메뉴 건너뛰기




Volumn 21, Issue 6, 2006, Pages 783-787

Inhibition of choline oxidase by quinoid dyes

Author keywords

Choline oxidase; Enzyme inhibition; Malachite green; Meldola blue; Methylene blue; Nile blue

Indexed keywords

CHOLINE; CHOLINE OXIDASE; DYE; LEUKOMALACHITE GREEN; MALACHITE GREEN; MELDOLA BLUE; METHYLENE BLUE; NILE BLUE SULFATE; NILE RED; PHENOTHIAZINE DERIVATIVE; PHENOXAZINE DERIVATIVE;

EID: 33845763402     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360600829530     Document Type: Article
Times cited : (7)

References (27)
  • 1
    • 0042622631 scopus 로고    scopus 로고
    • Kinetic mechanism of choline oxidase from arthrobacter globiformis
    • Gadda, G. (2003) Kinetic mechanism of choline oxidase from arthrobacter globiformis Biochim Biophys Acta, 1646, pp. 112-118.
    • (2003) Biochim Biophys Acta , vol.1646 , pp. 112-118
    • Gadda, G.1
  • 2
    • 32444447830 scopus 로고    scopus 로고
    • Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde
    • Fan, F and Germann, MW and Gadda, G. (2006) Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde Biochemistry, 45, pp. 1979-1986.
    • (2006) Biochemistry , vol.45 , pp. 1979-1986
    • Fan, F.1    Germann, M.W.2    Gadda, G.3
  • 3
    • 0037178195 scopus 로고    scopus 로고
    • Construction of an acetylcholinesterase-choline oxidase biosensor for aldicarb determination
    • Kok, FN and Bozoglu, F and Hasirci, V. (2002) Construction of an acetylcholinesterase-choline oxidase biosensor for aldicarb determination Biosens Bioelectron, 17, pp. 531-539.
    • (2002) Biosens Bioelectron , vol.17 , pp. 531-539
    • Kok, F.N.1    Bozoglu, F.2    Hasirci, V.3
  • 4
    • 1842835758 scopus 로고    scopus 로고
    • Amperometric determination of choline released from rat submandibular gland acinar cells using a choline oxidase biosensor
    • Razola, SS and Pochet, S and Grosfils, K and Kauffmann, JM. (2003) Amperometric determination of choline released from rat submandibular gland acinar cells using a choline oxidase biosensor Biosens Bioelectron, 18, pp. 185-191.
    • (2003) Biosens Bioelectron , vol.18 , pp. 185-191
    • Razola, S.S.1    Pochet, S.2    Grosfils, K.3    Kauffmann, J.M.4
  • 5
    • 0035142718 scopus 로고    scopus 로고
    • The use of bacterial choline oxidase, a glycinebetaine-synthesizing enzyme, to create stress-resistant transgenic plants
    • Sakamoto, A and Murata, N. (2001) The use of bacterial choline oxidase, a glycinebetaine-synthesizing enzyme, to create stress-resistant transgenic plants Plant Physiol, 125, pp. 180-188.
    • (2001) Plant Physiol , vol.125 , pp. 180-188
    • Sakamoto, A.1    Murata, N.2
  • 6
    • 0033764221 scopus 로고    scopus 로고
    • Genetic engineering of glycinebetaine production toward enhancing stress tolerance in plants: Metabolic limitations
    • Huang, J and Hirji, R and Adam, L and Rozwadowski, KL and Hammerlindl, JK and Keller, WA and Selvaraj, G. (2000) Genetic engineering of glycinebetaine production toward enhancing stress tolerance in plants: Metabolic limitations Plant Physiol, 122, pp. 747-756.
    • (2000) Plant Physiol , vol.122 , pp. 747-756
    • Huang, J.1    Hirji, R.2    Adam, L.3    Rozwadowski, K.L.4    Hammerlindl, J.K.5    Keller, W.A.6    Selvaraj, G.7
  • 7
    • 0025965867 scopus 로고
    • Choline oxidase, a catabolic enzyme in arthrobacter pascens, facilitates adaptation to osmotic stress in escherichia coli
    • Rozwadowski, KL and Khachatourians, GG and Selvaraj, G. (1991) Choline oxidase, a catabolic enzyme in arthrobacter pascens, facilitates adaptation to osmotic stress in escherichia coli J Bacteriol, 173, pp. 472-478.
    • (1991) J Bacteriol , vol.173 , pp. 472-478
    • Rozwadowski, K.L.1    Khachatourians, G.G.2    Selvaraj, G.3
  • 8
    • 0017666851 scopus 로고
    • Purification and characterization of choline oxidase from arthrobacter globiformis
