메뉴 건너뛰기




Volumn 5, Issue 4, 2014, Pages 299-318

Alcohol oxidation by flavoenzymes

Author keywords

Alcohol oxidation; carbanion intermediate; FMN dependent l hydroxyacid dehydrogenase family; glucose methanol choline oxidoreductase superfamily; hydride transfer

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DERIVATIVE; ALDEHYDE; HYDROXYACID; RIBOFLAVIN DERIVATIVE; STEROL;

EID: 84922417266     PISSN: 18685021     EISSN: 1868503X     Source Type: Journal    
DOI: 10.1515/bmc-2014-0016     Document Type: Review
Times cited : (38)

References (132)
  • 1
    • 0013648788 scopus 로고
    • The mechanism of action of flavoprotein catalyzed reactions
    • Berlin: Springer Verlag, Sund H, Ullrich V, Editors
    • Massey V, Ghisla S. The mechanism of action of flavoprotein catalyzed reactions. In: Sund H, Ullrich V, editors. Biological oxidations. Berlin: Springer-Verlag, 1983: 114-39.
    • (1983) Biological Oxidations , pp. 114-139
    • Massey, V.1    Ghisla, S.2
  • 3
    • 0032498830 scopus 로고    scopus 로고
    • The PHBH fold: Not only flavoenzymes
    • Mattevi A. The PHBH fold: not only flavoenzymes. Biophys Chem 1998; 70: 217-22.
    • (1998) Biophys Chem , vol.70 , pp. 217-222
    • Mattevi, A.1
  • 4
    • 39749159159 scopus 로고    scopus 로고
    • Active site and loop 4 movements within human glycolate oxidase: Implications for substrate specificity and drug design
    • Murray MS, Holmes RP, Lowther WT. Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design. Biochemistry 2008; 47: 2439-49.
    • (2008) Biochemistry , vol.47 , pp. 2439-2449
    • Murray, M.S.1    Holmes, R.P.2    Lowther, W.T.3
  • 6
    • 0018540477 scopus 로고
    • Purification and properties of alcohol oxidase from Poria contigua
    • Bringer S, Sprey B, Sahm H. Purification and properties of alcohol oxidase from Poria contigua. Eur J Biochem 1979; 101: 563-70.
    • (1979) Eur J Biochem , vol.101 , pp. 563-570
    • Bringer, S.1    Sprey, B.2    Sahm, H.3
  • 7
    • 0033586720 scopus 로고    scopus 로고
    • Conformational transitions accompanying oligomerization of yeast alcohol oxidase, a peroxisomal flavoenzyme
    • Boteva R, Visser AJWG, Filippi B, Vriend G, Veenhuis M, van der Klei IJ. Conformational transitions accompanying oligomerization of yeast alcohol oxidase, a peroxisomal flavoenzyme. Biochemistry 1999; 38: 5034-44.
    • (1999) Biochemistry , vol.38 , pp. 5034-5044
    • Boteva, R.1    Visser, A.J.W.G.2    Filippi, B.3    Vriend, G.4    Veenhuis, M.5    Van Der Klei, I.J.6
  • 9
    • 61649105477 scopus 로고    scopus 로고
    • New oxidase from Bjerkandera arthroconidial anamorph that oxidizes both phenolic and nonphenolic benzyl alcohols
    • Romero E, Ferreira P, Martínez AT, Martínez MJ. New oxidase from Bjerkandera arthroconidial anamorph that oxidizes both phenolic and nonphenolic benzyl alcohols. Biochim Biophys Acta 2009; 1794: 689-97.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 689-697
    • Romero, E.1    Ferreira, P.2    Martínez, A.T.3    Martínez, M.J.4
  • 10
    • 23644451045 scopus 로고    scopus 로고
    • Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated alcohols
    • Ferreira P, Medina M, Guillén F, Martínez MJ, van Berkel WJH, Martínez AT. Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated alcohols. Biochem J 2005; 389: 731-8.
    • (2005) Biochem J , vol.389 , pp. 731-738
    • Ferreira, P.1    Medina, M.2    Guillén, F.3    Martínez, M.J.4    Van Berkel, W.J.H.5    Martínez, A.T.6
  • 11
    • 84892980610 scopus 로고    scopus 로고
    • Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. Strain MP688
    • Dijkman WP, Fraaije MW. Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. strain MP688. Appl Environ Microbiol 2014; 80: 1082-90.
    • (2014) Appl Environ Microbiol , vol.80 , pp. 1082-1090
    • Dijkman, W.P.1    Fraaije, M.W.2
  • 12
    • 84998217098 scopus 로고
    • Properties of choline oxidase of Cylindrocarpon didymum M-1
    • Yamada H, Mori N, Tani Y. Properties of choline oxidase of Cylindrocarpon didymum M-1. Agric Biol Chem 1979; 43 2173-7.
    • (1979) Agric Biol Chem , vol.43 , pp. 2173-2177
    • Yamada, H.1    Mori, N.2    Tani, Y.3
  • 14
    • 84961829267 scopus 로고    scopus 로고
    • Choline Oxidase and Related Systems
    • Hille R, Miller S, Palfey B, editors. Handbook of flavoproteins Berlin: De Gruyter
    • Gadda G. Choline oxidase and related systems. In: Hille R, Miller S, Palfey B, editors. Handbook of flavoproteins. Oxidases, dehydrogenases and related systems. Berlin: De Gruyter, 2012: 155-76.
    • (2012) Oxidases, Dehydrogenases and Related Systems , pp. 155-176
    • Gadda, G.1
  • 15
    • 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 GT, Fan F, Orville AM, Gadda G. Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase. Biochemistry 2008; 47: 243-56.
    • (2008) Biochemistry , vol.47 , pp. 243-256
    • Quaye, O.1    Lountos, G.T.2    Fan, F.3    Orville, A.M.4    Gadda, G.5
  • 17
    • 84882752665 scopus 로고    scopus 로고
    • Human choline dehydrogenase: Medical promises and biochemical challenges
    • Salvi F, Gadda G. Human choline dehydrogenase: medical promises and biochemical challenges. Arch Biochem Biophys 2013; 537: 243-52.
