메뉴 건너뛰기




Volumn 61, Issue , 2001, Pages 219-239

Mechanisms of biosynthesis of protein-derived redox cofactors

Author keywords

[No Author keywords available]

Indexed keywords

6 HYDROXYDOPA QUINONE; 6-HYDROXYDOPA QUINONE; AMINO ACID; DOPA; DRUG DERIVATIVE; GALACTOSE OXIDASE; INDOLE DERIVATIVE; LYSINE; LYSINE TYROSYLQUINONE; OXIDOREDUCTASE; QUINONE DERIVATIVE; TRYPTOPHAN; TRYPTOPHAN TRYPTOPHYLQUINONE;

EID: 0035227063     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0083-6729(01)61007-0     Document Type: Review
Times cited : (14)

References (41)
  • 3
    • 0000687067 scopus 로고    scopus 로고
    • Circulating semicarbazide-sensitive amine oxidase is raised both in type I (insulin-dependent), type II (non-insulin-dependent) diabetes mellitus and even in childhood type I diabetes at first clinical diagnosis
    • F Boomsma A.H van der Meiracker S Winkel H.J Aanstoot M.R Batstra A.J Man in't Veld G.J Bruining Circulating semicarbazide-sensitive amine oxidase is raised both in type I (insulin-dependent), type II (non-insulin-dependent) diabetes mellitus and even in childhood type I diabetes at first clinical diagnosis Diabetologia 42 1999 233 237
    • (1999) Diabetologia , vol.42 , pp. 233-237
    • Boomsma, F1    van der Meiracker, A.H2    Winkel, S3    Aanstoot, H.J4    Batstra, M.R5    Man in't Veld, A.J6    Bruining, G.J7
  • 4
    • 0028605705 scopus 로고
    • Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
    • D Cai J.P Klinman Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase J. Biol. Chem. 269 1994 32039 32042
    • (1994) J. Biol. Chem. , vol.269 , pp. 32039-32042
    • Cai, D1    Klinman, J.P2
  • 5
    • 0030840721 scopus 로고    scopus 로고
    • Effect of metal on 2,4,5-trihydroxyphenylalanine (TOPA) quinone biogenesis in the Hansenula polymorpha copper amine oxidase
    • D Cai N.K Williams J.P Klinman Effect of metal on 2,4,5-trihydroxyphenylalanine (TOPA) quinone biogenesis in the Hansenula polymorpha copper amine oxidase J. Biol. Chem. 272 21 1997 19277 19281
    • (1997) J. Biol. Chem. , vol.272 , Issue.21 , pp. 19277-19281
    • Cai, D1    Williams, N.K2    Klinman, J.P3
  • 6
    • 0034663974 scopus 로고    scopus 로고
    • Crystal structure at 2.5 A resolution of Zn-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli
    • Z.-W Chen B Schwartz N.K Williams R Li J.P Klinman F.S Matthews Crystal structure at 2.5 A resolution of Zn-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli Biochemistry 39 2000 9709 9717
    • (2000) Biochemistry , vol.39 , pp. 9709-9717
    • Chen, Z.-W1    Schwartz, B2    Williams, N.K3    Li, R4    Klinman, J.P5    Matthews, F.S6
  • 7
    • 0025087101 scopus 로고
    • Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: Evidence for two tryptophan residues involved in the active center
    • A.Y Chistoserdov Y.D Tsygankov M.E Lidstrom Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: Evidence for two tryptophan residues involved in the active center Biochem. Biophys. Res. Commun. 172 1990 211 216
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 211-216
    • Chistoserdov, A.Y1    Tsygankov, Y.D2    Lidstrom, M.E3
  • 8
    • 0031434174 scopus 로고    scopus 로고
    • Micro-injection of recombinant lysyl oxidase blocks oncogenic p2I-Ha-Ras and progesterone effects on Xenopus laevis oocyte production
    • A.D Donato J.C Lacal M.D Duca M Giampuzzi G Ghiggeri R Gusmano Micro-injection of recombinant lysyl oxidase blocks oncogenic p2I-Ha-Ras and progesterone effects on Xenopus laevis oocyte production FEBS Lett. 419 1997 63 68
    • (1997) FEBS Lett. , vol.419 , pp. 63-68
    • Donato, A.D1    Lacal, J.C2    Duca, M.D3    Giampuzzi, M4    Ghiggeri, G5    Gusmano, R6
