Page last updated: 2024-09-03

6-hydroxydopa quinone and dihydroxyphenylalanine

6-hydroxydopa quinone has been researched along with dihydroxyphenylalanine in 141 studies

Compound Research Comparison

Studies (6-hydroxydopa quinone)	Trials (6-hydroxydopa quinone)	Recent Studies (post-2010) (6-hydroxydopa quinone)	Studies (dihydroxyphenylalanine)	Trials (dihydroxyphenylalanine)	Recent Studies (post-2010) (dihydroxyphenylalanine)
144	0	14	8,823	322	833

Research

Studies (141)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	73 (51.77)	18.2507
2000's	50 (35.46)	29.6817
2010's	18 (12.77)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Harris, ED	1
Brown, DE; Cooper, RA; Dooley, DM; Knowles, PF; McGuirl, MA	1
Duine, JA	3
Aizenman, E; Boeckman, FA; Rosenberg, PA	1
Acosta, M; Bañón-Arnao, M; García-Cánovas, F; Martinez-Ortiz, F; Rodríguez-López, JN; Tudela, J; Varón, R	1
Brown, DE; Dooley, DM; Janes, SM; Klinman, JP; Mure, M; Palcic, MM; Scaman, CH; Smith, AJ	1
Brown, DE; Dooley, DM; Janes, SM; Klinman, JP; Mu, D; Smith, AJ	1
Dooley, DM; Duine, JA; Klinman, JP; Knowles, PF; Mondovi, B; Villafranca, JJ	1
Brown, DE; Dooley, DM; Janes, SM; Klinman, JP; McGuirl, MA; Mu, D	1
Kumagai, H; Roh, JH; Suzuki, H; Takenaka, Y; Yamamoto, K	1
Fukui, T; Matsuzaki, R; Suzuki, S; Tanizawa, K; Yamaguchi, K	1
Aizenman, E; Newcomer, TA; Rosenberg, PA	2
Lerch, K; Schilling, B	1
Duine, JA; Klinman, JP; Moënne-Loccoz, P; Mure, M; Nakamura, N; Sanders-Loehr, J; Steinebach, V	1
Cai, D; Klinman, JP	1
Dooley, DM; McCahon, CD; McGuirl, MA; McKeown, KA	1
Alton, G; Beever, RJ; Palcic, MM; Taher, TH	1
Choi, YH; Fukui, T; Matsuzaki, R; Ozaki, Y; Sato, H; Shimizu, E; Tanizawa, K; Yorifuji, T	1
Klinman, JP; Mu, D	2
Fukui, T; Matsuzaki, R; Ozaki, Y; Sato, H; Tanizawa, K	1
Bossa, M; Morpurgo, GO; Morpurgo, L	1
McIntire, WS	1
Dooley, DM; McGuirl, MA; Turowski, PN	1
Aizenman, E; Newcomer, TA; Palmer, AM; Rosenberg, PA	1
Fuller, JH; McIntire, WS; Zhang, X	1
Goto, M; Ikeda, T; Kano, K; Mori, T; Uno, B	1
Cooper, RA; Hanlon, SP	1
Janes, SM; Klinman, JP	1
Janes, SM; Palcic, MM	1
Klinman, JP; Mure, M	1
Lee, Y; Sayre, LM	1
Dooley, DM; Hartmann, C	1
Tanizawa, K	2
Duine, JA; Groen, BW; Jongejan, JA; Niessen, WM; Steinebach, V; Wijmenga, SS	1
Esaki, N; Soda, K	1
Eklund, H; Fontecave, M	1
Blakeley, V; Convery, MA; Corner, AS; Knowles, PF; McPherson, MJ; Parsons, MR; Phillips, SE; Wilmot, CM; Yadav, KD	1
Choi, YH; Matsuzaki, R; Nakamura, N; Sanders-Loehr, J; Tanizawa, K	1
Bader, R; Benen, JA; De Vries, S; Duine, JA; Postma, PW; Steinebach, V	1
Adachi, O; Asano, Y; Frébort, I; Hirota, S; Kato, Y; Kitagawa, T; Luhová, L; Matsushita, K; Pec, P; Toyama, H; Ueno, T	1
De Jong, GA; De Vries, S; Duine, JA; Steinebach, V; Wijmenga, SS	1
Choi, YH; Matsuzaki, R; Suzuki, S; Tanizawa, K	1
Dooley, DM; Freeman, HC; Guss, JM; Harvey, I; Kumar, V; McGuirl, MA; Wilce, MC; Zubak, VM	1
Curreli, N; Finazzi-Agrò, A; Rescigno, A; Rinaldi, A; Rinaldi, AC; Sanjust, E; Soddu, G; Sollai, F	1
Klinman, JP	2
Brown, DE; Dooley, DM; Dove, JE; Klinman, JP; Kuchar, J; Smith, AJ	1
Anthony, C	1
Duine, JA; Hacisalihoglu, A; Jongejan, JA	1
Adachi, O; Frébort, I; Matsushita, K	1
Dooley, DM; Ruggiero, CE; Smith, JA; Tanizawa, K	1
Agostinelli, E; De Matteis, G; Mondovì, B; Morpurgo, L; Sinibaldi, A	1
Hartmann, C; McIntire, WS	1
Cai, D; Klinman, JP; Williams, NK	1
Cai, D; Dove, J; Klinman, JP; Nakamura, N; Sanders-Loehr, J	1
Klinman, JP; Moënne-Loccoz, P; Mure, M; Nakamura, N; Sanders-Loehr, J; Suzuki, S; Tanizawa, K	1
Dooley, DM; Freeman, HC; Guss, JM; Matsunami, H; McIntire, WS; Ruggiero, CE; Tanizawa, K; Wilce, MC; Yamaguchi, H	1
Curreli, N; Finazzi-Agró, A; Oliva, S; Porcu, CM; Rescigno, A; Rinaldi, A; Rinaldi, AC; Sanjust, E; Sollai, F	1
Alton, G; Holt, A; Loppnow, GR; Palcic, MM; Scaman, CH; Svendsen, I; Szpacenko, A	1
Klinman, JP; Li, R; Mathews, FS	1
Klinman, JP; Su, Q	1
Matsuzaki, R; Tanizawa, K	1
Green, EL; Klinman, JP; Sanders-Loehr, J; Schwartz, B	1
Dooley, DM; Ruggiero, CE	1
Hevel, JM; Klinman, JP; Mills, SA	1
Davidson, VL; Zhu, Z	1
Dooley, DM	1
Adachi, O; Hirota, S; Iwamoto, T; Tanizawa, K; Yamauchi, O	1
Hajdu, J; Knowles, PF; McPherson, MJ; Phillips, SE; Wilmot, CM	1
Dove, JE; Klinman, JP; Schwartz, B; Williams, NK	1
Dove, JE; Klinman, JP; Schwartz, B	1
Mitchell, AE; Rucker, RB; Stites, TE	1
Agostinelli, E; Bellelli, A; Mondovì, B; Morpurgo, L	1
Di Giulio, A; Oliva, S; Ponticelli, G; Rinaldi, AC; Sanjust, E	1
Green, EL; Klinman, JP; Melville, CR; Sanders-Loehr, J	1
Chen, Z; Klinman, JP; Li, R; Mathews, FS; Schwartz, B; Williams, NK	1
Klinman, JP; Schwartz, B	1
Jabre, F; Réglier, M; Slama, P; Tron, T	1
Klinman, JP; Olgin, AK; Schwartz, B	1
Dove, JE; Klinman, JP	1
Hirota, S; Iwamoto, T; Kishishita, S; Okajima, T; Tanizawa, K; Yamauchi, O	1
Dawkes, HC; Phillips, SE	1
Dooley, DM; Green, EL; Klinman, JP; Nakamura, N; Sanders-Loehr, J	1
Knowles, PF; McPherson, MJ; Murray, JM; Phillips, SE; Saysell, CG; Tambyrajah, WS; Wilmot, CM	1
Bollinger, JA; Dooley, DM; Elmore, BO	1
Kawamori, A; Kim, M; Kishishita, S; Okajima, T; Tanizawa, K; Yamaguchi, H; Yoshimura, M	1
Klinman, JP; Mills, SA; Mure, M	1
Dooley, DM; Elmore, BO; Kuchar, JA; Sayre, LM; Shepard, EM; Smith, J	1
Goto, Y; Klinman, JP	1
Conti, A; Corpillo, D; Finazzi-Agrò, A; Giuffrida, MG; Giunta, C; Rossi, A; Valetti, F	1
Mondovi, B; Morpurgo, L; Nocera, S; Pietrangeli, P	1
Minaev, BF; Prabhakar, R; Siegbahn, PE	1
Amii, RN; Dooley, DM; Gray, HB; Hess, CR; Hill, MG; Juda, GA; Winkler, JR	1
Okajima, T; Tanizawa, K	1
Clauss, A; Lundwall, A; Malm, J; Olsson, AY; Valtonen-Andre, C	1
Cohen, AE; Dooley, DM; Duff, AP; Ellis, PJ; Freeman, HC; Guss, JM; Kuchar, JA; Langley, DB; Shepard, EM	1
Mure, M	1
Hirota, S; Hori, H; Kuroda, S; Matsunami, H; Okajima, T; Tanizawa, K; Yamaguchi, H	1
Prabhakar, R; Siegbahn, PE	1
Brazeau, BJ; Johnson, BJ; Wilmot, CM	1
Basran, J; Hothi, P; Masgrau, L; Scrutton, NS; Sutcliffe, MJ	1
Dooley, DM; Duff, AP; Freeman, HC; Guss, JM; Jeon, HB; Langley, DB; O'Connell, KM; Sayre, LM; Shepard, EM; Sun, G	1
Ling, KQ; Sayre, LM	1
Floris, G; Frycák, P; Lamplot, Z; Longu, S; Medda, R; Padiglia, A; Pec, P; Sebela, M	1
Jakobsson, E; Kleywegt, GJ; Nilsson, J; Ogg, D	1
Klinman, JP; Samuels, NM	2
Frébort, I; Lenobel, R; Sebela, M	1
Hayashi, H; Kuroda, S; Murakawa, T; Nakamoto, T; Okajima, T; Taki, M; Tanizawa, K; Yamamoto, Y	1
DuBois, JL; Klinman, JP	1
Chiu, YC; Hayashi, H; Hirota, S; Kamiya, N; Kawano, Y; Kim, M; Kuroda, S; Murakawa, T; Okajima, T; Taki, M; Tanizawa, K; Uchida, M; Yamaguchi, H; Yamamoto, Y	1
Klinman, JP; Takahashi, K	1
Finazzi Agrò, A; Floris, G; Medda, R; Mura, A; Padiglia, A; Pintus, F	1
Dooley, DM; Shepard, EM	1
Anedda, R; Casu, M; Floris, G; Medda, R; Mura, A; Padiglia, A; Pintus, F	1
Culpepper, MB; Hirota, S; Moore, RH; Murakawa, T; Mure, M; Okajima, T; Spies, MA; Tanizawa, K	1
Amani, M; Floris, G; Heli, H; Jabbari, A; Moosavi-Movahedi, AA; Mura, A	1
Hayashi, H; Murakawa, T; Nakamoto, T; Okajima, T; Taki, M; Tanizawa, K; Uchida, M; Yamamoto, Y	1
Schwelberger, HG	1
Gaule, TG; Knowles, PF; Kurtis, CR; McPherson, MJ; Pearson, AR; Phillips, SE; Pirrat, P; Smith, MA; Trinh, CH	1
Chen, ZW; Datta, S; Dubois, JL; Klinman, JP; Mathews, FS	1
Caradoc-Davies, T; Collyer, CA; Guss, JM; McGrath, AP	1
Kataoka, M; Okajima, T; Otsu, M; Oya, H; Tanizawa, K; Tominaga, A; Yamaguchi, H	1
Ernberg, K; Guss, JM; Ko, K; Lee, I; Miller, L; Nguyen, YH; Sayre, LM; Zhong, B	1
Cramer, CJ; Ertem, MZ; Fujieda, N; Itoh, S; Kunishita, A; Sugimoto, H; Tabuchi, K; Tano, T	1
Bligt, E; Elovaara, H; Jalkanen, S; Kidron, H; Nymalm, Y; Ollikka, P; Parkash, V; Pihlavisto, M; Salmi, M; Salminen, TA; Smith, DJ	1
Nakai, T; Okajima, T; Tanizawa, K	1
Hayashi, H; Kawano, Y; Murakawa, T; Okajima, T; Taki, M; Tanizawa, K; Yamamoto, Y	1
Fleury, MB; Largeron, M	1