    • (2013) Arch Biochem Biophys , vol.537 , pp. 243-252
    • Salvi, F.1    Gadda, G.2
  • 19
    • 2342626462 scopus 로고    scopus 로고
    • The nitrogen-fixing symbiotic bacterium Mesorhizobium loti has and expresses the gene encoding pyridoxine 4-oxidase involved in the degradation of vitamin B6
    • Yuan B, Yoshikane Y, Yokochi N, Ohnishi K, Yagi T. The nitrogen-fixing symbiotic bacterium Mesorhizobium loti has and expresses the gene encoding pyridoxine 4-oxidase involved in the degradation of vitamin B6. FEMS Microbiol Lett 2004; 234: 225-30.
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 225-230
    • Yuan, B.1    Yoshikane, Y.2    Yokochi, N.3    Ohnishi, K.4    Yagi, T.5
  • 21
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg BM, Henriksson G, Pettersson G, Divne C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J Mol Biol 2002; 315: 421-34.
    • (2002) J Mol Biol , vol.315 , pp. 421-434
    • Hallberg, B.M.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 24
    • 73449127186 scopus 로고    scopus 로고
    • Amino acid substitution at the substrate-binding subsite alters the specificity of the Phanerochaete chrysosporium cellobiose dehydrogenase
    • Desriani, Ferri S, Sode K. Amino acid substitution at the substrate-binding subsite alters the specificity of the Phanerochaete chrysosporium cellobiose dehydrogenase. Biochem Biophys Res Commun 2010; 391 1246-50.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1246-1250
    • Desriani Ferri, S.1    Sode, K.2
  • 26
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • Phillips CM, Beeson WT, Cate JH, Marletta MA. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol 2011; 6: 1399-406.
    • (2011) ACS Chem Biol , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 27
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ. 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Cryst D 1999; 55: 969-77.
    • (1999) Acta Cryst D , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.J.6
  • 28
    • 13444310821 scopus 로고    scopus 로고
    • Glucose oxidase from Aspergillus niger: The mechanism of action with molecular oxygen, quinones, and one-electron acceptors
    • Leskovac V, Trivi S, Wohlfahrt G, Kandra J, Periin D. Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors. Int J Biochem Cell Biol 2005; 37: 731-50.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 731-750
    • Leskovac, V.1    Trivi, S.2    Wohlfahrt, G.3    Kandra, J.4    Periin, D.5
  • 30
    • 33745154878 scopus 로고    scopus 로고
    • New biotransformations of some reducing sugars to the corresponding (di)dehydro(glycosyl) aldoses or aldonic acids using fungal pyranose dehydrogenase
    • Sedmera P, Halada P, Kubátová E, Haltrich D, Prikrylová V, Volc J. New biotransformations of some reducing sugars to the corresponding (di)dehydro(glycosyl) aldoses or aldonic acids using fungal pyranose dehydrogenase. J Mol Catal B: Enzym 2006; 41: 32-42.
    • (2006) J Mol Catal B: Enzym , vol.41 , pp. 32-42
    • Sedmera, P.1    Halada, P.2    Kubátová, E.3    Haltrich, D.4    Prikrylová, V.5    Volc, J.6
  • 32
  • 33
    • 0006665893 scopus 로고
    • Glucose 2-oxidase (Coriolus versicolor) and its application to d-glucose colorimetry
    • Taguchi T, Ohwaki K, Okuda J. Glucose 2-oxidase (Coriolus versicolor) and its application to d-glucose colorimetry. J Appl Biochem 1985; 7: 289-95.
    • (1985) J Appl Biochem , vol.7 , pp. 289-295
    • Taguchi, T.1    Ohwaki, K.2    Okuda, J.3
  • 34
    • 0031742179 scopus 로고    scopus 로고
    • Rare keto-aldoses from enzymatic oxidation: Substrates and oxidation products of pyranose 2-oxidase
    • Freimund S, Huwig A, Giffhorn F, Köpper S. Rare keto-aldoses from enzymatic oxidation: substrates and oxidation products of pyranose 2-oxidase. Chem Eur J 1998; 4: 2442-55.
    • (1998) Chem Eur J , vol.4 , pp. 2442-2455
    • Freimund, S.1    Huwig, A.2    Giffhorn, F.3    Köpper, S.4
  • 36
    • 33644983893 scopus 로고    scopus 로고
    • Screening of yeasts producing stable l-lactate cytochrome c oxidoreductase and study of the regulation of enzyme synthesis
    • Smutok OV, Os'mak GS, Gaida GZ, Gonchar MV. Screening of yeasts producing stable l-lactate cytochrome c oxidoreductase and study of the regulation of enzyme synthesis. Microbiology 2006; 75: 20-4.
    • (2006) Microbiology , vol.75 , pp. 20-24
    • Smutok, O.V.1    Os'Mak, G.S.2    Gaida, G.Z.3    Gonchar, M.V.4
  • 37
    • 0032127767 scopus 로고    scopus 로고
    • Re-design of Saccharomyces cerevisiae flavocytochrome b2: Introduction of l-mandelate dehydrogenase activity
    • Sinclair R, Reid G, Chapman S. Re-design of Saccharomyces cerevisiae flavocytochrome b2: introduction of l-mandelate dehydrogenase activity. Biochem J 1998; 333: 117-20.
    • (1998) Biochem J , vol.333 , pp. 117-120
    • Sinclair, R.1    Reid, G.2    Chapman, S.3
  • 38
    • 0028109025 scopus 로고
    • Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2
    • Daff S, Manson FDC, Reid GA, Chapman SK. Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2. Biochem J 1994; 301: 829-34.