  • 9
    • 85120123084 scopus 로고    scopus 로고
    • Galactose oxidase pro-sequence cleavage and cofactor assembly are self-processing reactions
    • D.M Dooley Galactose oxidase pro-sequence cleavage and cofactor assembly are self-processing reactions J. Am. Chem. Soc. 122 2000 990 991
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 990-991
    • Dooley, D.M1
  • 10
    • 0034603777 scopus 로고    scopus 로고
    • 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
    • J.E Dove B Schwartz N.K Williams J.P Klinman 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 39 13 2000 3699 3707
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3699-3707
    • Dove, J.E1    Schwartz, B2    Williams, N.K3    Klinman, J.P4
  • 11
    • 0003041009 scopus 로고    scopus 로고
    • Radical reactions featuring lysine 2,3-aminomutase
    • P.A Frey Radical reactions featuring lysine 2,3-aminomutase Comp. Nat. Prod. Chem. 5 1999 371 400
    • (1999) Comp. Nat. Prod. Chem. , vol.5 , pp. 371-400
    • Frey, P.A1
  • 12
    • 0032706535 scopus 로고    scopus 로고
    • Mechanisms of sulfoxidation catalyzed by high-valent intermediates of heme enzymes: Electrontransfer vs. oxygen-transfer mechanism
    • Y Goto T Matsui S Ozaki Y Watanabe S Fukuzumi Mechanisms of sulfoxidation catalyzed by high-valent intermediates of heme enzymes: Electrontransfer vs. oxygen-transfer mechanism J. Am. Chem. Soc. 121 1999 9497 9502
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9497-9502
    • Goto, Y1    Matsui, T2    Ozaki, S3    Watanabe, Y4    Fukuzumi, S5
  • 13
    • 0032788792 scopus 로고    scopus 로고
    • Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides
    • M.E Graichen L.H Jones B Sharma R.J.M van Spanning J.P Hosler V.L Davidson Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides J. Bacteriol. 181 1999 4216 4222
    • (1999) J. Bacteriol. , vol.181 , pp. 4216-4222
    • Graichen, M.E1    Jones, L.H2    Sharma, B3    van Spanning, R.J.M4    Hosler, J.P5    Davidson, V.L6
  • 14
    • 0344131951 scopus 로고    scopus 로고
    • Learning nature's strategies for making deoxy sugars Pathways, mechanisms, and combinatorial applications
    • T.M Hallis H.W Liu Learning nature's strategies for making deoxy sugars Pathways, mechanisms, and combinatorial applications Acc. Chem. Res. 32 1999 579 588
    • (1999) Acc. Chem. Res. , vol.32 , pp. 579-588
    • Hallis, T.M1    Liu, H.W2
  • 15
    • 0014209801 scopus 로고
    • Electrochemical studies of the oxidation pathways of catecholamines
    • M.D Hawley S.V Tatawawadi S Piekarski R.N Adams Electrochemical studies of the oxidation pathways of catecholamines J. Am. Chem. Soc. 89 2 1967 447 450
    • (1967) J. Am. Chem. Soc. , vol.89 , Issue.2 , pp. 447-450
    • Hawley, M.D1    Tatawawadi, S.V2    Piekarski, S3    Adams, R.N4
  • 16
    • 0020648930 scopus 로고
    • Amino acid sequence studies of the light subunit of methylamine dehydrogenase from Pseudomonas AM1: Existence of two residues binding the prosthetic group
    • Y Ishii T Hase Y Fukumori H Matsubara J Tobari Amino acid sequence studies of the light subunit of methylamine dehydrogenase from Pseudomonas AM1: Existence of two residues binding the prosthetic group J. Biochem. (Tokyo) 93 1983 107 119
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 107-119
    • Ishii, Y1    Hase, T2    Fukumori, Y3    Matsubara, H4    Tobari, J5
  • 17
    • 0029120081 scopus 로고
    • Model studies of cofactor tryptophan tryptophylquinone
    • S Itoh Y Ohshiro Model studies of cofactor tryptophan tryptophylquinone J.P Klinman Methods in Enzymology Vol. 258 1995 Academic Press San Diego, CA 164 176