    • Ikuta, S and Imamura, S and Misaki, H and Horiuti, Y. (1977) Purification and characterization of choline oxidase from arthrobacter globiformis J Biochem (Tokyo), 82, pp. 1741-1749.
    • (1977) J Biochem (Tokyo) , vol.82 , pp. 1741-1749
    • Ikuta, S.1    Imamura, S.2    Misaki, H.3    Horiuti, Y.4
  • 9
    • 0019039047 scopus 로고
    • Identification and properties of the prosthetic group of choline oxidase from alcaligenes sp
    • Ohta-Fukuyama, M and Miyake, Y and Emi, S and Yamano, T. (1980) Identification and properties of the prosthetic group of choline oxidase from alcaligenes sp. J Biochem (Tokyo), 88, pp. 197-203.
    • (1980) J Biochem (Tokyo) , vol.88 , pp. 197-203
    • Ohta-Fukuyama, M.1    Miyake, Y.2    Emi, S.3    Yamano, T.4
  • 10
    • 0023082653 scopus 로고
    • A simplified method of production of choline oxidase suitable for choline assay
    • Lartillot, S. (1987) A simplified method of production of choline oxidase suitable for choline assay Prep Biochem, 17, pp. 283-295.
    • (1987) Prep Biochem , vol.17 , pp. 283-295
    • Lartillot, S.1
  • 11
    • 0348109494 scopus 로고    scopus 로고
    • Cloning, sequence analysis and purification of choline oxidase from arthrobacter globiformis: A bacterial enzyme involved in osmotic stress tolerance
    • Fan, F and Ghanem, M and Gadda, G. (2004) Cloning, sequence analysis and purification of choline oxidase from arthrobacter globiformis: A bacterial enzyme involved in osmotic stress tolerance Arch Biochem Biophys, 421, pp. 149-158.
    • (2004) Arch Biochem Biophys , vol.421 , pp. 149-158
    • Fan, F.1    Ghanem, M.2    Gadda, G.3
  • 12
    • 0347594221 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of recombinant choline oxidase from arthrobacter globiformis
    • Ghanem, M and Fan, F and Francis, K and Gadda, G. (2003) Spectroscopic and kinetic properties of recombinant choline oxidase from arthrobacter globiformis Biochemistry, 42, pp. 15179-15188.
    • (2003) Biochemistry , vol.42 , pp. 15179-15188
    • Ghanem, M.1    Fan, F.2    Francis, K.3    Gadda, G.4
  • 13
    • 0038807899 scopus 로고    scopus 로고
    • Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from arthrobacter globiformis
    • Rand, T and Halkier, T and Hansen, OC. (2003) Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from arthrobacter globiformis Biochemistry, 42, pp. 7188-7194.
    • (2003) Biochemistry , vol.42 , pp. 7188-7194
    • Rand, T.1    Halkier, T.2    Hansen, O.C.3
  • 14
    • 12344271332 scopus 로고    scopus 로고
    • On the catalytic mechanism of choline oxidase
    • Fan, F and Gadda, G. (2005) On the catalytic mechanism of choline oxidase J Am Chem Soc, 127, pp. 2067-2074.
    • (2005) J Am Chem Soc , vol.127 , pp. 2067-2074
    • Fan, F.1    Gadda, G.2
  • 15
    • 12344251747 scopus 로고    scopus 로고
    • On the catalytic role of the conserved active site residue His466 of choline oxidase
    • Ghanem, M and Gadda, G. (2005) On the catalytic role of the conserved active site residue His466 of choline oxidase Biochemistry, 44, pp. 893-904.
    • (2005) Biochemistry , vol.44 , pp. 893-904
    • Ghanem, M.1    Gadda, G.2
  • 16
    • 29344449107 scopus 로고    scopus 로고
    • Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: Correlating reversible hydride transfer with environmentally enhanced tunneling
    • Fan, F and Gadda, G. (2005) Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: Correlating reversible hydride transfer with environmentally enhanced tunneling J Am Chem Soc, 127, pp. 17954-17961.
    • (2005) J Am Chem Soc , vol.127 , pp. 17954-17961
    • Fan, F.1    Gadda, G.2
  • 17
    • 0141976293 scopus 로고    scopus 로고
    • pH and deuterium kinetic isotope effects studies on the oxidation of choline to betaine-aldehyde catalyzed by choline oxidase
    • Gadda, G. (2003) pH and deuterium kinetic isotope effects studies on the oxidation of choline to betaine-aldehyde catalyzed by choline oxidase Biochim Biophys Acta, 1650, pp. 4-9.