    • (1994) Biochem J , vol.301 , pp. 829-834
    • Daff, S.1    Manson, F.D.C.2    Reid, G.A.3    Chapman, S.K.4
  • 39
    • 0037006976 scopus 로고    scopus 로고
    • Crystallographic study of the recombinant flavin-binding domain of baker' s yeast flavocytochrome b2: Comparison with the intact wild-type enzyme
    • Cunane LM, Barton JD, Chen ZW, Welsh FE, Chapman SK, Reid GA, Mathews FS. Crystallographic study of the recombinant flavin-binding domain of baker's yeast flavocytochrome b2: comparison with the intact wild-type enzyme. Biochemistry 2002; 41: 4264-72.
    • (2002) Biochemistry , vol.41 , pp. 4264-4272
    • Cunane, L.M.1    Barton, J.D.2    Chen, Z.W.3    Welsh, F.E.4    Chapman, S.K.5    Reid, G.A.6    Mathews, F.S.7
  • 40
    • 36049016125 scopus 로고    scopus 로고
    • Flavocytochrome b2: Reactivity of its flavin with molecular oxygen
    • Boubacar AKO, Pethe S, Mahy J-P, Lederer F. Flavocytochrome b2: reactivity of its flavin with molecular oxygen. Biochemistry 2007; 46: 13080-8.
    • (2007) Biochemistry , vol.46 , pp. 13080-13088
    • Boubacar, A.K.O.1    Pethe, S.2    Mahy, J.-P.3    Lederer, F.4
  • 41
    • 3242733821 scopus 로고    scopus 로고
    • Altered substrate specificity in flavocytochrome b2: Structural insights into the mechanism of l-lactate dehydrogenation
    • Mowat CG, Wehenkel, A., Green, A. J., Walkinshaw, M. D., Reid, G. A., and Chapman, S. K. Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of l-lactate dehydrogenation. Biochemistry 2004; 43: 9519-26.
    • (2004) Biochemistry , vol.43 , pp. 9519-9526
    • Mowat, C.G.1    Wehenkel, A.2    Green, A.J.3    Walkinshaw, M.D.4    Reid, G.A.5    Chapman, S.K.6
  • 42
    • 0028954322 scopus 로고
    • Involvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase
    • Stenberg K, Clausen T, Lindqvist Y, Macheroux P. Involvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase. Eur J Biochem 1995; 228: 408-16.
    • (1995) Eur J Biochem , vol.228 , pp. 408-416
    • Stenberg, K.1    Clausen, T.2    Lindqvist, Y.3    MacHeroux, P.4
  • 43
    • 0029911191 scopus 로고    scopus 로고
    • Conversion of l-lactate oxidase to a long chain hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine
    • Yorita K, Aki K, Ohkuma-Soyejima T, Kokubo T, Misaki H, Massey V. Conversion of l-lactate oxidase to a long chain hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine. J Biol Chem 1996; 271: 28300-5.
    • (1996) J Biol Chem , vol.271 , pp. 28300-28305
    • Yorita, K.1    Aki, K.2    Ohkuma-Soyejima, T.3    Kokubo, T.4    Misaki, H.5    Massey, V.6
  • 44
    • 0030940522 scopus 로고    scopus 로고
    • Three-dimensional structures of glycolate oxidase with bound active-site inhibitors
    • Stenberg K, Lindqvist Y. Three-dimensional structures of glycolate oxidase with bound active-site inhibitors. Protein Sci 1997; 6: 1009-15.
    • (1997) Protein Sci , vol.6 , pp. 1009-1015
    • Stenberg, K.1    Lindqvist, Y.2
  • 45
    • 0016207266 scopus 로고
    • Identification and properties of new flavins in electron-transferring flavoprotein from Peptostreptococcus elsdenii and pig-liver glycolate oxidase
    • Mayhew SG, Whitfield CD, Ghisla S, Schuman-Jörns M. Identification and properties of new flavins in electron-transferring flavoprotein from Peptostreptococcus elsdenii and pig-liver glycolate oxidase. Eur J Biochem 1974; 44: 579-91.
    • (1974) Eur J Biochem , vol.44 , pp. 579-591
    • Mayhew, S.G.1    Whitfield, C.D.2    Ghisla, S.3    Schuman-Jörns, M.4
  • 46
    • 0034725053 scopus 로고    scopus 로고
    • Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases
    • Jones JM, Morrell JC, Gould SJ. Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem 2000; 275: 12590-7.
    • (2000) J Biol Chem , vol.275 , pp. 12590-12597
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 47
    • 0028078052 scopus 로고
    • The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex
    • Tegoni M, Cambillau C. The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex Protein Sci 1994; 3: 303-13.
    • (1994) Protein Sci , vol.3 , pp. 303-313
    • Tegoni, M.1    Cambillau, C.2
  • 50
    • 0034700157 scopus 로고    scopus 로고
    • Interaction of two arginine residues in lactate oxidase with the enzyme flavin: Conversion of FMN to 8-formyl-FMN
    • Yorita K, Matsuoka T, Misaki H, Massey V. Interaction of two arginine residues in lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN. Proc Natl Acad Sci USA 2000; 97: 13039-44.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13039-13044
    • Yorita, K.1    Matsuoka, T.2    Misaki, H.3    Massey, V.4
  • 51
    • 0034702818 scopus 로고    scopus 로고
    • Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization
    • Lehoux IE, Mitra B. Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization. Biochemistry 2000; 39: 10055-65.
    • (2000) Biochemistry , vol.39 , pp. 10055-10065
    • Lehoux, I.E.1    Mitra, B.2
  • 52
    • 0037108170 scopus 로고    scopus 로고
    • Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: Role in catalysis and substrate binding
    • Xu Y, Dewanti AR, Mitra B. Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and substrate binding. Biochemistry 2002; 41: 12313-9.
    • (2002) Biochemistry , vol.41 , pp. 12313-12319
    • Xu, Y.1    Dewanti, A.R.2    Mitra, B.3
  • 53
    • 0024462849 scopus 로고
    • Purification and properties of Aerococcus viridans lactate oxidase
    • Duncan JD, Wallis JO, Azari MR. Purification and properties of Aerococcus viridans lactate oxidase. Biochem Biophys Res Commun 1989; 164: 919-26.