    • (1995) , pp. 164-176
    • Itoh, S1    Ohshiro, Y2
  • 19
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-Hydroxydopa at the active site of bovine serum amine oxidase
    • S.M Janes D Mu D Wemmer A.J Smith S Kaur D Maltby A.L Burlingame J.P Klinman A new redox cofactor in eukaryotic enzymes: 6-Hydroxydopa at the active site of bovine serum amine oxidase Science 248 1990 981 987
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M1    Mu, D2    Wemmer, D3    Smith, A.J4    Kaur, S5    Maltby, D6    Burlingame, A.L7    Klinman, J.P8
  • 22
    • 0030932016 scopus 로고    scopus 로고
    • Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase
    • K Ma A Hutchins S.-J.S Sung M.W.W Adams Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus , functions as a CoA-dependent pyruvate decarboxylase Proc. Natl. Acad. Sci. U.S.A. 94 1997 9608 9613
    • (1997) , pp. 9608-9613
    • Ma, K1    Hutchins, A2    Sung, S.-J.S3    Adams, M.W.W4
  • 23
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
    • R Matsuzaki T Fukui H Sato Y Ozaki K Tanizawa Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue FEBS Lett. 351 1994 360 364
    • (1994) FEBS Lett. , vol.351 , pp. 360-364
    • Matsuzaki, R1    Fukui, T2    Sato, H3    Ozaki, Y4    Tanizawa, K5
  • 24
    • 85120146816 scopus 로고
    • W.S McIntire C Hartmann V.L Davidson Principles and Applications of Quinoproteins 1993 Dekker New York 97 172
    • (1993) , pp. 97-172
    • McIntire, W.S1    Hartmann, C2
  • 25
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • W.S McIntire D.E Wemmer A Chistoserdov M.E Lidstrom A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase Science 252 1991 817 824
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S1    Wemmer, D.E2    Chistoserdov, A3    Lidstrom, M.E4
  • 26
    • 84889288508 scopus 로고    scopus 로고
    • A non-redox role for copper during catalysis by a copper amine oxidase from yeast
    • S.A Mills J.P Klinman A non-redox role for copper during catalysis by a copper amine oxidase from yeast J. Am. Chem. Soc. 2000 in press
    • (2000) J. Am. Chem. Soc.
    • Mills, S.A1    Klinman, J.P2
  • 27
    • 0029867254 scopus 로고    scopus 로고
    • Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: Evidence from resonance Raman spectroscopy of model compounds
    • P Moenne-Loccoz N Nakamura S Itoh S Fukuzumi A.C.F Gorren J.A Duine J Sanders-Loehr Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: Evidence from resonance Raman spectroscopy of model compounds Biochemistry 35 1996 4713 4720
    • (1996) Biochemistry , vol.35 , pp. 4713-4720
    • Moenne-Loccoz, P1    Nakamura, N2    Itoh, S3    Fukuzumi, S4    Gorren, A.C.F5    Duine, J.A6    Sanders-Loehr, J7
  • 28
    • 0026722905 scopus 로고
    • Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases
    • D Mu S.M Janes A.J Smith D.E Brown D.M Dooley J.P Klinman Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases J. Biol. Chem. 267 1992 7979 7982
    • (1992) J. Biol. Chem. , vol.267 , pp. 7979-7982
    • Mu, D1    Janes, S.M2    Smith, A.J3    Brown, D.E4    Dooley, D.M5    Klinman, J.P6
  • 29
    • 85120116465 scopus 로고    scopus 로고
    • Mure, M., and Klinman, J. P. (2000). Manuscript in preparation.
  • 30
    • 0029926099 scopus 로고    scopus 로고
    • Biosynthesis of topa quinone cofactor in bacterial amine oxidases: Solvent origin of C-2 oxygen determined by raman spectroscopy
    • N Nakamura R Matsuzaki Y-H Choi K Tanizawa J Sanders-Loehr Biosynthesis of topa quinone cofactor in bacterial amine oxidases: Solvent origin of C-2 oxygen determined by raman spectroscopy J. Biol. Chem. 271 9 1996 4718 4724