Klema, VJ; Wilmot, CM	1
Klema, VJ; Klinman, JP; Solheid, CJ; Wilmot, CM	1
Bonnot, F; Klinman, JP	1
Cai, H; Fu, Z; Xu, F	1
Altmann, F; Boehm, T; Bonta, M; Borth, N; Furtmüller, PG; Gludovacz, E; Jilma, B; Limbeck, A; Maresch, D; Szöllösi, H; Weik, R	1
Baba, S; Hayashi, H; Kawano, Y; Kumasaka, T; Murakawa, T; Okajima, T; Tanizawa, K; Yamamoto, M; Yano, T	1
Adelson, CN; Broderick, JB; Brown, DE; Dey, SG; Dooley, DM; Hilmer, KM; Johnston, EM; Shepard, EM; Solomon, EI; Watts, H	1

Reviews

25 review(s) available for 6-hydroxydopa quinone and dihydroxyphenylalanine

Article	Year
The pyrroloquinoline quinone (PQQ) coenzymes: a case of mistaken identity. Nutrition reviews, 1992, Volume: 50, Issue:9 Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Molecular Structure; PQQ Cofactor; Quinolones	1992
Quinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone. European journal of biochemistry, 1991, Sep-01, Volume: 200, Issue:2 Topics: Coenzymes; Dihydroxyphenylalanine; Enzymes; Gram-Negative Bacteria; Indolequinones; Molecular Conformation; Oxidoreductases; PQQ Cofactor; Protein Conformation; Quinolones; Quinones; Tryptophan	1991
Status of the cofactor identity in copper oxidative enzymes. FEBS letters, 1991, Apr-22, Volume: 282, Issue:1 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Coenzymes; Copper; Dihydroxyphenylalanine; Dopamine beta-Hydroxylase; Galactose Oxidase; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones	1991
Quinoenzymes in biology. Annual review of biochemistry, 1994, Volume: 63 Topics: Amino Acid Sequence; Animals; Coenzymes; Dihydroxyphenylalanine; Indolequinones; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones; Quinones; Sequence Homology, Amino Acid; Tryptophan	1994
Quinoproteins. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1994, Volume: 8, Issue:8 Topics: Coenzymes; Dihydroxyphenylalanine; Indolequinones; Oxidation-Reduction; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1994
Biogenesis of novel quinone coenzymes. Journal of biochemistry, 1995, Volume: 118, Issue:4 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Coenzymes; Dihydroxyphenylalanine; Humans; Indolequinones; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Sequence Alignment; Tryptophan	1995
[Trace elements as activation factors of enzymes: characteristic enzymes and their activation mechanisms]. Nihon rinsho. Japanese journal of clinical medicine, 1996, Volume: 54, Issue:1 Topics: Amine Oxidase (Copper-Containing); Animals; Dihydroxyphenylalanine; Formate Dehydrogenases; Humans; Oxidoreductases Acting on CH-NH Group Donors; Trace Elements	1996
Copper amine oxidase: a novel use for a tyrosine. Structure (London, England : 1993), 1995, Nov-15, Volume: 3, Issue:11 Topics: Amine Oxidase (Copper-Containing); Bacterial Proteins; Binding Sites; Catalysis; Dihydroxyphenylalanine; Escherichia coli; Models, Chemical; Oxidation-Reduction; Protein Conformation; Quaternary Ammonium Compounds; Tyrosine	1995
New quinocofactors in eukaryotes. The Journal of biological chemistry, 1996, Nov-01, Volume: 271, Issue:44 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Binding Sites; Chemotactic Factors; Dihydroxyphenylalanine; Gram-Negative Bacteria; Lysine; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones; Quinones	1996
Quinoprotein-catalysed reactions. The Biochemical journal, 1996, Dec-15, Volume: 320 ( Pt 3) Topics: Alcohol Oxidoreductases; Amine Oxidase (Copper-Containing); Bacterial Proteins; Binding Sites; Coenzymes; Dihydroxyphenylalanine; Disulfides; Electron Transport; Indolequinones; Lysine; Models, Chemical; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Protein-Lysine 6-Oxidase; Quinolones; Quinones; Tryptophan	1996
Structure and biogenesis of topaquinone and related cofactors. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 1999, Volume: 4, Issue:1 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Galactose Oxidase; Lysine; Mechanics; Models, Molecular; Oxidation-Reduction; Quinones; Tyrosine	1999
[Built-in cofactors: amino acid residue-derived new cofactors]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1999, Volume: 44, Issue:13 Topics: Amino Acids; Animals; Catalysis; Coenzymes; Dihydroxyphenylalanine; Indolequinones; Lysine; Protein Processing, Post-Translational; Quinones; Tryptophan	1999
Physiological importance of quinoenzymes and the O-quinone family of cofactors. The Journal of nutrition, 2000, Volume: 130, Issue:4 Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Enzymes; Humans; Indolequinones; Lysine; PQQ Cofactor; Quinolones; Quinones; Tryptophan	2000
Mechanisms of biosynthesis of protein-derived redox cofactors. Vitamins and hormones, 2001, Volume: 61 Topics: Amino Acid Oxidoreductases; Amino Acids; Coenzymes; Dihydroxyphenylalanine; Galactose Oxidase; Indolequinones; Lysine; Oxidation-Reduction; Quinones; Tryptophan	2001
Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase. Advances in protein chemistry, 2001, Volume: 58 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Dihydroxyphenylalanine; Humans; Lysine; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein-Lysine 6-Oxidase; Quinones; Sequence Homology, Amino Acid	2001
Copper amine oxidase: cunning cofactor and controversial copper. Current opinion in structural biology, 2001, Volume: 11, Issue:6 Topics: Amine Oxidase (Copper-Containing); Amino Acid Substitution; Animals; Binding Sites; Catalysis; Coenzymes; Copper; Dihydroxyphenylalanine; Oxidation-Reduction; Protein Conformation	2001
The multi-functional topa-quinone copper amine oxidases. Biochimica et biophysica acta, 2003, Apr-11, Volume: 1647, Issue:1-2 Topics: Amine Oxidase (Copper-Containing); Catalysis; Dihydroxyphenylalanine	2003
Is the catalytic mechanism of bacteria, plant, and mammal copper-TPQ amine oxidases identical? Biochimica et biophysica acta, 2003, Apr-11, Volume: 1647, Issue:1-2 Topics: Amine Oxidase (Copper-Containing); Bacteria; Catalysis; Dihydroxyphenylalanine; Hydrogen Peroxide; Oxidation-Reduction; Plants; Protein Subunits	2003
A theoretical study of the dioxygen activation by glucose oxidase and copper amine oxidase. Biochimica et biophysica acta, 2003, Apr-11, Volume: 1647, Issue:1-2 Topics: Amine Oxidase (Copper-Containing); Dihydroxyphenylalanine; Glucose Oxidase; Superoxides	2003
[New progress in research on peptidyl built-in cofactors]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 2003, Volume: 48, Issue:6 Topics: Amine Oxidase (Copper-Containing); Animals; Binding Sites; Catalysis; Coenzymes; Crystallography, X-Ray; Dihydroxyphenylalanine; Dipeptides; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Quinones	2003
Tyrosine-derived quinone cofactors. Accounts of chemical research, 2004, Volume: 37, Issue:2 Topics: Amine Oxidase (Copper-Containing); Animals; Binding Sites; Coenzymes; Dihydroxyphenylalanine; Humans; Lysine; Models, Molecular; Protein-Lysine 6-Oxidase; Quinones	2004
Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective. Archives of biochemistry and biophysics, 2004, Aug-01, Volume: 428, Issue:1 Topics: Amine Oxidase (Copper-Containing); Catalysis; Coenzymes; Dihydroxyphenylalanine; Enzyme Activation; Models, Molecular; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Species Specificity; Structure-Activity Relationship	2004
Hydrogen tunneling in quinoproteins. Archives of biochemistry and biophysics, 2004, Aug-01, Volume: 428, Issue:1 Topics: Dihydroxyphenylalanine; Enzyme Activation; Hydrogen; Hydrogen Bonding; Kinetics; Models, Chemical; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor	2004