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 919-926
    • Duncan, J.D.1    Wallis, J.O.2    Azari, M.R.3
  • 55
    • 0015524246 scopus 로고
    • Mechanism of action of the flavoenzyme lactate oxidase
    • Lockridge O, Massey V, Sullivan PA. Mechanism of action of the flavoenzyme lactate oxidase. J Biol Chem 1972; 247: 8097-106.
    • (1972) J Biol Chem , vol.247 , pp. 8097-8106
    • Lockridge, O.1    Massey, V.2    Sullivan, P.A.3
  • 56
    • 0017273344 scopus 로고
    • L-Hydroxyacid oxidase isozymes purification and molecular properties
    • Duley JA, Holmes RS. l-Hydroxyacid oxidase isozymes purification and molecular properties. Eur J Biochem 1976; 63: 163-73.
    • (1976) Eur J Biochem , vol.63 , pp. 163-173
    • Duley, J.A.1    Holmes, R.S.2
  • 58
    • 84862789275 scopus 로고    scopus 로고
    • High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl) sulfanyl]-1 2 3-thiadiazole. Implications for inhibitor specificity and drug design
    • Chen Z-W, Vignaud C, Jaafar A, Lévy B, Guéritte F, Guénard D, Lederer F, Mathews FS. High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl) sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design. Biochimie 2012; 94: 1172-9.
    • (2012) Biochimie , vol.94 , pp. 1172-1179
    • Chen, Z.-W.1    Vignaud, C.2    Jaafar, A.3    Lévy, B.4    Guéritte, F.5    Guénard, D.6    Lederer, F.7    Mathews, F.S.8
  • 59
    • 0033592410 scopus 로고    scopus 로고
    • A highly active, soluble mutant of the membraneassociated (S)-mandelate dehydrogenase from Pseudomonas putida
    • Xu Y, Mitra B. A highly active, soluble mutant of the membraneassociated (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry 1999; 38: 12367-76.
    • (1999) Biochemistry , vol.38 , pp. 12367-12376
    • Xu, Y.1    Mitra, B.2
  • 60
    • 0035928723 scopus 로고    scopus 로고
    • Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase
    • Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS. Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase. Biochemistry 2001; 40: 9870-8.
    • (2001) Biochemistry , vol.40 , pp. 9870-9878
    • Sukumar, N.1    Xu, Y.2    Gatti, D.L.3    Mitra, B.4    Mathews, F.S.5
  • 61
    • 0027751820 scopus 로고
    • A novel structural basis for membrane association of a protein: Construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida
    • Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA. A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry 1993; 32: 12959-67.
    • (1993) Biochemistry , vol.32 , pp. 12959-12967
    • Mitra, B.1    Gerlt, J.A.2    Babbitt, P.C.3    Koo, C.W.4    Kenyon, G.L.5    Joseph, D.6    Petsko, G.A.7
  • 62
    • 70449709431 scopus 로고    scopus 로고
    • Cholesterol oxidase: Biochemistry and structural features
    • Vrielink A, Ghisla S. Cholesterol oxidase: biochemistry and structural features. FEBS J 2009; 276: 6826-43.
    • (2009) FEBS J , vol.276 , pp. 6826-6843
    • Vrielink, A.1    Ghisla, S.2
  • 63
    • 0033528745 scopus 로고    scopus 로고
    • Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
    • Yue QK, Kass IJ, Sampson NS, Vrielink A. Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants. Biochemistry 1999; 38: 4277-86.
    • (1999) Biochemistry , vol.38 , pp. 4277-4286
    • Yue, Q.K.1    Kass, I.J.2    Sampson, N.S.3    Vrielink, A.4
  • 64
    • 0035839498 scopus 로고    scopus 로고
    • Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair
    • Coulombe R, Yue KQ, Ghisla S, Vrielink A. Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair. J Biol Chem 2001; 276: 30435-41.
    • (2001) J Biol Chem , vol.276 , pp. 30435-30441
    • Coulombe, R.1    Yue, K.Q.2    Ghisla, S.3    Vrielink, A.4
  • 65
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution
    • Vrielink A, Lloyd LF, Blow DM. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution. J Mol Biol 1991; 219: 533-54.
    • (1991) J Mol Biol , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 67
    • 79953280815 scopus 로고    scopus 로고
    • Initial step in the catabolism of cholesterol by Mycobacterium smegmatis mc2155
    • Uhiá I, Galán B, Morales V, Garciá JL. Initial step in the catabolism of cholesterol by Mycobacterium smegmatis mc2155. Environ Microbiol 2011; 13: 943-59.
    • (2011) Environ Microbiol , vol.13 , pp. 943-959
    • Uhiá, I.1    Galán, B.2    Morales, V.3    Garciá, J.L.4
  • 68
    • 0031027536 scopus 로고    scopus 로고
    • Isomerization, but not oxidation, is suppressed by a single point mutation, E361Q, in the reaction catalyzed by cholesterol oxidase
    • Sampson NS, Kass IJ. Isomerization, but not oxidation, is suppressed by a single point mutation, E361Q, in the reaction catalyzed by cholesterol oxidase. J Am Chem Soc 1997; 119: 855-62.
    • (1997) J Am Chem Soc , vol.119 , pp. 855-862
    • Sampson, N.S.1    Kass, I.J.2
  • 69
    • 10044289888 scopus 로고
    • The reversible hydration of carbonyl compounds
    • Bell RP. The reversible hydration of carbonyl compounds. Adv Phys Org Chem 1966; 4: 1-29.
    • (1966) Adv Phys Org Chem , vol.4 , pp. 1-29
    • Bell, R.P.1
  • 70
    • 0017121464 scopus 로고
    • Alcohol oxidases of Kloeckera sp. and Hansenula polymorpha
    • Kato N, Omori Y, Tani Y, Ogata K. Alcohol oxidases of Kloeckera sp. and Hansenula polymorpha. Eur J Biochem 1976; 64: 341-50.
