J. McCoy, N.W. Moriarty, R.J. Read, J.C. Sacchettini, N.K. Sauter, and T.C. Terwilliger PHENIX: Building new software for automated crystallographic structure determination Acta Crystallogr. D58 2002 1948 1954
-
(2002)
Acta Crystallogr.
, vol.58 D
, pp. 1948-1954
-
-
Adams, P.D.1
Grosse-Kunstleve, R.W.2
Hung, L.-W.3
Ioerger, T.R.4
Mccoy, A.J.5
Moriarty, N.W.6
Read, R.J.7
Sacchettini, J.C.8
Sauter, N.K.9
Terwilliger, T.C.10
-
20
-
-
0032922193
-
SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
-
A.A. Vaguine, J. Richelle, and S.J. Wodak SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr. D55 1999 191 205
-
(1999)
Acta Crystallogr.
, vol.55 D
, pp. 191-205
-
-
Vaguine, A.A.1
Richelle, J.2
Wodak, S.J.3
-
21
-
-
0033824470
-
DaliLite workbench for protein structure comparison
-
L. Holm, and J. Park DaliLite workbench for protein structure comparison Bioinformatics 16 2000 566 567
-
(2000)
Bioinformatics
, vol.16
, pp. 566-567
-
-
Holm, L.1
Park, J.2
-
22
-
-
27344454932
-
GROMACS: Fast, flexible, and free
-
D. Van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A.E. Mark, and H.J.C. Berendsen GROMACS: Fast, flexible, and free J. Comput. Chem. 26 2005 1701 1718
-
(2005)
J. Comput. Chem.
, vol.26
, pp. 1701-1718
-
-
Van Der Spoel, D.1
Lindahl, E.2
Hess, B.3
Groenhof, G.4
Mark, A.E.5
Berendsen, H.J.C.6
-
23
-
-
7544226311
-
PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
-
A.W. Schüttelkopf, and D.M.F. Van Aalten PRODRG: A tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr. D60 2004 1355 1363
-
(2004)
Acta Crystallogr.
, vol.60 D
, pp. 1355-1363
-
-
Schüttelkopf, A.W.1
Van Aalten, D.M.F.2
-
24
-
-
0017184389
-
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
-
M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Chem. 72 1976 248 254
-
(1976)
Anal. Chem.
, vol.72
, pp. 248-254
-
-
Bradford, M.M.1
-
25
-
-
33745006425
-
Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase
-
Y. Yoshikane, N. Yokochi, K. Ohnishi, H. Hayashi, and T. Yagi Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase Biochem. J. 396 2006 499 507
-
(2006)
Biochem. J.
, vol.396
, pp. 499-507
-
-
Yoshikane, Y.1
Yokochi, N.2
Ohnishi, K.3
Hayashi, H.4
Yagi, T.5
-
26
-
-
77956177377
-
Structural and kinetic studies on the Ser101Ala variant of choline oxidase: Catalysis by compromise
-
S. Finnegana, H. Yuana, Y.-F. Wang, A.M. Orvilled, I.T. Webera, and G. Gadda Structural and kinetic studies on the Ser101Ala variant of choline oxidase: Catalysis by compromise Arch. Biochem. Biophys. 501 2010 207 213
-
(2010)
Arch. Biochem. Biophys.
, vol.501
, pp. 207-213
-
-
Finnegana, S.1
Yuana, H.2
Wang, Y.-F.3
Orvilled, A.M.4
Webera, I.T.5
Gadda, G.6
-
27
-
-
73349130778
-
Novel structural features in the GMC family of oxidoreductases revealed by the crystal structure of fungal aryl-alcohol oxidase
-
I.S. Fernandez, F.J. Ruiz-Duenas, E. Santillana, P. Ferreira, M.J. Martinez, A.T. Martinez, and A. Romero Novel structural features in the GMC family of oxidoreductases revealed by the crystal structure of fungal aryl-alcohol oxidase Acta Crystallogr. D65 2009 1196 1205
-
(2009)
Acta Crystallogr.
