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Volumn 49, Issue 13, 2010, Pages 2952-2961

Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase

Author keywords

[No Author keywords available]

Indexed keywords

3D STRUCTURE; BIMOLECULAR RATE CONSTANTS; CHOLINE OXIDASE; COFACTORS; ELECTROSTATIC CATALYSIS; FLAVIN OXIDATION; HYDROPHOBIC CAVITIES; MONOOXYGENASES; NON-POLAR; RAPID REACTIONS; SIDE CHAINS; TIME-RESOLVED; VISUAL ANALYSIS; WILD-TYPE ENZYMES;

EID: 77950407407     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902048c     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins. J. Biol. Chem. 269, 22459-22462.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 2
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31, 276-283.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 3
    • 0000374069 scopus 로고
    • Simple synthesis of a 4a-hydroperoxy adduct of a 1,5-dihydroflavine: Preliminary studies of a model for bacterial luciferase
    • Kemal, C., and Bruice, T. C. (1976) Simple synthesis of a 4a-hydroperoxy adduct of a 1,5-dihydroflavine: preliminary studies of a model for bacterial luciferase. Proc. Natl. Acad. Sci. U.S.A. 73, 995-999.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 995-999
    • Kemal, C.1    Bruice, T.C.2
  • 4
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey, V. (2000) The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28, 283-296.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 5
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla, S., and Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181, 1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 6
    • 0025819901 scopus 로고
    • Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen
    • Wang, R., and Thorpe, C. (1991) Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen. Biochemistry 30, 7895-7901.
    • (1991) Biochemistry , vol.30 , pp. 7895-7901
    • Wang, R.1    Thorpe, C.2
  • 8
    • 0030035112 scopus 로고    scopus 로고
    • Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis
    • Sun, W., Williams, C. H., Jr., and Massey, V. (1996) Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis. J. Biol. Chem. 271, 17226-17233.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17226-17233
    • Sun, W.1    Williams Jr., C.H.2    Massey, V.3
  • 9
    • 63249113097 scopus 로고    scopus 로고
    • Identification of a gatekeeper residue that prevents dehydrogenases from acting as oxidases
    • Leferink, N. G., Fraaije, M. W., Joosten, H. J., Schaap, P. J., Mattevi, A., and van Berkel, W. J. (2009) Identification of a gatekeeper residue that prevents dehydrogenases from acting as oxidases. J. Biol. Chem. 284, 4392-4397.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4392-4397
    • Leferink, N.G.1    Fraaije, M.W.2    Joosten, H.J.3    Schaap, P.J.4    Mattevi, A.5    Van Berkel, W.J.6
  • 10
    • 34447638717 scopus 로고    scopus 로고
    • How do enzymes activate oxygen without inactivating themselves?
    • Klinman, J. P. (2007) How do enzymes activate oxygen without inactivating themselves? Acc. Chem. Res. 40, 325-333.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 325-333
    • Klinman, J.P.1
  • 12
    • 0037422546 scopus 로고    scopus 로고
    • Catalysis of electron transfer during activation of 02 by the flavoprotein glucose oxidase
    • Roth, J. P., and Klinman, J. P. (2003) Catalysis of electron transfer during activation of 02 by the flavoprotein glucose oxidase. Proc. Natl. Aad. Sci. 62-61.
    • (2003) Proc. Natl. Aad. Sci. , pp. 62-61
    • Roth, J.P.1    Klinman, J.P.2
  • 13
    • 0033614811 scopus 로고    scopus 로고
    • Nature of oxygen activation in glucose oxidase from aspergillus niger. the importance of electrostatic stabilization in superoxide formation
    • Su,Q.,andKlinman,J.P.(1999) NatureofoxygenactivationinglucoseoxidasefromAspergillusniger: theimportanceofelectrostaticstabilizationinsuperoxideformation.Biochemistry38, 8572-8581.(Pubitemid129515174)
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8572-8581
    • Su, Q.1    Klinman, J.P.2
  • 14
    • 50849101652 scopus 로고    scopus 로고
    • Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis
    • Zhao, G., Bruckner, R. C., and Jorns, M. S. (2008) Identification of the oxygen activation site in monomeric sarcosine oxidase: role of Lys265 in catalysis. Biochemistry 47, 9124-9135.
    • (2008) Biochemistry , vol.47 , pp. 9124-9135
    • Zhao, G.1    Bruckner, R.C.2    Jorns, M.S.3
  • 15
    • 33745713811 scopus 로고    scopus 로고
    • On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase
    • Gadda, G., Fan, F., and Hoang, J. V. (2006) On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase. Arch, Biochem. Biophys. 451, 182-187.