    • (1976) Eur J Biochem , vol.64 , pp. 341-350
    • Kato, N.1    Omori, Y.2    Tani, Y.3    Ogata, K.4
  • 71
    • 0037391235 scopus 로고    scopus 로고
    • Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata
    • Gadda G, McAllister-Wilkins EE. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl Environ Microbiol 2003; 69: 2126-32.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2126-2132
    • Gadda, G.1    McAllister-Wilkins, E.E.2
  • 72
    • 0018900263 scopus 로고
    • Studies on the reaction mechanism of lactate oxidase. Formation of two covalent flavinsubstrate adducts on reaction with glycollate
    • Massey V, Ghisla S, Kieschkeg K. Studies on the reaction mechanism of lactate oxidase. Formation of two covalent flavinsubstrate adducts on reaction with glycollate. J Biol Chem 1980; 255: 2796-806.
    • (1980) J Biol Chem , vol.255 , pp. 2796-2806
    • Massey, V.1    Ghisla, S.2    Kieschkeg, K.3
  • 73
    • 0019892217 scopus 로고
    • Thiol-glyoxylate adducts as substrates for rat kidney l-hydroxy acid oxidase
    • Brush EJ, Hamilton GA. Thiol-glyoxylate adducts as substrates for rat kidney l-hydroxy acid oxidase. Biochem Biophys Res Commun 1981; 103: 1194-200.
    • (1981) Biochem Biophys Res Commun , vol.103 , pp. 1194-1200
    • Brush, E.J.1    Hamilton, G.A.2
  • 74
    • 84902284072 scopus 로고    scopus 로고
    • Enzyme-catalyzed oxidation of 5-hydroxymethylfurfural to furan-2, 5-dicarboxylic acid
    • Dijkman WP, Groothuis DE, Fraaije MW. Enzyme-catalyzed oxidation of 5-hydroxymethylfurfural to furan-2, 5-dicarboxylic acid. Angew Chem Int Ed 2014; 53: 6515-8.
    • (2014) Angew Chem Int Ed , vol.53 , pp. 6515-6518
    • Dijkman, W.P.1    Groothuis, D.E.2    Fraaije, M.W.3
  • 76
    • 0022426161 scopus 로고
    • Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase
    • Gómez-Moreno C, Edmondson DE. Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase. Arch Biochem Biophys 1985; 239: 46-52.
    • (1985) Arch Biochem Biophys , vol.239 , pp. 46-52
    • Gómez-Moreno, C.1    Edmondson, D.E.2
  • 77
    • 0030707706 scopus 로고    scopus 로고
    • Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum
    • Koga S, Ogawa J, Cheng L, Choi Y, Yamada H, Shimizu S. Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum. Appl Environ Microbiol 1997; 63: 4282-6.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4282-4286
    • Koga, S.1    Ogawa, J.2    Cheng, L.3    Choi, Y.4    Yamada, H.5    Shimizu, S.6
  • 78
    • 0042622631 scopus 로고    scopus 로고
    • Kinetic mechanism of choline oxidase from Arthrobacter globiformis
    • Gadda G. Kinetic mechanism of choline oxidase from Arthrobacter globiformis. Biochim Biophys Acta 2003; 1646: 112-8.
    • (2003) Biochim Biophys Acta , vol.1646 , pp. 112-118
    • Gadda, G.1
  • 79
    • 32444447830 scopus 로고    scopus 로고
    • Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3, 3-dimethylbutyraldehyde
    • Fan F, Germann MW, Gadda G. Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3, 3-dimethylbutyraldehyde. Biochemistry 2006; 45: 1979-86.
    • (2006) Biochemistry , vol.45 , pp. 1979-1986
    • Fan, F.1    Germann, M.W.2    Gadda, G.3
  • 81
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla S, Massey V. Mechanisms of flavoprotein-catalyzed reactions. Eur J Biochem 1989; 181: 1-17.
    • (1989) Eur J Biochem , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 82
    • 84901486385 scopus 로고
    • Glossary of terms used in physical organic chemistry
    • Muller P. Glossary of terms used in physical organic chemistry. Pure Appl Chem 1994; 66: 1077-184.
    • (1994) Pure Appl Chem , vol.66 , pp. 1077-1184
    • Muller, P.1
  • 83
    • 12344271332 scopus 로고    scopus 로고
    • On the catalytic mechanism of choline oxidase
    • Fan F, Gadda G. On the catalytic mechanism of choline oxidase. J Am Chem Soc 2005; 127: 2067-74.
    • (2005) J Am Chem Soc , vol.127 , pp. 2067-2074
    • Fan, F.1    Gadda, G.2
  • 85
    • 77951683048 scopus 로고    scopus 로고
    • Kinetic isotope effects on the noncovalent flavin mutant protein of pyranose 2-oxidase reveal insights into the flavin reduction mechanism
    • Sucharitakul J, Wongnate T, Chaiyen P. Kinetic isotope effects on the noncovalent flavin mutant protein of pyranose 2-oxidase reveal insights into the flavin reduction mechanism. Biochemistry 2010; 49: 3753-65.
    • (2010) Biochemistry , vol.49 , pp. 3753-3765
    • Sucharitakul, J.1    Wongnate, T.2    Chaiyen, P.3
  • 86
    • 0014197974 scopus 로고
    • The oxidation of 1-deuterated glucose by glucose oxidase
    • Bright HJ, Gibson QH. The oxidation of 1-deuterated glucose by glucose oxidase. J Biol Chem 1967; 242: 994-1003.
    • (1967) J Biol Chem , vol.242 , pp. 994-1003
    • Bright, H.J.1    Gibson, Q.H.2
  • 87
    • 0032558937 scopus 로고    scopus 로고
    • Evaluation of the role of His447 in the reaction catalyzed by cholesterol oxidase
    • Kass IJ, Sampson NS. Evaluation of the role of His447 in the reaction catalyzed by cholesterol oxidase. Biochemistry 1998; 37: 17990-8000.