, vol.65 D
, pp. 1196-1205
-
-
Fernandez, I.S.1
Ruiz-Duenas, F.J.2
Santillana, E.3
Ferreira, P.4
Martinez, M.J.5
Martinez, A.T.6
Romero, A.7
-
28
-
-
0033135955
-
1.8 and 1.9 Å resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
-
G. Wohlfahrt, S. Witt, J. Hendle, D. Schomburg, H.M. Kalisz, and H.J. Hecht 1.8 and 1.9 Å resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes Acta Crystallogr. D55 1999 969 977
-
(1999)
Acta Crystallogr.
, vol.55 D
, pp. 969-977
-
-
Wohlfahrt, G.1
Witt, S.2
Hendle, J.3
Schomburg, D.4
Kalisz, H.M.5
Hecht, H.J.6
-
29
-
-
37849031214
-
Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase
-
O. Quaye, G.T. Lountos, F. Fan, A.M. Orville, and G. Gadda Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase Biochemistry 47 2008 243 256
-
(2008)
Biochemistry
, vol.47
, pp. 243-256
-
-
Quaye, O.1
Lountos, G.T.2
Fan, F.3
Orville, A.M.4
Gadda, G.5
-
30
-
-
69849104100
-
Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase
-
O. Quaye, and G. Gadda Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase Arch. Biochem. Biophys. 489 2009 10 14
-
(2009)
Arch. Biochem. Biophys.
, vol.489
, pp. 10-14
-
-
Quaye, O.1
Gadda, G.2
-
31
-
-
77950407407
-
Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase
-
S. Finnegan, J. Agniswamy, T. Irene, I.T. Weber, and G. Gadda Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase Biochemistry 49 2010 2952 2961
-
(2010)
Biochemistry
, vol.49
, pp. 2952-2961
-
-
Finnegan, S.1
Agniswamy, J.2
Irene, T.3
Weber, I.T.4
Gadda, G.5
-
32
-
-
0032735104
-
Structural and mechanistic mapping of a unique fumarate reductase
-
P. Taylor, S.L. Pealing, G.A. Reid, S.K. Chapman, and M.D. Walkinshaw Structural and mechanistic mapping of a unique fumarate reductase Nat. Struct. Biol. 6 1999 1108 1112
-
(1999)
Nat. Struct. Biol.
, vol.6
, pp. 1108-1112
-
-
Taylor, P.1
Pealing, S.L.2
Reid, G.A.3
Chapman, S.K.4
Walkinshaw, M.D.5
-
33
-
-
0001406338
-
Structure of l-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase family
-
A. Mattevi Structure of l-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase family Struct. Fold. Des. 7 1999 745 756
-
(1999)
Struct. Fold. Des.
, vol.7
, pp. 745-756
-
-
Mattevi, A.1
-
34
-
-
0035882572
-
Adenine recognition: A motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins
-
K.A. Denessiouk, V.-V. Rantanen, and M.S. Johnson Adenine recognition: A motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins Proteins 44 2001 282 291
-
(2001)
Proteins
, vol.44
, pp. 282-291
-
-
Denessiouk, K.A.1
Rantanen, V.-V.2
Johnson, M.S.3
-
35
-
-
0036303472
-
Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
-
M.B. Hallberg, G. Henriksson, G. Pettersson, and C. Divne Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase J. Mol. Biol. 315 2002 421 434
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 421-434
-
-
Hallberg, M.B.1
Henriksson, G.2
Pettersson, G.3
Divne, C.4
-
36
-
-
0033528745
-
Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
-
Q.K. Yue, I.J. Kass, N.S. Sampson, and A. Vrielink Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants Biochemistry 38 1999 4277 4286
-
(1999)
Biochemistry
, vol.38
, pp. 4277-4286
-
-
Yue, Q.K.1
Kass, I.J.2
Sampson, N.S.3
Vrielink, A.4
-
37
-
-
79956001462
-
Substrate diffusion and oxidation in GMC oxidoreductases: An experimental and computational study on fungal aryl-alcohol oxidase
-
A. Hernández-Ortega, K. Borrelli, P. Ferreira, M. Medina, A.T. Martínez, and V. Guallar Substrate diffusion and oxidation in GMC oxidoreductases: An experimental and computational study on fungal aryl-alcohol oxidase Biochem. J. 436 2011 341 350
-
(2011)
Biochem. J.