[Mechanisms of biosynthesis of built-in cofactors]. Seikagaku. The Journal of Japanese Biochemical Society, 2011, Volume: 83, Issue:8 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Catalysis; Codon, Terminator; Coenzymes; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Dipeptides; Endonucleases; Humans; Indolequinones; Ions; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; RNA-Directed DNA Polymerase; Tryptophan	2011
Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ. Chemical reviews, 2014, Apr-23, Volume: 114, Issue:8 Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Dipeptides; Humans; Indolequinones; Lysine; PQQ Cofactor; Quinones; Tryptophan	2014

Other Studies

116 other study(ies) available for 6-hydroxydopa quinone and dihydroxyphenylalanine

Article	Year
Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12. The Biochemical journal, 1992, Dec-01, Volume: 288 ( Pt 2) Topics: Amine Oxidase (Copper-Containing); Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Escherichia coli; Oxidoreductases Acting on CH-NH Group Donors; Phenethylamines; Spectrum Analysis; Spectrum Analysis, Raman	1992
The quinoid cofactors, pyrroloquinoline quinone (PQQ), topaquinone (TPQ) and tryptophan tryptophylquinone (TTQ). Journal of nutritional science and vitaminology, 1992, Volume: Spec No Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Humans; Indolequinones; Molecular Structure; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1992
Glutathione prevents 2,4,5-trihydroxyphenylalanine excitotoxicity by maintaining it in a reduced, non-active form. Neuroscience letters, 1992, Sep-14, Volume: 144, Issue:1-2 Topics: Animals; Cerebral Cortex; Dihydroxyphenylalanine; Electrophysiology; Glutathione; Neurons; Oxidation-Reduction; Rats	1992
Catalytic oxidation of 2,4,5-trihydroxyphenylalanine by tyrosinase: identification and evolution of intermediates. Biochimica et biophysica acta, 1992, Nov-20, Volume: 1160, Issue:2 Topics: Animals; Dihydroxyphenylalanine; Kinetics; Monophenol Monooxygenase; Oxidation-Reduction; Substrate Specificity	1992
Identification of topaquinone and its consensus sequence in copper amine oxidases. Biochemistry, 1992, Dec-08, Volume: 31, Issue:48 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Binding Sites; Chromatography, High Pressure Liquid; Coenzymes; Consensus Sequence; Dihydroxyphenylalanine; Fabaceae; Kidney; Molecular Sequence Data; Peptide Fragments; Phenylhydrazines; Plants, Medicinal; Spectrum Analysis, Raman; Swine; Trypsin	1992
Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases. The Journal of biological chemistry, 1992, Apr-25, Volume: 267, Issue:12 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Binding Sites; Cell Line; Chromatography, High Pressure Liquid; Codon; Dihydroxyphenylalanine; Electrophoresis, Polyacrylamide Gel; Molecular Sequence Data; Pichia; Protein Processing, Post-Translational; Sequence Homology, Nucleic Acid; Spectrum Analysis, Raman; Tyrosine	1992
The organic functional group in copper-containing amine oxidases. Resonance Raman spectra are consistent with the presence of topa quinone (6-hydroxydopa quinone) in the active site. The Journal of biological chemistry, 1991, Mar-05, Volume: 266, Issue:7 Topics: Amine Oxidase (Copper-Containing); Animals; Arthrobacter; Binding Sites; Cattle; Copper; Dihydroxyphenylalanine; Kidney; Metalloproteins; Oxidoreductases Acting on CH-NH Group Donors; Plants; Spectrum Analysis, Raman; Swine	1991
Escherichia coli K-12 copper-containing monoamine oxidase: investigation of the copper binding ligands by site-directed mutagenesis, elemental analysis and topa quinone formation. Biochemical and biophysical research communications, 1995, Jul-26, Volume: 212, Issue:3 Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Copper; Dihydroxyphenylalanine; DNA Primers; DNA, Bacterial; Elements; Escherichia coli; Histidine; Ligands; Molecular Sequence Data; Monoamine Oxidase; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Spectrophotometry	1995
Spectroscopic studies on the mechanism of the topa quinone generation in bacterial monoamine oxidase. Biochemistry, 1995, Apr-11, Volume: 34, Issue:14 Topics: Arthrobacter; Circular Dichroism; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Monoamine Oxidase	1995
TOPA quinone, a kainate-like agonist and excitotoxin is generated by a catecholaminergic cell line. The Journal of neuroscience : the official journal of the Society for Neuroscience, 1995, Volume: 15, Issue:4 Topics: Adrenal Gland Neoplasms; Animals; Aromatic Amino Acid Decarboxylase Inhibitors; Catecholamines; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Glutathione; Hydrazines; Kinetics; PC12 Cells; Pheochromocytoma; Rats; Tyrosine	1995
Amine oxidases from Aspergillus niger: identification of a novel flavin-dependent enzyme. Biochimica et biophysica acta, 1995, Apr-13, Volume: 1243, Issue:3 Topics: Amino Acid Sequence; Aspergillus niger; Binding Sites; Clorgyline; Consensus Sequence; Copper; Dihydroxyphenylalanine; Flavin-Adenine Dinucleotide; Molecular Sequence Data; Monoamine Oxidase; Monoamine Oxidase Inhibitors; Pargyline; Recombinant Proteins; Semicarbazides; Sequence Homology; Spectrophotometry; Substrate Specificity	1995
Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy. Biochemistry, 1995, May-30, Volume: 34, Issue:21 Topics: Amine Oxidase (Copper-Containing); Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Escherichia coli; Oxidoreductases Acting on CH-NH Group Donors; Oxygen Isotopes; Spectrum Analysis, Raman	1995
Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. The Journal of biological chemistry, 1994, Dec-23, Volume: 269, Issue:51 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Base Sequence; Binding Sites; Catalysis; Coenzymes; Consensus Sequence; Copper; Dihydroxyphenylalanine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Saccharomyces cerevisiae	1994
Purification and characterization of pea seedling amine oxidase for crystallization studies. Plant physiology, 1994, Volume: 106, Issue:3 Topics: Amine Oxidase (Copper-Containing); Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Durapatite; Electrophoresis, Polyacrylamide Gel; Fabaceae; Molecular Weight; Oxidoreductases Acting on CH-NH Group Donors; Plants, Medicinal; Spectrophotometry	1994
Stereochemistry of benzylamine oxidation by copper amine oxidases. Archives of biochemistry and biophysics, 1995, Jan-10, Volume: 316, Issue:1 Topics: Amine Oxidase (Copper-Containing); Animals; Benzaldehydes; Benzylamines; Cattle; Copper; Dihydroxyphenylalanine; Dopamine; Enzymes; Horses; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Rabbits; Sheep; Stereoisomerism; Swine; Tyramine	1995
Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme, and generation of topa quinone cofactor. The Journal of biological chemistry, 1995, Mar-03, Volume: 270, Issue:9 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Arthrobacter; Base Sequence; Cloning, Molecular; Copper; Dihydroxyphenylalanine; DNA, Bacterial; Enzyme Activation; Enzyme Precursors; Molecular Sequence Data; Phenylhydrazines; Sequence Homology, Amino Acid	1995
Iron-mediated oxidation of 3,4-dihydroxyphenylalanine to an excitotoxin. Journal of neurochemistry, 1995, Volume: 64, Issue:4 Topics: 6-Cyano-7-nitroquinoxaline-2,3-dione; Animals; Ascorbic Acid; Cells, Cultured; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Electrophysiology; Hydrogen Peroxide; Iron; Neurons; Neurotoxins; Oxidation-Reduction; Rats	1995
Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS letters, 1994, Sep-12, Volume: 351, Issue:3 Topics: Arthrobacter; Coenzymes; Copper; Dihydroxyphenylalanine; Escherichia coli; Monoamine Oxidase; Oxidation-Reduction; Recombinant Proteins; Spectrum Analysis; Tyrosine	1994