    • (1998) Biochemistry , vol.37 , pp. 17990-18000
    • Kass, I.J.1    Sampson, N.S.2
  • 88
    • 0032491078 scopus 로고    scopus 로고
    • The importance of Glu361 position in the reaction catalyzed by cholesterol oxidase
    • Kass IJ, Sampson NS. The importance of Glu361 position in the reaction catalyzed by cholesterol oxidase. Bioorg Med Chem Lett 1998; 8: 2663-8.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 2663-2668
    • Kass, I.J.1    Sampson, N.S.2
  • 89
    • 70049087992 scopus 로고    scopus 로고
    • Aryl-alcohol oxidase involved in lignin degradation. A mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates
    • Ferreira P, Hernández-Ortega A, Herguedas B, Martínez AT, Medina M. Aryl-alcohol oxidase involved in lignin degradation. A mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates. J Biol Chem 2009; 284: 24840-7.
    • (2009) J Biol Chem , vol.284 , pp. 24840-24847
    • Ferreira, P.1    Hernández-Ortega, A.2    Herguedas, B.3    Martínez, A.T.4    Medina, M.5
  • 90
    • 79956001462 scopus 로고    scopus 로고
    • V. G. Substrate diffusion and oxidation in GMC oxidoreductases: An experimental and computational study on fungal aryl-alcohol oxidase
    • Hernández-Ortega A, Borrelli K, Ferreira P, Medina M, Martínez AT, V. G. Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase. Biochem J 2011; 436: 341-50.
    • (2011) Biochem J , vol.436 , pp. 341-350
    • Hernández-Ortega, A.1    Borrelli, K.2    Ferreira, P.3    Medina, M.4    Martínez, A.T.5
  • 91
    • 0028935332 scopus 로고
    • Substituted alcohols as mechanistic probes of alcohol oxidase
    • Menon V, Hsieh CT, Fitzpatrick PF. Substituted alcohols as mechanistic probes of alcohol oxidase. Bioorg Chem 1995; 23: 42-53.
    • (1995) Bioorg Chem , vol.23 , pp. 42-53
    • Menon, V.1    Hsieh, C.T.2    Fitzpatrick, P.F.3
  • 92
    • 0346963173 scopus 로고    scopus 로고
    • Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism
    • Sobrado P, Fitzpatrick PF. Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism. Biochemistry 2003; 42: 15208-14.
    • (2003) Biochemistry , vol.42 , pp. 15208-15214
    • Sobrado, P.1    Fitzpatrick, P.F.2
  • 93
    • 63049126082 scopus 로고    scopus 로고
    • Fois E. L-Lactate dehydrogenation in flavocytochrome b2: A first principles molecular dynamics study
    • Tabacchi G, Zucchini D, Caprini G, Gamba A, Lederer F, Vanoni MA, Fois E. l-Lactate dehydrogenation in flavocytochrome b2: a first principles molecular dynamics study. FEBS J 2009; 276: 2368-80.
    • (2009) FEBS J , vol.276 , pp. 2368-2380
    • Tabacchi, G.1    Zucchini, D.2    Caprini, G.3    Gamba, A.4    Lederer, F.5    Vanoni, M.A.6
  • 94
    • 0242424115 scopus 로고    scopus 로고
    • A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
    • Dewanti AR, Mitra B. A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry 2003; 42: 12893-901.
    • (2003) Biochemistry , vol.42 , pp. 12893-12901
    • Dewanti, A.R.1    Mitra, B.2
  • 95
    • 0015803181 scopus 로고
    • Studies on the mechanism of action of the flavoenzyme lactate oxidase. Oxidation and elimination with chlorolactate
    • Walsh C, Lockridge O, Massey V, Abeles R. Studies on the mechanism of action of the flavoenzyme lactate oxidase. Oxidation and elimination with chlorolactate. J Biol Chem 1973; 248.
    • (1973) J Biol Chem , vol.248
    • Walsh, C.1    Lockridge, O.2    Massey, V.3    Abeles, R.4
  • 96
    • 0023752684 scopus 로고
    • Rat kidney l-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker' s yeast
    • Urban P, Chirat I, Lederer F. Rat kidney l-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast. Biochemistry 1988; 27: 7365-71.
    • (1988) Biochemistry , vol.27 , pp. 7365-7371
    • Urban, P.1    Chirat, I.2    Lederer, F.3
  • 97
    • 81755172448 scopus 로고    scopus 로고
    • Revisitation of the ?Clelimination reaction of d-amino acid oxidase. New interpretation of the reaction that sparked flavoprotein dehydrogenation mechanisms
    • Ghisla S, Pollegioni L, Molla G. Revisitation of the ?Clelimination reaction of d-amino acid oxidase. New interpretation of the reaction that sparked flavoprotein dehydrogenation mechanisms. J Biol Chem 2011; 286: 40987-98.
    • (2011) J Biol Chem , vol.286 , pp. 40987-40998
    • Ghisla, S.1    Pollegioni, L.2    Molla, G.3
  • 98
    • 1942485882 scopus 로고    scopus 로고
    • Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations
    • Fitzpatrick PF. Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations. Bioorg Chem 2004; 32: 125-39.
    • (2004) Bioorg Chem , vol.32 , pp. 125-139
    • Fitzpatrick, P.F.1
  • 99
    • 84901336098 scopus 로고    scopus 로고
    • MD and QM/MM studies on long chain l-hydroxy acid oxidase: Substrate binding features and oxidation mechanism
    • Cao Y, Han S, Yu L, Qian H, Chen JZ. MD and QM/MM studies on long chain l-hydroxy acid oxidase: substrate binding features and oxidation mechanism. J Phys Chem B 2014; 118: 5406-17.
    • (2014) J Phys Chem B , vol.118 , pp. 5406-5417
    • Cao, Y.1    Han, S.2    Yu, L.3    Qian, H.4    Chen, J.Z.5
  • 100
    • 84990162459 scopus 로고
    • The cyclopropyl group in studies of enzyme mechanism and inhibition
    • Suckling CJ. The cyclopropyl group in studies of enzyme mechanism and inhibition. Angew Chem Int Ed Engl 1988; 27: 537-52.