    • (1996) J. Biol. Chem. , vol.271 , Issue.9 , pp. 4718-4724
    • Nakamura, N1    Matsuzaki, R2    Choi, Y-H3    Tanizawa, K4    Sanders-Loehr, J5
  • 31
    • 0030590845 scopus 로고    scopus 로고
    • Expression of active, human lysyl oxidase in Escherichia coli
    • M Ouzzine A Boyd D.J.S Hulmes Expression of active, human lysyl oxidase in Escherichia coli FEBS Lett. 399 1996 215 219
    • (1996) FEBS Lett. , vol.399 , pp. 215-219
    • Ouzzine, M1    Boyd, A2    Hulmes, D.J.S3
  • 32
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • L Que Jr. R.Y.N Ho Dioxygen activation by enzymes with mononuclear non-heme iron active sites Chem. Rev. 96 1996 2607 2624
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que, L1    Ho, R.Y.N2
  • 33
    • 0034603707 scopus 로고    scopus 로고
    • A kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast
    • B Schwartz J.E Dove J.P Klinman A kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast Biochemistry 39 13 2000 3708 3717
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3708-3717
    • Schwartz, B1    Dove, J.E2    Klinman, J.P3
  • 34
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • J Stubbe W.A van der Donk Protein radicals in enzyme catalysis Chem. Rev. 98 1998 705 762
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J1    van der Donk, W.A2
  • 35
    • 0032497371 scopus 로고    scopus 로고
    • Probing the mechanism of proton coupled electron transfer to dioxygen: The oxidative half-reaction of bovine serum amine oxidase
    • Q Su J.P Klinman Probing the mechanism of proton coupled electron transfer to dioxygen: The oxidative half-reaction of bovine serum amine oxidase Biochemistry 37 1998 12513 12525
    • (1998) Biochemistry , vol.37 , pp. 12513-12525
    • Su, Q1    Klinman, J.P2
  • 37
    • 0032559208 scopus 로고    scopus 로고
    • Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl radical reactivity
    • Y Wang J.L Dubois B Hedman K.O Hodgson T.D.P Stack Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl radical reactivity Science 279 1998 537 540
    • (1998) Science , vol.279 , pp. 537-540
    • Wang, Y1    Dubois, J.L2    Hedman, B3    Hodgson, K.O4    Stack, T.D.P5
  • 38
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone
    • M.C.J Wilce D.M Dooley H.C Freeman J.M Guss H Matsunami W.S McIntire C.E Ruggiero K Tanizawa H Yamaguchi Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone Biochemistry 36 1997 16116 16133
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.J1    Dooley, D.M2    Freeman, H.C3    Guss, J.M4    Matsunami, H5    McIntire, W.S6    Ruggiero, C.E7    Tanizawa, K8    Yamaguchi, H9
  • 39
    • 85120138297 scopus 로고    scopus 로고
    • M.S Wolin K.M Mohazzab-H J.G Scandalios Oxidative Stress and the Molecular Biology of Antioxidant Defenses 1997 Cold Spring Harbor Lab. Press Plainview, NY 21 48
    • (1997) , pp. 21-48
    • Wolin, M.S1    Mohazzab-H, K.M2
  • 40
    • 0019160926 scopus 로고
    • Electrochemical study of the oxidation of Ó-methyldopa and 5,6-dihydroxy-2-methylindole
    • T.E Young B.W Babbitt L.A Wolfe Electrochemical study of the oxidation of Ó-methyldopa and 5,6-dihydroxy-2-methylindole J. Org. Chem. 45 1980 2899 2902
    • (1980) J. Org. Chem. , vol.45 , pp. 2899-2902
    • Young, T.E1    Babbitt, B.W2    Wolfe, L.A3
  • 41
    • 0031833636 scopus 로고    scopus 로고
    • Methylamine dehydrogenase is a light-dependent oxidase
    • Z Zhu V.L Davidson Methylamine dehydrogenase is a light-dependent oxidase Biochim. Biophys. Acta 1364 1998 297 300
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 297-300
    • Zhu, Z1    Davidson, V.L2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.