    • (2006) Arch, Biochem. Biophys. , vol.451 , pp. 182-187
    • Gadda, G.1    Fan, F.2    Hoang, J.V.3
  • 16
    • 4444281751 scopus 로고    scopus 로고
    • The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase
    • DOI 10.1016/j.abb.2004.07.011, PII S000398610400400X
    • Gadda, G., Powell, N. L., and Menon, P. (2004) The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Arch. Biochem. Biophys. 430, 264-273. (Pubitemid 39208973)
    • (2004) Archives of Biochemistry and Biophysics , vol.430 , Issue.2 , pp. 264-273
    • Gadda, G.1    Powell, N.L.N.2    Menon, P.3
  • 17
    • 43249129470 scopus 로고    scopus 로고
    • The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase
    • Chen, L., Lyubimov, A. Y., Brammer, L., Vrielink, A., and Sampson, N. S. (2008) The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase. Biochemistry 47, 5368-5377.
    • (2008) Biochemistry , vol.47 , pp. 5368-5377
    • Chen, L.1    Lyubimov, A.Y.2    Brammer, L.3    Vrielink, A.4    Sampson, N.S.5
  • 20
    • 33846244268 scopus 로고    scopus 로고
    • Trapping choline oxidase in a nonfunctional conformation by freezing at low pH
    • Hoang, J. V., and Gadda, G. (2007) Trapping choline oxidase in a nonfunctional conformation by freezing at low pH. Proteins 66, 611-620.
    • (2007) Proteins , vol.66 , pp. 611-620
    • Hoang, J.V.1    Gadda, G.2
  • 21
    • 33644868234 scopus 로고    scopus 로고
    • Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase
    • DOI 10.1021/bi052514m
    • 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, 3437-3447. (Pubitemid 43376363)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3437-3447
    • Ghanem, M.1    Gadda, G.2
  • 22
    • 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., 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. Bichem. Biophys. 421, 149-158.
    • (2004) Arch. Bichem. Biophys. , vol.421 , pp. 149-158
    • Fan, F.1    Ghanem, M.2    Gadda, G.3
  • 23
    • 0347594221 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis
    • Ghanem, M., Fan, F., Francis, K., and Gadda, G. (2003) Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis. Biochemistry 42, 15179-15188.
    • (2003) Biochemistry , vol.42 , pp. 15179-15188
    • Ghanem, M.1    Fan, F.2    Francis, K.3    Gadda, G.4
  • 24
    • 60749096264 scopus 로고    scopus 로고
    • Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase
    • Orville, A. M., Lountos, G. T., Finnegan, S., Gadda, G., and Prabhakar, R. (2009) Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase. Biochemistry 48, 720-728.
    • (2009) Biochemistry , vol.48 , pp. 720-728
    • Orville, A.M.1    Lountos, G.T.2    Finnegan, S.3    Gadda, G.4    Prabhakar, R.5
  • 25
    • 37849031214 scopus 로고    scopus 로고
    • Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase
    • Quaye, O., Lountos, G. T., Fan, F., Orville, A. M., and Gadda, G. (2008) Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase. Biochemistry 47, 243-256.
    • (2008) Biochemistry , vol.47 , pp. 243-256
    • Quaye, O.1    Lountos, G.T.2    Fan, F.3    Orville, A.M.4    Gadda, G.5
  • 26
    • 67650541861 scopus 로고    scopus 로고
    • Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
    • (in press).
    • Gadda, G., Quaye, O., Cowins, S. (2009) Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase, J. Biol. Chem. (in press).
    • (2009) J. Biol. Chem.
    • Gadda, G.1    Quaye, O.2    Cowins, S.3
  • 27
    • 46049114878 scopus 로고    scopus 로고
    • On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase
    • Rungsrisuriyachai, K., and Gadda, G. (2008) On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase. Biochemistry 47, 6767-6769.
    • (2008) Biochemistry , vol.47 , pp. 6767-6769
    • Rungsrisuriyachai, K.1    Gadda, G.2
  • 28
    • 58849110962 scopus 로고    scopus 로고
    • Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase
    • Finnegan, S., and Gadda, G. (2008) Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase. Biochemistry 47, 13850-13861.
    • (2008) Biochemistry , vol.47 , pp. 13850-13861
    • Finnegan, S.1    Gadda, G.2
  • 29
    • 34249676309 scopus 로고    scopus 로고
    • An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase
    • DOI 10.1021/bi700255v
    • Fan, F., and Gadda, G. (2007) An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase. Biochemistry 46, 6402-6408. (Pubitemid 46842883)
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6402-6408
    • Fan, F.1    Gadda, G.2
  • 30
    • 32444447830 scopus 로고    scopus 로고
    • Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde
    • DOI 10.1021/bi0517537
    • Fan, F., Germann, M. W., and Gadda, G. (2006) Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3, 3-dimethylbutyraldehyde. Biochemistry 45, 1979-1986. (Pubitemid 43224249)