    • (1988) Angew Chem Int Ed Engl , vol.27 , pp. 537-552
    • Suckling, C.J.1
  • 101
    • 0022429988 scopus 로고
    • Mechanism of action of methanol oxidase, reconstitution of methanol oxidase with 5-deazaflavin, and inactivation of methanol oxidase by cyclopropanol
    • Sherry B, Abeles RH. Mechanism of action of methanol oxidase, reconstitution of methanol oxidase with 5-deazaflavin, and inactivation of methanol oxidase by cyclopropanol. Biochemistry 1985; 24: 2594-605.
    • (1985) Biochemistry , vol.24 , pp. 2594-2605
    • Sherry, B.1    Abeles, R.H.2
  • 102
    • 0017186397 scopus 로고
    • Nicotinamide-dependent one-electron and two-electron (flavin) oxidoreduction: Thermodynamics, kinetics, and mechanism
    • Blankenhorn G. Nicotinamide-dependent one-electron and two-electron (flavin) oxidoreduction: thermodynamics, kinetics, and mechanism. Eur J Biochem 1976; 67: 67-80.
    • (1976) Eur J Biochem , vol.67 , pp. 67-80
    • Blankenhorn, G.1
  • 103
    • 0034639465 scopus 로고    scopus 로고
    • A C6-flavin adduct is the major product of irreversible inactivation of cholesterol oxidase by 2?, 3cyclopropano-5cholestan-3ol
    • McCann AE, Sampson NS. A C6-flavin adduct is the major product of irreversible inactivation of cholesterol oxidase by 2?, 3cyclopropano-5cholestan-3ol. J Am Chem Soc 2000; 122: 35-9.
    • (2000) J Am Chem Soc , vol.122 , pp. 35-39
    • McCann, A.E.1    Sampson, N.S.2
  • 104
    • 0019332641 scopus 로고
    • Studies on the catalytic mechanism of lactate oxidase. Formation of enantiomeric flavin-N(5)-glycollyl adducts through carbanion intermediates
    • Ghisla S, Massey V. Studies on the catalytic mechanism of lactate oxidase. Formation of enantiomeric flavin-N(5)-glycollyl adducts through carbanion intermediates. J Biol Chem 1980; 255: 5688-96.
    • (1980) J Biol Chem , vol.255 , pp. 5688-5696
    • Ghisla, S.1    Massey, V.2
  • 105
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen A, Cannio R, Bartolucci S, Klinman JP. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature 1999; 399: 496-9.
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 106
    • 0037046991 scopus 로고    scopus 로고
    • Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: The relationship of modification of the protein envelope to C-H activation and tunneling
    • Seymour SL, Klinman JP. Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling. Biochemistry 2002; 41: 8747-58.
    • (2002) Biochemistry , vol.41 , pp. 8747-8758
    • Seymour, S.L.1    Klinman, J.P.2
  • 107
    • 62249181529 scopus 로고    scopus 로고
    • An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling
    • Klinman JP. An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling. Chem Phys Lett 2009; 471: 179-93.
    • (2009) Chem Phys Lett , vol.471 , pp. 179-193
    • Klinman, J.P.1
  • 108
    • 34249676309 scopus 로고    scopus 로고
    • An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase
    • Fan F, Gadda G. An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase. Biochemistry 2007; 46: 6402-8.
    • (2007) Biochemistry , vol.46 , pp. 6402-6408
    • Fan, F.1    Gadda, G.2
  • 109
    • 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
    • Osbourne Q, Gadda G. 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 2009; 489: 10-4.
    • (2009) Arch Biochem Biophys , vol.489 , pp. 10-14
    • Osbourne, Q.1    Gadda, G.2
  • 110
    • 67650541861 scopus 로고    scopus 로고
    • Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
    • Osbourne Q, Cowins S, Gadda G. Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase. J Biol Chem 2009; 284: 16990-7.
    • (2009) J Biol Chem , vol.284 , pp. 16990-16997
    • Osbourne, Q.1    Cowins, S.2    Gadda, G.3
  • 112
    • 84865435786 scopus 로고    scopus 로고
    • The enigmatic reaction of flavins with oxygen
    • Chaiyen P, Fraaije MW, Mattevi A. The enigmatic reaction of flavins with oxygen. TIBS 2012; 37: 373-80.
    • (2012) TIBS , vol.37 , pp. 373-380
    • Chaiyen, P.1    Fraaije, M.W.2    Mattevi, A.3
  • 113
    • 84859376000 scopus 로고    scopus 로고
    • Oxygen activation in flavoprotein oxidases: The importance of being positive
    • Gadda G. Oxygen activation in flavoprotein oxidases: the importance of being positive. Biochemistry 2012; 51: 2662-9.
    • (2012) Biochemistry , vol.51 , pp. 2662-2669
    • Gadda, G.1
  • 114
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey V. Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 1994; 269: 22459-62.
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 115
    • 78650858458 scopus 로고    scopus 로고
    • Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase
    • Pennati A, Gadda G. Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase. Biochemistry 2010; 50: 1-3.
    • (2010) Biochemistry , vol.50 , pp. 1-3
    • Pennati, A.1    Gadda, G.2
  • 116
    • 84892170130 scopus 로고    scopus 로고
    • Proton-coupled electron transfer and adduct configuration are important for C4ahydroperoxyflavin formation and stabilization in a flavoenzyme
    • Wongnate T, Surawatanawong P, Visitsatthawong S, Sucharitakul J, Scrutton NS, Chaiyen P. Proton-coupled electron transfer and adduct configuration are important for C4ahydroperoxyflavin formation and stabilization in a flavoenzyme. J Am Chem Soc 2013; 136: 241-53.
    • (2013) J Am Chem Soc , vol.136 , pp. 241-253
    • Wongnate, T.1    Surawatanawong, P.2    Visitsatthawong, S.3    Sucharitakul, J.4    Scrutton, N.S.5    Chaiyen, P.6
  • 117
    • 84874032081 scopus 로고    scopus 로고
    • Relative timing of hydrogen and proton transfers in the reaction of flavin oxidation catalyzed by choline oxidase
    • Gannavaram S, Gadda G. Relative timing of hydrogen and proton transfers in the reaction of flavin oxidation catalyzed by choline oxidase. Biochemistry 2013; 52: 1221-6.