    • (2003) Biochim Biophys Acta , vol.1650 , pp. 4-9
    • Gadda, G.1
  • 18
    • 33644868234 scopus 로고    scopus 로고
    • Effects of reversing the protein positive charge in the proximity of the flavin n(1) locus of choline oxidase
    • Ghanem, M and Gadda, G. (2006) Effects of reversing the protein positive charge in the proximity of the flavin n(1) locus of choline oxidase Biochemistry, 45, pp. 3437-3447.
    • (2006) Biochemistry , vol.45 , pp. 3437-3447
    • Ghanem, M.1    Gadda, G.2
  • 19
    • 4444281751 scopus 로고    scopus 로고
    • The trimethylammonium head group of choline is a major determinant for substrate binding and specificity in choline oxidase
    • Gadda, G and Powell, NL and Menon, P. (2004) The trimethylammonium head group of choline is a major determinant for substrate binding and specificity in choline oxidase Arch Biochem Biophys, 430, pp. 264-273.
    • (2004) Arch Biochem Biophys , vol.430 , pp. 264-273
    • Gadda, G.1    Powell, N.L.2    Menon, P.3
  • 20
    • 0142213903 scopus 로고    scopus 로고
    • Electrophilic reactivity of cationic triarylmethane dyes towards proteins and protein-related nucleophiles
    • Eldem, Y and Ozer, I. (2004) Electrophilic reactivity of cationic triarylmethane dyes towards proteins and protein-related nucleophiles Dyes Pigments, 60, pp. 49-54.
    • (2004) Dyes Pigments , vol.60 , pp. 49-54
    • Eldem, Y.1    Ozer, I.2
  • 21
    • 7744245736 scopus 로고    scopus 로고
    • Adduct-forming tendencies of cationic triarylmethane dyes with proteins: Metabolic and toxicological implications
    • Tacal, O and Ozer, I. (2004) Adduct-forming tendencies of cationic triarylmethane dyes with proteins: Metabolic and toxicological implications J Biochem Mol Toxicol, 18, pp. 253-256.
    • (2004) J Biochem Mol Toxicol , vol.18 , pp. 253-256
    • Tacal, O.1    Ozer, I.2
  • 22
    • 33845810402 scopus 로고    scopus 로고
    • Reactivity of meldola blue towards sulfhydryl groups: Analytical and biomedical aspects
    • Ozer, I. (2005) Reactivity of meldola blue towards sulfhydryl groups: Analytical and biomedical aspects Turk J Biochem, 30, pp. 220-224.
    • (2005) Turk J Biochem , vol.30 , pp. 220-224
    • Ozer, I.1
  • 23
    • 23744437423 scopus 로고    scopus 로고
    • Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: Mechanistic implications
    • Kucukkilinc, T and Ozer, I. (2005) Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: Mechanistic implications Arch Biochem Biophys, 440, pp. 118-122.
    • (2005) Arch Biochem Biophys , vol.440 , pp. 118-122
    • Kucukkilinc, T.1    Ozer, I.2
  • 24
    • 0344011673 scopus 로고    scopus 로고
    • Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases
    • Saxena, A and Fedorko, JM and Vinayaka, CR and Medhekar, R and Radic, Z and Taylor, P and Lockridge, O and Doctor, BP. (2003) Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases Eur J Biochem, 270, pp. 4447-4458.
    • (2003) Eur J Biochem , vol.270 , pp. 4447-4458
    • Saxena, A.1    Fedorko, J.M.2    Vinayaka, C.R.3    Medhekar, R.4    Radic, Z.5    Taylor, P.6    Lockridge, O.7    Doctor, B.P.8
  • 25
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radic, Z and Pickering, N.A. and Vellom, D.C. and Camp, S and Taylor, P. (1993) Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors Biochemistry, 32, pp. 12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 26
    • 0003518480 scopus 로고
    • In New York: Wiley-Interscience
    • Segel, IH.(1975) Enzyme Kinetics,. In (pp. 170-176). New York: Wiley-Interscience.
    • (1975) Enzyme Kinetics , pp. 170-176
    • Segel, I.H.1
  • 27
    • 0003518480 scopus 로고
    • In New York: Wiley-Interscience
    • Segel, IH.(1975) Enzyme Kinetics,. In (pp. 199-202). New York: Wiley-Interscience.
    • (1975) Enzyme Kinetics , pp. 199-202
    • Segel, I.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.