    • (2006) Biochemistry , vol.45 , Issue.6 , pp. 1979-1986
    • Fan, F.1    Germann, M.W.2    Gadda, G.3
  • 31
    • 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, 17954-17961.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17954-17961
    • Fan, F.1    Gadda, G.2
  • 32
    • 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, 2067-2074.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2067-2074
    • Fan, F.1    Gadda, G.2
  • 33
    • 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. Biochem. Biophys. Acta 1650, 4-9.
    • (2003) Biochem. Biophys. Acta , vol.1650 , pp. 4-9
    • Gadda, G.1
  • 34
    • 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. Bionhvs. Acta 1646, 112-118.
    • (2003) Biochim. Bionhvs. Acta , vol.1646 , pp. 112-118
    • Gadda, G.1
  • 35
    • 69849104100 scopus 로고    scopus 로고
    • Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase
    • Quaye, O., and Gadda, G. (2009) Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase. Arch. Biochem. BiophYs. 489, 10-14.
    • (2009) Arch. Biochem. BiophYs. , vol.489 , pp. 10-14
    • Quaye, O.1    Gadda, G.2
  • 36
    • 58849100936 scopus 로고    scopus 로고
    • Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases
    • Gadda, G. (2008) Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases. Biochemistry 47, 13745-13753.
    • (2008) Biochemistry , vol.47 , pp. 13745-13753
    • Gadda, G.1
  • 37
    • 67650541861 scopus 로고    scopus 로고
    • Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
    • Quaye, O., Cowins, S., and Gadda, G. (2009) Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase. J. Biol. Chem. 284, 16990-16997.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16990-16997
    • Quaye, O.1    Cowins, S.2    Gadda, G.3
  • 38
    • 12344251747 scopus 로고    scopus 로고
    • 466 of choline oxidase
    • DOI 10.1021/bi048056j
    • Ghanem, M., and Gadda, G. (2005) On the catalytic role of the conserved active site residue His466 of choline oxidase. Biochemistry 44, 893-904. (Pubitemid 40129649)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 893-904
    • Ghanem, M.1    Gadda, G.2
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Minor, Z. O. A. W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzvmol. 276, 307-326.
    • (1997) Methods Enzvmol. , vol.276 , pp. 307-326
    • Minor, Z.O.A.W.1
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crvstalloer. A 47 (Part 2), 110-119.
    • (1991) Acta Crvstalloer. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 45
    • 0028057108 scopus 로고
    • Raster3D Version. 2.0. A program for photorealistic molecular graphics
    • Merritt, E. A., and Murphy, M. E. (1994) Raster3D Version. 2.0. A program for photorealistic molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallgr. 50, 869-873.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallgr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 46
    • 0018722049 scopus 로고
    • Practical considerations in the design of initial velocity enzyme rate assays
    • (Purich, D. L., Ed.) Academic Press, New York.
    • Allison, D. R., and Purich, D. L. (1979) Practical considerations in the design of initial velocity enzyme rate assays, in Methods in Enzymology (Purich, D. L., Ed.) pp 3-19, Academic Press, New York.
    • (1979) Methods in Enzymology , pp. 3-19
    • Allison, D.R.1    Purich, D.L.2
  • 47
    • 70449805655 scopus 로고    scopus 로고
    • Enzyme kinetics and mechanism
    • London and New York.
    • Cook, P. F., and Cleland, W. W. (2007) Enzyme kinetics and mechanism, Garland Science, London and New York.
    • (2007) Garland Science
    • Cook, P.F.1    Cleland, W.W.2
  • 48
    • 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, 2067-2074.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2067-2074
    • Fan, F.1    Gadda, G.2
  • 49
    • 0347594221 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis
    • Ghanem, M., Fan, F., Francis, K., and Gadda, G. (2003) Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis. Biochemistry 42, 15179-15188.
    • (2003) Biochemistry , vol.42 , pp. 15179-15188
    • Ghanem, M.1    Fan, F.2    Francis, K.3    Gadda, G.4
  • 50
    • 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, 112-118.
    • (2003) Biochim. Biophys., Acta , vol.1646 , pp. 112-118
    • Gadda, G.1
  • 51
    • 8744220371 scopus 로고    scopus 로고
    • Inverse thinking about double mutants of enzymes
    • Mildvan, A. S. (2004) Inverse thinking about double mutants of enzymes. Biochemistry 43, 14517-14520.
    • (2004) Biochemistry , vol.43 , pp. 14517-14520
    • Mildvan, A.S.1


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