    • (2013) Biochemistry , vol.52 , pp. 1221-1226
    • Gannavaram, S.1    Gadda, G.2
  • 119
    • 84865428476 scopus 로고    scopus 로고
    • Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle
    • Hernández-Ortega A, Lucas F, Ferreira P, Medina M, Guallar V, Martínez AT. Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle. Biochemistry 2012; 51: 6595-608.
    • (2012) Biochemistry , vol.51 , pp. 6595-6608
    • Hernández-Ortega, A.1    Lucas, F.2    Ferreira, P.3    Medina, M.4    Guallar, V.5    Martínez, A.T.6
  • 120
    • 12344251747 scopus 로고    scopus 로고
    • On the catalytic role of the conserved active site residue His466 of choline oxidase
    • Ghanem M, Gadda G. On the catalytic role of the conserved active site residue His466 of choline oxidase. Biochemistry 2005; 44: 893-904.
    • (2005) Biochemistry , vol.44 , pp. 893-904
    • Ghanem, M.1    Gadda, G.2
  • 121
    • 0347594221 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis
    • Ghanem M, Fan F, Francis K, Gadda G. Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis. Biochemistry 2003; 42: 15179-88.
    • (2003) Biochemistry , vol.42 , pp. 15179-15188
    • Ghanem, M.1    Fan, F.2    Francis, K.3    Gadda, G.4
  • 122
    • 81555196346 scopus 로고    scopus 로고
    • Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction
    • Wongnate T, Sucharitakul J, Chaiyen P. Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction. ChemBioChem 2011; 12: 2577-86.
    • (2011) ChemBioChem , vol.12 , pp. 2577-2586
    • Wongnate, T.1    Sucharitakul, J.2    Chaiyen, P.3
  • 123
    • 0037422546 scopus 로고    scopus 로고
    • Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase
    • Roth JP, Klinman JP. Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase. Proc Natl Acad Sci USA 2003; 100: 62-7.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 62-67
    • Roth, J.P.1    Klinman, J.P.2
  • 124
    • 33646457379 scopus 로고    scopus 로고
    • Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment
    • Lyubimov AY, Lario PI, Moustafa I, Vrielink A. Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment. Nat Chem Biol 2006; 2: 259-64.
    • (2006) Nat Chem Biol , vol.2 , pp. 259-264
    • Lyubimov, A.Y.1    Lario, P.I.2    Moustafa, I.3    Vrielink, A.4
  • 125
    • 0037446732 scopus 로고    scopus 로고
    • Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Rotsaert FA, Renganathan V, Gold MH. Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium. Biochemistry 2003; 42: 4049-56.
    • (2003) Biochemistry , vol.42 , pp. 4049-4056
    • Rotsaert, F.A.1    Renganathan, V.2    Gold, M.H.3
  • 126
    • 84878503057 scopus 로고    scopus 로고
    • Molecular dynamics simulations give insight into d-glucose dioxidation at C2 and C3 by Agaricus meleagris pyranose dehydrogenase
    • Graf MMH, Bren U, Haltrich D, Oostenbrink C. Molecular dynamics simulations give insight into d-glucose dioxidation at C2 and C3 by Agaricus meleagris pyranose dehydrogenase. J Comput Aided Mol Des 2013; 27: 295-304.
    • (2013) J Comput Aided Mol des , vol.27 , pp. 295-304
    • Graf, M.M.H.1    Bren, U.2    Haltrich, D.3    Oostenbrink, C.4
  • 127
    • 0028363964 scopus 로고
    • Lactate Monooxygenase. Site-directed mutagenesis of the postulated active site base histidine 290
    • Müh U, Williams CH, Massey V. Lactate Monooxygenase. Site-directed mutagenesis of the postulated active site base histidine 290. J Biol Chem 1994; 269: 7989-93.
    • (1994) J Biol Chem , vol.269 , pp. 7989-7993
    • Müh, U.1    Williams, C.H.2    Massey, V.3
  • 128
    • 34347334604 scopus 로고    scopus 로고
    • Mechanistic and structural studies of H373Q flavocytochrome b2: Effects of mutating the active site base
    • Tsai CL, Gokulan K, Sobrado P, Sacchettini JC, Fitzpatrick PF. Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base. Biochemistry 2007; 46: 7844-51.
    • (2007) Biochemistry , vol.46 , pp. 7844-7851
    • Tsai, C.L.1    Gokulan, K.2    Sobrado, P.3    Sacchettini, J.C.4    Fitzpatrick, P.F.5
  • 129
    • 0033520066 scopus 로고    scopus 로고
    • S-Mandelate dehydrogenase from Pseudomonas putida: Mutations of the catalytic base histidine-274 and chemical rescue of activity
    • Lehoux IE, Mitra B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity. Biochemistry 1999; 38: 9948-55.
    • (1999) Biochemistry , vol.38 , pp. 9948-9955
    • Lehoux, I.E.1    Mitra, B.2
  • 130
    • 71449113304 scopus 로고    scopus 로고
    • Involvement of ionizable groups in catalysis of human liver glycolate oxidase
    • Pennati A, Gadda G. Involvement of ionizable groups in catalysis of human liver glycolate oxidase J Biol Chem 2009; 284: 31214-22.
    • (2009) J Biol Chem , vol.284 , pp. 31214-31222
    • Pennati, A.1    Gadda, G.2
  • 131
    • 4344582358 scopus 로고    scopus 로고
    • Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase
    • Hallberg BM, Leitner C, Haltrich D, Divne C. Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase. J Mol Biol 2004; 341: 781-96.
    • (2004) J Mol Biol , vol.341 , pp. 781-796
    • Hallberg, B.M.1    Leitner, C.2    Haltrich, D.3    Divne, C.4
  • 132
    • 0025259157 scopus 로고
    • Massey V. L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family
    • Giegel DA, Williams CH, Massey V. l-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family. J Biol Chem 1990; 265: 6626-32.
    • (1990) J Biol Chem , vol.265 , pp. 6626-6632
    • Giegel, D.A.1    Ch, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.