Models and molecular orbital semiempirical calculations in the study of the spectroscopic properties of bovine serum amine oxidase quinone cofactor. Biochemistry, 1994, Apr-12, Volume: 33, Issue:14 Topics: Amine Oxidase (Copper-Containing); Animals; Benzoquinones; Cattle; Coenzymes; Copper; Dihydroxyphenylalanine; Electrons; Hydrazines; Hydrogen; Magnetic Resonance Spectroscopy; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Solvents; Spectrophotometry, Infrared	1994
Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase. The Journal of biological chemistry, 1993, Aug-25, Volume: 268, Issue:24 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Electron Transport; Fabaceae; Kinetics; Models, Structural; Oxidoreductases Acting on CH-NH Group Donors; Plants, Medicinal; Spectrophotometry	1993
Nonenzymatic conversion of 3,4-dihydroxyphenylalanine to 2,4,5-trihydroxyphenylalanine and 2,4,5-trihydroxyphenylalanine quinone in physiological solutions. Journal of neurochemistry, 1993, Volume: 61, Issue:3 Topics: Buffers; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Norepinephrine; Oxidation-Reduction; Solutions	1993
Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph. Journal of bacteriology, 1993, Volume: 175, Issue:17 Topics: Amino Acid Sequence; Animals; Arthrobacter; Base Sequence; Blotting, Northern; Blotting, Southern; Blotting, Western; Cloning, Molecular; Copper; Dihydroxyphenylalanine; DNA, Bacterial; Gene Expression Regulation, Bacterial; Genes, Bacterial; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Restriction Mapping; Sequence Homology, Amino Acid; Transcription, Genetic	1993
Characterization of topa quinone cofactor. Biochimica et biophysica acta, 1993, Jul-11, Volume: 1157, Issue:3 Topics: Benzoquinones; Dihydroxyphenylalanine; Electrochemistry; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Oxidation-Reduction; Phenylalanine	1993
Cellular location influences copper-dependent topaquinone formation for phenylethylamine oxidase expressed in Escherichia coli K-12. FEMS microbiology letters, 1995, Nov-15, Volume: 133, Issue:3 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Cell Compartmentation; Copper; Dihydroxyphenylalanine; Escherichia coli; Mutation	1995
Cloning of mammalian topa quinone-containing enzymes. Methods in enzymology, 1995, Volume: 258 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Carrier Proteins; Cattle; Cloning, Molecular; Dihydroxyphenylalanine; DNA Primers; Humans; Mammals; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Polymerase Chain Reaction; Recombinant Proteins; Sequence Homology, Amino Acid	1995
Isolation of 2,4,5-trihydroxyphenylalanine quinone (topa quinone) from copper amine oxidases. Methods in enzymology, 1995, Volume: 258 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Binding Sites; Cattle; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Indicators and Reagents; Kidney; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Pisum sativum; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Spectrophotometry; Swine; Thermolysin; Trypsin	1995
Spectrophotometric detection of topa quinone. Methods in enzymology, 1995, Volume: 258 Topics: Amine Oxidase (Copper-Containing); Animals; Arthrobacter; Cattle; Chromatography, Gel; Dihydroxyphenylalanine; Fabaceae; Female; Horses; Indicators and Reagents; Kidney; Molecular Structure; Plants, Medicinal; Spectrophotometry; Swine	1995
Model studies of topa quinone: synthesis and characterization of topa quinone derivatives. Methods in enzymology, 1995, Volume: 258 Topics: Amine Oxidase (Copper-Containing); Animals; Binding Sites; Cattle; Deuterium Oxide; Dihydroxyphenylalanine; Indicators and Reagents; Magnetic Resonance Spectroscopy; Models, Chemical; Resorcinols; Schiff Bases; Spectrophotometry; Structure-Activity Relationship	1995
Catalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases. Methods in enzymology, 1995, Volume: 258 Topics: Aerobiosis; Amine Oxidase (Copper-Containing); Animals; Benzoquinones; Benzylamines; Catalysis; Deamination; Dihydroxyphenylalanine; Indicators and Reagents; Kinetics; Magnetic Resonance Spectroscopy; Mammals; Models, Chemical; Oxidation-Reduction; Schiff Bases; Substrate Specificity	1995
Detection of reaction intermediates in topa quinone enzymes. Methods in enzymology, 1995, Volume: 258 Topics: Amine Oxidase (Copper-Containing); Ammonia; Animals; Benzylamines; Carbon Radioisotopes; Cattle; Circular Dichroism; Dihydroxyphenylalanine; Electrochemistry; Electron Spin Resonance Spectroscopy; Indicators and Reagents; Kinetics; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Pisum sativum; Radioisotope Dilution Technique; Regression Analysis; Spectrophotometry; Thermodynamics; Tritium	1995
Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase. Analytical biochemistry, 1995, Sep-01, Volume: 230, Issue:1 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Consensus Sequence; Dihydroxyphenylalanine; Escherichia coli; Indicators and Reagents; Kidney; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Spectrophotometry; Swine	1995
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure (London, England : 1993), 1995, Nov-15, Volume: 3, Issue:11 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Bacterial Proteins; Base Sequence; Binding Sites; Catalysis; Cloning, Molecular; Crystallography, X-Ray; Dihydroxyphenylalanine; Escherichia coli; Histidine; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Alignment	1995
Biosynthesis of topa quinone cofactor in bacterial amine oxidases. Solvent origin of C-2 oxygen determined by Raman spectroscopy. The Journal of biological chemistry, 1996, Mar-01, Volume: 271, Issue:9 Topics: Amine Oxidase (Copper-Containing); Amino Acid Oxidoreductases; Arthrobacter; Cloning, Molecular; Coenzymes; Copper; Dihydroxyphenylalanine; Escherichia coli; Indicators and Reagents; Isotope Labeling; Methylamines; Oxygen Isotopes; Phenylhydrazines; Recombinant Proteins; Solvents; Spectrum Analysis, Raman; Water	1996
Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme. European journal of biochemistry, 1996, May-01, Volume: 237, Issue:3 Topics: Amino Acid Sequence; Base Sequence; Chromatography, Ion Exchange; Cloning, Molecular; Dihydroxyphenylalanine; DNA, Bacterial; Electron Spin Resonance Spectroscopy; Escherichia coli; Gene Expression; Genes, Bacterial; Molecular Sequence Data; Molecular Weight; Monoamine Oxidase; Operon; Phenylhydrazines; Plasmids; Spectrophotometry	1996
Two amine oxidases from Aspergillus niger AKU 3302 contain topa quinone as the cofactor: unusual cofactor link to the glutamyl residue occurs only at one of the enzymes. Biochimica et biophysica acta, 1996, Jun-07, Volume: 1295, Issue:1 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Aspergillus niger; Coenzymes; Consensus Sequence; Dihydroxyphenylalanine; Glutamic Acid; Models, Chemical; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Peptide Fragments; Phenylhydrazines; Sequence Analysis	1996
The copper-topaquinone-phenylhydrazine-adduct geometry in Escherichia coli amine oxidase derivatized with phenylhydrazines substituted with 19F-NMR relaxation measurements. European journal of biochemistry, 1996, Jun-15, Volume: 238, Issue:3 Topics: Amine Oxidase (Copper-Containing); Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Escherichia coli; Fluorine Radioisotopes; Magnetic Resonance Spectroscopy; Models, Molecular; Phenylhydrazines	1996
Role of conserved Asn-Tyr-Asp-Tyr sequence in bacterial copper/2,4, 5-trihydroxyphenylalanyl quinone-containing histamine oxidase. The Journal of biological chemistry, 1996, Sep-13, Volume: 271, Issue:37 Topics: Amine Oxidase (Copper-Containing); Base Sequence; Conserved Sequence; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Escherichia coli; Kinetics; Molecular Sequence Data; Oxygen Consumption; Phenylhydrazines; Plasmids; Protein Conformation; Spectrophotometry, Atomic	1996
Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution. Structure (London, England : 1993), 1996, Aug-15, Volume: 4, Issue:8 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Binding Sites; Copper; Crystallography, X-Ray; Cystine; Dihydroxyphenylalanine; Dimerization; Glycosylation; Models, Molecular; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Pisum sativum; Plant Proteins; Protein Conformation; Protein Processing, Post-Translational; Seeds; Sequence Alignment; Sequence Homology, Amino Acid	1996
Dopaquinone hydroxylation through topaquinone cofactor in copper amine oxidases: a simplified chemical model. Biochemistry and molecular biology international, 1996, Volume: 40, Issue:1 Topics: Amine Oxidase (Copper-Containing); Benzoquinones; Dihydroxyphenylalanine; Hydroxylation; Models, Chemical	1996
Tryptophan-derived cofactors functioning in oxidoreductases. Advances in experimental medicine and biology, 1996, Volume: 398 Topics: Coenzymes; Dihydroxyphenylalanine; Indolequinones; Molecular Structure; Oxidoreductases; Paracoccus denitrificans; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1996
Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. FEBS letters, 1996, Dec-02, Volume: 398, Issue:2-3 Topics: Amino Acid Sequence; Binding Sites; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Hydrazones; Pichia; Protein-Lysine 6-Oxidase; Spectrum Analysis, Raman	1996
Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology (Reading, England), 1997, Volume: 143 ( Pt 2) Topics: Amines; Amino Acid Sequence; Copper; Dihydroxyphenylalanine; Klebsiella; Magnetic Resonance Spectroscopy; Metalloproteins; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Phenethylamines; Sequence Analysis; Sequence Homology, Amino Acid; Spectrophotometry; Subcellular Fractions	1997
The fungus Gibberella fujikuroi produces copper/topaquinone-containing amine oxidase when induced by N-butylamine. Biochemistry and molecular biology international, 1997, Volume: 41, Issue:1 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Butylamines; Dihydroxyphenylalanine; Gibberella; Molecular Sequence Data; Molecular Weight; Sequence Alignment; Substrate Specificity	1997
Mechanistic studies of topa quinone biogenesis in phenylethylamine oxidase. Biochemistry, 1997, Feb-25, Volume: 36, Issue:8 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Copper; Dihydroxyphenylalanine; Kinetics	1997
Reactions of the oxidized organic cofactor in copper-depleted bovine serum amine oxidase. The Biochemical journal, 1997, Jun-01, Volume: 324 ( Pt 2) Topics: Amine Oxidase (Copper-Containing); Animals; Benzylamines; Catalysis; Cattle; Copper; Dihydroxyphenylalanine; Enzyme Inhibitors; Fabaceae; Hydrazines; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Plant Proteins; Plants, Medicinal; Pyridines; Semicarbazides; Species Specificity	1997
Amine-oxidizing quinoproteins. Methods in enzymology, 1997, Volume: 280 Topics: Amino Acid Sequence; Coenzymes; Copper; Diabetes Mellitus; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Heart Failure; Humans; Indolequinones; Liver Cirrhosis; Lysine; Menkes Kinky Hair Syndrome; Metalloproteins; Mixed Function Oxygenases; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Protein-Lysine 6-Oxidase; Quinolones; Quinones; Semicarbazides; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Stereoisomerism; Substrate Specificity; Tryptophan	1997
Effect of metal on 2,4,5-trihydroxyphenylalanine (topa) quinone biogenesis in the Hansenula polymorpha copper amine oxidase. The Journal of biological chemistry, 1997, Aug-01, Volume: 272, Issue:31 Topics: Amine Oxidase (Copper-Containing); Copper; Dihydroxyphenylalanine; Escherichia coli; Pichia; Recombinant Proteins; Saccharomyces cerevisiae; Zinc	1997
Mechanism-based inactivation of a yeast methylamine oxidase mutant: implications for the functional role of the consensus sequence surrounding topaquinone. Biochemistry, 1997, Sep-23, Volume: 36, Issue:38 Topics: Consensus Sequence; Dihydroxyphenylalanine; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Methylamines; Models, Chemical; Molecular Conformation; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Schiff Bases; Spectrophotometry; Spectrum Analysis, Raman	1997
Topaquinone-dependent amine oxidases: identification of reaction intermediates by Raman spectroscopy. Biochemistry, 1997, Sep-23, Volume: 36, Issue:38 Topics: Amine Oxidase (Copper-Containing); Aniline Compounds; Arthrobacter; Dihydroxyphenylalanine; Methylamines; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen Isotopes; Recombinant Proteins; Spectrum Analysis, Raman	1997
Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry, 1997, Dec-23, Volume: 36, Issue:51 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Apoenzymes; Arthrobacter; Binding Sites; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Dimerization; Hydrogen Bonding; Metalloproteins; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Sequence Alignment; Substrate Specificity; Tyrosine	1997
Biosynthesis of the topaquinone cofactor in copper amine oxidases--evidence from model studies. European journal of biochemistry, 1998, Jan-15, Volume: 251, Issue:1-2 Topics: Aldehydes; Amine Oxidase (Copper-Containing); Benzene Derivatives; Benzoquinones; Binding Sites; Catalase; Catechols; Copper; Dihydroxyphenylalanine; Free Radical Scavengers; Hydroxylation; Oxidation-Reduction; Structure-Activity Relationship; Superoxide Dismutase; Zinc	1998
Identification of the quinone cofactor in mammalian semicarbazide-sensitive amine oxidase. Biochemistry, 1998, Apr-07, Volume: 37, Issue:14 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Aorta; Cattle; Chromatography, High Pressure Liquid; Coenzymes; Dihydroxyphenylalanine; Hydrolysis; Molecular Sequence Data; Peptide Fragments; Spectrum Analysis, Raman; Swine	1998
Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation. Structure (London, England : 1993), 1998, Mar-15, Volume: 6, Issue:3 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Histidine; Models, Molecular; Oxidation-Reduction; Oxygen; Pichia; Protein Conformation	1998
Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase. Biochemistry, 1998, Sep-08, Volume: 37, Issue:36 Topics: Amine Oxidase (Copper-Containing); Animals; Cattle; Dihydroxyphenylalanine; Electron Transport; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Oxygen Isotopes; Peroxides; Protons; Solvents; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Substrate Specificity; Titrimetry; Viscosity	1998
Exploring a channel to the active site of copper/topaquinone-containing phenylethylamine oxidase by chemical modification and site-specific mutagenesis. Biochemistry, 1998, Oct-06, Volume: 37, Issue:40 Topics: 4-Chloro-7-nitrobenzofurazan; Amine Oxidase (Copper-Containing); Amino Acid Sequence; Apoenzymes; Binding Sites; Copper; Cysteine; Dihydroxyphenylalanine; Dithionitrobenzoic Acid; Fluorescent Dyes; Histidine; Holoenzymes; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Substrate Specificity	1998
Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast. Biochemistry, 1998, Nov-24, Volume: 37, Issue:47 Topics: Alanine; Amine Oxidase (Copper-Containing); Amino Acid Sequence; Asparagine; Catalysis; Coenzymes; Conserved Sequence; Dihydroxyphenylalanine; Enzyme Activation; Kinetics; Methylamines; Mutagenesis, Site-Directed; Pichia; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet; Temperature	1998
Stoichiometry of the topa quinone biogenesis reaction in copper amine oxidases. Biochemistry, 1999, Mar-09, Volume: 38, Issue:10 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Dihydroxyphenylalanine; Dimerization; Hydrogen Peroxide; Oxidation-Reduction; Oxygen; Oxygen Consumption; Spectrophotometry, Ultraviolet	1999