, vol.436
, pp. 341-350
-
-
Hernández-Ortega, A.1
Borrelli, K.2
Ferreira, P.3
Medina, M.4
Martínez, A.T.5
Guallar, V.6
-
38
-
-
84865428476
-
Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle
-
A. Hernández-Ortega, F. Lucas, P. Ferreira, M. Medina, V. Guallar, and A.T. Martínez Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle Biochemistry 51 2012 6595 6608
-
(2012)
Biochemistry
, vol.51
, pp. 6595-6608
-
-
Hernández-Ortega, A.1
Lucas, F.2
Ferreira, P.3
Medina, M.4
Guallar, V.5
Martínez, A.T.6
-
39
-
-
77949505450
-
Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase
-
K. Rungsrisuriyachai, and G. Gadda Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase Biochemistry 49 2010 2483 2490
-
(2010)
Biochemistry
, vol.49
, pp. 2483-2490
-
-
Rungsrisuriyachai, K.1
Gadda, G.2
-
40
-
-
46049114878
-
On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase
-
K. Rungsrisuriyachai, and G. Gadda On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase Biochemistry 47 2008 6762 6769
-
(2008)
Biochemistry
, vol.47
, pp. 6762-6769
-
-
Rungsrisuriyachai, K.1
Gadda, G.2
-
41
-
-
79957747146
-
Regioselective control of β-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy
-
T.-C. Tan, D. Haltrich, and C. Divne Regioselective control of β-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy J. Mol. Biol. 409 2011 588 600
-
(2011)
J. Mol. Biol.
, vol.409
, pp. 588-600
-
-
Tan, T.-C.1
Haltrich, D.2
Divne, C.3
-
42
-
-
81555196346
-
Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction
-
T. Wongnate, J. Sucharitakul, and P. Chaiyen Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction ChemBioChem 12 2011 2577 2586
-
(2011)
ChemBioChem
, vol.12
, pp. 2577-2586
-
-
Wongnate, T.1
Sucharitakul, J.2
Chaiyen, P.3
-
43
-
-
0037470246
-
Mechanism of the reductive half-reaction in cellobiose dehydrogenase
-
B.M. Hallberg, G. Henriksson, G. Pettersson, A. Vasella, and C. Divne Mechanism of the reductive half-reaction in cellobiose dehydrogenase J. Biol. Chem. 278 2003 7160 7166
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 7160-7166
-
-
Hallberg, B.M.1
Henriksson, G.2
Pettersson, G.3
Vasella, A.4
Divne, C.5
-
44
-
-
0035923397
-
The presence of a hydrogen bond between asparagine 485 and the π system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase
-
Y. Yin, N.S. Sampson, A. Vrielink, and P.I. Lario The presence of a hydrogen bond between asparagine 485 and the π system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase Biochemistry 40 2001 13779 13787
-
(2001)
Biochemistry
, vol.40
, pp. 13779-13787
-
-
Yin, Y.1
Sampson, N.S.2
Vrielink, A.3
Lario, P.I.4
-
45
-
-
0037446732
-
Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium
-
F.A.J. Rotsaert, V. Renganathan, and M.H. Gold Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium Biochemistry 42 2003 4049 4056
-
(2003)
Biochemistry
, vol.42
, pp. 4049-4056
-
-
Rotsaert, F.A.J.1
Renganathan, V.2
Gold, M.H.3
|