Mutation of a strictly conserved, active-site residue alters substrate specificity and cofactor biogenesis in a copper amine oxidase. Biochemistry, 1999, Mar-23, Volume: 38, Issue:12 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalysis; Conserved Sequence; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Pichia; Protein Conformation; Saccharomyces cerevisiae; Schiff Bases; Substrate Specificity	1999
Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin. Biochemistry, 1999, Apr-13, Volume: 38, Issue:15 Topics: Bacterial Proteins; Catalysis; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Potassium Chloride; Pyridoxal Phosphate; Quinones; Spectrum Analysis	1999
Spectroscopic characterization of carbon monoxide complexes generated for copper/topa quinone-containing amine oxidases. Biochemistry, 1999, Oct-26, Volume: 38, Issue:43 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Aspergillus niger; Carbon Monoxide; Copper; Dihydroxyphenylalanine; Dithionite; Electron Spin Resonance Spectroscopy; Metalloproteins; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Substrate Specificity	1999
Visualization of dioxygen bound to copper during enzyme catalysis. Science (New York, N.Y.), 1999, Nov-26, Volume: 286, Issue:5445 Topics: Aerobiosis; Amine Oxidase (Copper-Containing); Anaerobiosis; Aspartic Acid; Binding Sites; Catalysis; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Dimerization; Electrons; Escherichia coli; Hydrogen Bonding; Nitric Oxide; Oxidation-Reduction; Oxygen; Phenethylamines; Protein Conformation; Protein Structure, Secondary; Protons; Spectrum Analysis	1999
Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast. Biochemistry, 2000, Apr-04, Volume: 39, Issue:13 Topics: Amine Oxidase (Copper-Containing); Asparagine; Aspartic Acid; Binding Sites; Coenzymes; Copper; Cysteine; Dihydroxyphenylalanine; Glutamic Acid; Glutamine; Histidine; Mutagenesis, Site-Directed; Oxygen Consumption; Pichia; Recombinant Proteins; Spectrophotometry, Atomic; Spectrophotometry, Ultraviolet	2000
Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast. Biochemistry, 2000, Apr-04, Volume: 39, Issue:13 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Coenzymes; Copper; Deuterium; Dihydroxyphenylalanine; Enzyme Precursors; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxygen; Oxygen Consumption; Pichia; Solvents; Temperature; Tyrosine; Viscosity	2000
The oxidation and reduction reactions of bovine serum amine oxidase. A kinetic study. European journal of biochemistry, 2000, Volume: 267, Issue:11 Topics: Amine Oxidase (Copper-Containing); Animals; Catalysis; Cattle; Coenzymes; Dihydroxyphenylalanine; Enzyme Inhibitors; Hydrazines; Kinetics; Oxidation-Reduction; Oxygen; Phenylhydrazines	2000
Copper-promoted overall transformation of 4-tert-butylphenol to its para-hydroxyquinonic derivative, 2-hydroxy-5-tert-butyl-1,4-benzoquinone. Biomimetic studies on the generation of topaquinone in copper amine oxidases. Bioorganic & medicinal chemistry letters, 2000, May-01, Volume: 10, Issue:9 Topics: Amine Oxidase (Copper-Containing); Benzoquinones; Copper; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Hydroxylation; Lysine; Oxidation-Reduction; Phenols; Quinones	2000
Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds. Biochemistry, 2000, Jun-27, Volume: 39, Issue:25 Topics: Amine Oxidase (Copper-Containing); Aspergillus niger; Binding Sites; Dihydroxyphenylalanine; Magnetic Resonance Spectroscopy; Protein Conformation	2000
Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli. Biochemistry, 2000, Aug-15, Volume: 39, Issue:32 Topics: Amine Oxidase (Copper-Containing); Catalytic Domain; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Models, Molecular; Oxidation-Reduction; Pichia; Protein Processing, Post-Translational; Recombinant Proteins; Tyrosine; Zinc	2000
Dopamine beta-hydroxylase inactivation generates a protein-bound quinone derivative. FEBS letters, 2001, Feb-23, Volume: 491, Issue:1-2 Topics: Animals; Ascorbic Acid; Cattle; Dihydroxyphenylalanine; Dopamine beta-Hydroxylase; Electrophoresis, Polyacrylamide Gel; Hydrogen Peroxide; Oxygen; Spectrophotometry, Ultraviolet; Tyramine; Ultraviolet Rays	2001
The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast. Biochemistry, 2001, Mar-06, Volume: 40, Issue:9 Topics: Amine Oxidase (Copper-Containing); Anaerobiosis; Catalysis; Coenzymes; Copper; Dihydroxyphenylalanine; Enzyme Inhibitors; Enzyme Precursors; Holoenzymes; Kinetics; Oxygen; Oxygen Consumption; Pichia; Sodium Azide; Titrimetry	2001
Spectroscopic observation of intermediates formed during the oxidative half-reaction of copper/topa quinone-containing phenylethylamine oxidase. Biochemistry, 2001, Dec-25, Volume: 40, Issue:51 Topics: Amine Oxidase (Copper-Containing); Catalysis; Copper; Dihydroxyphenylalanine; Micrococcaceae; Nickel; Oxidation-Reduction; Oxygen; Peroxides; Spectrophotometry, Ultraviolet; Substrate Specificity	2001
Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases. Biochemistry, 2002, Jan-15, Volume: 41, Issue:2 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Dihydroxyphenylalanine; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Models, Chemical; Mutation; Oxygen; Pichia; Protein Binding; Spectrum Analysis, Raman	2002
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue. The Biochemical journal, 2002, Aug-01, Volume: 365, Issue:Pt 3 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalysis; Coenzymes; Dihydroxyphenylalanine; Enzyme Inhibitors; Escherichia coli; Hydrogen-Ion Concentration; Molecular Structure; Mutation; Phenethylamines; Protein Binding; Tranylcypromine	2002
Human kidney diamine oxidase: heterologous expression, purification, and characterization. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2002, Volume: 7, Issue:6 Topics: Amine Oxidase (Copper-Containing); Amines; Animals; Binding Sites; Cell Line; Dihydroxyphenylalanine; Drosophila; Humans; Hydrogen-Ion Concentration; Kidney; Kinetics; Molecular Weight; Organ Specificity; Oxidation-Reduction; Phenylhydrazines; Recombinant Proteins	2002
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase. Nature structural biology, 2002, Volume: 9, Issue:8 Topics: Amine Oxidase (Copper-Containing); Apoenzymes; Arthrobacter; Catalytic Domain; Crystallography, X-Ray; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Models, Molecular; Protein Conformation; Spectrophotometry; Static Electricity	2002
Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry, 2002, Jul-30, Volume: 41, Issue:30 Topics: Amine Oxidase (Copper-Containing); Catalysis; Dihydroxyphenylalanine; Dimerization; Models, Molecular; Oxidation-Reduction	2002
Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases. European journal of biochemistry, 2002, Volume: 269, Issue:15 Topics: Amine Oxidase (Copper-Containing); Animals; Bacteria; Diamines; Dihydroxyphenylalanine; Drug Design; Enzyme Inhibitors; Mammals; Models, Molecular; Naphthalenes; Phenylhydrazines; Protein Conformation; Protein-Lysine 6-Oxidase; Species Specificity; Time Factors; Titrimetry	2002
Binding of dioxygen to non-metal sites in proteins: exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha. Biochemistry, 2002, Nov-19, Volume: 41, Issue:46 Topics: Amine Oxidase (Copper-Containing); Animals; Binding Sites; Catalysis; Cattle; Cobalt; Copper; Dihydroxyphenylalanine; DNA Primers; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Pichia; Polymerase Chain Reaction; Structure-Activity Relationship; Viscosity	2002
Induction and characterization of a novel amine oxidase from the yeast Kluyveromyces marxianus. Yeast (Chichester, England), 2003, Apr-15, Volume: 20, Issue:5 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Base Sequence; Benzylamine Oxidase; Chromatography, DEAE-Cellulose; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Glycosylation; Hydrogen-Ion Concentration; Isoelectric Point; Kinetics; Kluyveromyces; Molecular Sequence Data; Molecular Weight; Putrescine; Sequence Homology, Amino Acid; Ultrafiltration	2003
Gold electrodes wired for coupling with the deeply buried active site of Arthrobacter globiformis amine oxidase. Journal of the American Chemical Society, 2003, Jun-18, Volume: 125, Issue:24 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Binding Sites; Dihydroxyphenylalanine; Electrochemistry; Electrodes; Gold; Models, Molecular; Oxidation-Reduction	2003
Molecular cloning of complementary DNA encoding mouse seminal vesicle-secreted protein SVS I and demonstration of homology with copper amine oxidases. Biology of reproduction, 2003, Volume: 69, Issue:6 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins; Chromosome Mapping; Cloning, Molecular; Dihydroxyphenylalanine; DNA, Complementary; Exons; Glycosylation; Humans; Introns; Male; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Molecular Weight; Rats; Seminal Vesicle Secretory Proteins; Sequence Analysis; Sequence Homology, Amino Acid	2003
The crystal structure of Pichia pastoris lysyl oxidase. Biochemistry, 2003, Dec-30, Volume: 42, Issue:51 Topics: Amine Oxidase (Copper-Containing); Animals; Arthrobacter; Binding Sites; Crystallization; Crystallography, X-Ray; Dihydroxyphenylalanine; Dimerization; Fungal Proteins; Humans; Models, Molecular; Pichia; Pisum sativum; Protein Subunits; Protein-Lysine 6-Oxidase; Substrate Specificity	2003
Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor. Biochemistry, 2004, Mar-02, Volume: 43, Issue:8 Topics: Alanine; Amine Oxidase (Copper-Containing); Amines; Arthrobacter; Bacterial Proteins; Binding Sites; Coenzymes; Copper; Crystallization; Crystallography, X-Ray; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Histidine; Imidazoles; Mutagenesis, Site-Directed; Protein Binding; Substrate Specificity	2004
A theoretical study of the mechanism for the biogenesis of cofactor topaquinone in copper amine oxidases. Journal of the American Chemical Society, 2004, Mar-31, Volume: 126, Issue:12 Topics: Amine Oxidase (Copper-Containing); Combinatorial Chemistry Techniques; Crystallography, X-Ray; Dihydroxyphenylalanine; Models, Chemical; Models, Molecular; Molecular Structure; Thermodynamics	2004
Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation. Biochemistry, 2004, Aug-31, Volume: 43, Issue:34 Topics: Allylamine; Amine Oxidase (Copper-Containing); Animals; Arthrobacter; Cattle; Coenzymes; Crystallography, X-Ray; Diamines; Dihydroxyphenylalanine; Enzyme Inhibitors; Horses; Naphthalenes; Pargyline; Pichia; Pisum sativum; Propylamines; Protein-Lysine 6-Oxidase; Quinones	2004
A dopaquinone model that mimics the water addition step of cofactor biogenesis in copper amine oxidases. Journal of the American Chemical Society, 2005, Apr-06, Volume: 127, Issue:13 Topics: Amination; Amine Oxidase (Copper-Containing); Benzoquinones; Biomimetic Materials; Catechols; Coenzymes; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Kinetics; Ligands; Manganese; Oxidation-Reduction; Periodic Acid; Spectrophotometry, Ultraviolet; Water	2005
Reactions of plant copper/topaquinone amine oxidases with N6-aminoalkyl derivatives of adenine. Journal of enzyme inhibition and medicinal chemistry, 2005, Volume: 20, Issue:2 Topics: Adenine; Amine Oxidase (Copper-Containing); Cytokinins; Dihydroxyphenylalanine; Enzyme Inhibitors; Hydrogen-Ion Concentration; Kinetics; Lens Plant; Models, Chemical; Pisum sativum; Plant Extracts; Plants; Plants, Medicinal; Spectrophotometry; Substrate Specificity; Temperature	2005
Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. Acta crystallographica. Section D, Biological crystallography, 2005, Volume: 61, Issue:Pt 11 Topics: Amine Oxidase (Copper-Containing); Amino Acid Motifs; Binding Sites; Cell Adhesion Molecules; Cell Line; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Humans; Models, Molecular; Protein Conformation; Pyridones	2005
2,4,5-Trihydroxyphenylalanine quinone biogenesis in the copper amine oxidase from Hansenula polymorpha with the alternate metal nickel. Biochemistry, 2005, Nov-01, Volume: 44, Issue:43 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Dihydroxyphenylalanine; Kinetics; Metals; Nickel; Oxygen; Pichia; Protein Processing, Post-Translational; Tyrosine	2005
Mapping the primary structure of copper/topaquinone-containing methylamine oxidase from Aspergillus niger. Folia microbiologica, 2005, Volume: 50, Issue:5 Topics: Amino Acid Sequence; Aspergillus niger; Chromatography, Liquid; Computational Biology; Copper; Dihydroxyphenylalanine; Isoelectric Focusing; Isoelectric Point; Molecular Sequence Data; Molecular Weight; Oxidoreductases Acting on CH-NH Group Donors; Peptide Mapping; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin	2005
Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction. Biochemical and biophysical research communications, 2006, Apr-07, Volume: 342, Issue:2 Topics: Amine Oxidase (Copper-Containing); Amino Acid Substitution; Bacterial Proteins; Crystallography, X-Ray; Deuterium; Dihydroxyphenylalanine; Kinetics; Mutation; Oxidation-Reduction; Phenethylamines; Protein Structure, Tertiary; Quantum Theory; Spectrophotometry, Ultraviolet; Temperature	2006
Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha. Biochemistry, 2006, Mar-14, Volume: 45, Issue:10 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalysis; Coenzymes; Conserved Sequence; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Ethylamines; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylhydrazines; Pichia; Tyrosine	2006
Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase. Biochemistry, 2006, Apr-04, Volume: 45, Issue:13 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Arthrobacter; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Dihydroxyphenylalanine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Oxidation-Reduction; Schiff Bases; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman	2006
Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits. Biochemistry, 2006, Apr-11, Volume: 45, Issue:14 Topics: Amine Oxidase (Copper-Containing); Copper; Dihydroxyphenylalanine; Kinetics; Models, Chemical; Oxidation-Reduction; Pichia; Protein Structure, Quaternary; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry; Zinc	2006
Investigation of Cu(I)-dependent 2,4,5-trihydroxyphenylalanine quinone biogenesis in Hansenula polymorpha amine oxidase. The Journal of biological chemistry, 2006, Jul-28, Volume: 281, Issue:30 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Kinetics; Models, Chemical; Pichia; Spectrophotometry; Superoxides; Tyrosine; Ultraviolet Rays	2006
Properties of copper-free pig kidney amine oxidase: role of topa quinone. FEBS letters, 2006, Aug-07, Volume: 580, Issue:18 Topics: Amine Oxidase (Copper-Containing); Aniline Compounds; Animals; Apoenzymes; Benzylamines; Catalysis; Copper; Dihydroxyphenylalanine; Kidney; Kinetics; Swine	2006
Intramolecular electron transfer rate between active-site copper and TPQ in Arthrobacter globiformis amine oxidase. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006, Volume: 11, Issue:8 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Binding Sites; Catalysis; Copper; Dihydroxyphenylalanine; Electron Transport; Hydrogen-Ion Concentration; Kinetics; Oxidation-Reduction; Temperature	2006
An important lysine residue in copper/quinone-containing amine oxidases. The FEBS journal, 2007, Volume: 274, Issue:10 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Binding Sites; Cattle; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Euphorbia; Kidney; Kinetics; Lens Plant; Lysine; Nuclear Magnetic Resonance, Biomolecular; Pisum sativum; Sequence Alignment; Swine; Xenon Isotopes	2007
Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis. Journal of the American Chemical Society, 2007, Sep-19, Volume: 129, Issue:37 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Benzoquinones; Binding Sites; Crystallography, X-Ray; Dihydroxyphenylalanine; Escherichia coli; Hydrogen Bonding; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman	2007
Electroactive centers in Euphorbia latex and lentil seedling amine oxidases. Bioscience, biotechnology, and biochemistry, 2008, Volume: 72, Issue:1 Topics: Amine Oxidase (Copper-Containing); Amino Acid Oxidoreductases; Amino Acid Sequence; Binding Sites; Copper; Dihydroxyphenylalanine; Electrochemistry; Electrodes; Euphorbia; Kinetics; Lens Plant; Molecular Sequence Data; Oxidation-Reduction; Plant Proteins; Seedlings	2008
Further insight into the mechanism of stereoselective proton abstraction by bacterial copper amine oxidase. Biochemistry, 2008, Jul-22, Volume: 47, Issue:29 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Bacterial Proteins; Crystallography, X-Ray; Deuterium; Dihydroxyphenylalanine; Ethylamines; Magnetic Resonance Spectroscopy; Models, Molecular; Phenethylamines; Stereoisomerism; Substrate Specificity	2008
Structural organization of mammalian copper-containing amine oxidase genes. Inflammation research : official journal of the European Histamine Research Society ... [et al.], 2010, Volume: 59 Suppl 2 Topics: Amine Oxidase (Copper-Containing); Animals; Catalytic Domain; Chromosome Mapping; Cloning, Molecular; Dihydroxyphenylalanine; Gene Expression Regulation, Enzymologic; Gene Library; Humans; Mice; Open Reading Frames; Protein Folding; Rats; Species Specificity; Swine	2010
Exploring the roles of the metal ions in Escherichia coli copper amine oxidase. Biochemistry, 2010, Feb-16, Volume: 49, Issue:6 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Calcium; Catalytic Domain; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Edetic Acid; Enzyme Activation; Escherichia coli Proteins; Humans; Metals, Alkaline Earth; Metals, Heavy; Molecular Sequence Data; Oxidation-Reduction; Protein Binding	2010
Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity. Biochemistry, 2010, Aug-31, Volume: 49, Issue:34 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Mutation; Oxidation-Reduction; Oxygenases; Pichia; Tyrosine	2010
Correlation of active site metal content in human diamine oxidase with trihydroxyphenylalanine quinone cofactor biogenesis . Biochemistry, 2010, Sep-28, Volume: 49, Issue:38 Topics: Amine Oxidase (Copper-Containing); Benzoquinones; Binding Sites; Copper; Dihydroxyphenylalanine; Humans; Metals; Quinones; Recombinant Proteins; X-Ray Diffraction; Zinc	2010
Detection of the reaction intermediates catalyzed by a copper amine oxidase. Journal of synchrotron radiation, 2011, Volume: 18, Issue:1 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Catalysis; Crystallography, X-Ray; Dihydroxyphenylalanine; Phenethylamines; Schiff Bases; X-Ray Diffraction	2011
Structural and enzyme activity studies demonstrate that aryl substituted 2,3-butadienamine analogs inactivate Arthrobacter globiformis amine oxidase (AGAO) by chemical derivatization of the 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor. Biochimica et biophysica acta, 2011, Volume: 1814, Issue:5 Topics: Amine Oxidase (Copper-Containing); Amines; Arthrobacter; Coenzymes; Dihydroxyphenylalanine; Models, Molecular; Molecular Structure	2011
Reactions of copper(II)-phenol systems with O2: models for TPQ biosynthesis in copper amine oxidases. Inorganic chemistry, 2011, Mar-07, Volume: 50, Issue:5 Topics: Amine Oxidase (Copper-Containing); Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Models, Chemical; Oxygen; Phenol; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Fast Atom Bombardment; Spectroscopy, Fourier Transform Infrared	2011
Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3. Biochemistry, 2011, Jun-21, Volume: 50, Issue:24 Topics: Amine Oxidase (Copper-Containing); Amino Acid Substitution; Animals; Binding Sites; Catalytic Domain; Cell Adhesion Molecules; CHO Cells; Cricetinae; Cricetulus; Crystallography, X-Ray; Dihydroxyphenylalanine; Disulfides; Humans; Hydrogen Bonding; Imidazoles; In Vitro Techniques; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Spectrophotometry; Substrate Specificity	2011
Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors. Journal of biochemistry, 2012, Volume: 151, Issue:2 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Bacterial Proteins; Binding Sites; Catalysis; Dihydroxyphenylalanine; Enzyme Inhibitors; Hydrazines; Hydrolysis; Kinetics; Oxidation-Reduction; Schiff Bases; Substrate Specificity	2012
A biologically inspired Cu(I)/topaquinone-like co-catalytic system for the highly atom-economical aerobic oxidation of primary amines to imines. Angewandte Chemie (International ed. in English), 2012, May-29, Volume: 51, Issue:22 Topics: Amines; Catalysis; Copper; Dihydroxyphenylalanine; Imines; Magnetic Resonance Spectroscopy; Molecular Structure; Oxidation-Reduction	2012
The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase. International journal of molecular sciences, 2012, Volume: 13, Issue:5 Topics: Amine Oxidase (Copper-Containing); Animals; Coenzymes; Crystallography, X-Ray; Dihydroxyphenylalanine; Humans; Models, Molecular; Protein Biosynthesis; Protein Conformation; Protein Processing, Post-Translational	2012
Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha. Biochemistry, 2013, Apr-02, Volume: 52, Issue:13 Topics: Amine Oxidase (Copper-Containing); Benzylamines; Catalytic Domain; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Ethylamines; Kinetics; Models, Molecular; Pichia; Protein Binding; Protein Conformation; Substrate Specificity	2013
Cu(II)-mediated phenol oxygenation: chemical evidence implicates a unique role of the enzyme active site in promoting the chemically difficult tyrosine monooxygenation in TPQ cofactor biogenesis of copper amine oxidases. Bioorganic chemistry, 2015, Volume: 59 Topics: Amine Oxidase (Copper-Containing); Catalytic Domain; Coenzymes; Copper; Dihydroxyphenylalanine; Oxidation-Reduction; Oxygen; Phenols; Tyrosine	2015
Characterization of recombinant human diamine oxidase (rhDAO) produced in Chinese Hamster Ovary (CHO) cells. Journal of biotechnology, 2016, Jun-10, Volume: 227 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Blotting, Western; CHO Cells; Chromatography, Liquid; Circular Dichroism; Coenzymes; Cricetinae; Cricetulus; Dihydroxyphenylalanine; Electrophoresis, Polyacrylamide Gel; Gene Expression; Glycosylation; Humans; Kinetics; Metals; Peptides; Phenylhydrazines; Polysaccharides; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Substrate Specificity	2016
Proceedings of the National Academy of Sciences of the United States of America, 2019, 01-02, Volume: 116, Issue:1 Topics: Amine Oxidase (Copper-Containing); Arthrobacter; Catalysis; Coenzymes; Dihydroxyphenylalanine; Molecular Conformation; Temperature; Thermodynamics; X-Ray Diffraction	2019
Characterization of the Preprocessed Copper Site Equilibrium in Amine Oxidase and Assignment of the Reactive Copper Site in Topaquinone Biogenesis. Journal of the American Chemical Society, 2019, 06-05, Volume: 141, Issue:22 Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalytic Domain; Copper; Dihydroxyphenylalanine; Models, Molecular	2019