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Volumn 253, Issue 3, 1998, Pages 712-719

Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4- alkylphenols

Author keywords

Alkylphenol; Flavoprotein; Kinetic isotope effect; P quinone methide; Vanillyl alcohol oxidase

Indexed keywords

4 ETHYLPHENOL; 4 PROPYLPHENOL; OXIDOREDUCTASE; UNCLASSIFIED DRUG; VANILLYL ALCOHOL OXIDASE;

EID: 0032079529     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530712.x     Document Type: Article
Times cited : (36)

References (25)
  • 2
    • 0030999852 scopus 로고    scopus 로고
    • Enigmatic gratuitous induction of the covalent flavoprotein vanillyl-alcohol oxidase in Penicillium simplicissimum
    • Fraaije, M. W., Pikkemaat, M. & van Berkel, W. J. H. (1997) Enigmatic gratuitous induction of the covalent flavoprotein vanillyl-alcohol oxidase in Penicillium simplicissimum, Appl. Environ. Microbiol. 63, 435-439.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 435-439
    • Fraaije, M.W.1    Pikkemaat, M.2    Van Berkel, W.J.H.3
  • 3
    • 0026665175 scopus 로고
    • Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum
    • De Jong, E., van Berkel, W. J. H., van der Zwan, R. P. & De Bont, J. A. M. (1992) Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum, Eur. J. Biochem. 208, 651-657.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 651-657
    • De Jong, E.1    Van Berkel, W.J.H.2    Van Der Zwan, R.P.3    De Bont, J.A.M.4
  • 4
    • 0031016081 scopus 로고    scopus 로고
    • Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers
    • Fraaije, M. W., Mattevi, A. & van Berkel, W. J. H. (1997) Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers, FEBS Lett. 402, 33-35.
    • (1997) FEBS Lett. , vol.402 , pp. 33-35
    • Fraaije, M.W.1    Mattevi, A.2    Van Berkel, W.J.H.3
  • 5
    • 0028852139 scopus 로고
    • Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum
    • Fraaije, M. W., Veeger, C. & van Berkel, W. J. H. (1995) Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum, Eur. J. Biochem. 234, 271-277.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 271-277
    • Fraaije, M.W.1    Veeger, C.2    Van Berkel, W.J.H.3
  • 6
    • 0030739371 scopus 로고    scopus 로고
    • Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase
    • Fraaije, M. W. & van Berkel, W. J. H. (1997) Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase, J. Biol. Chem. 272, 18 111-18 116.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18111-18116
    • Fraaije, M.W.1    Van Berkel, W.J.H.2
  • 7
    • 0021666137 scopus 로고
    • Stereochemistry of 1-(4′-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase
    • McIntire, W. S., Hopper, D. J., Craig, J. C., Everhart, E. T., Webster, R. V., Causer, M. J. & Singer, T. P. (1984) Stereochemistry of 1-(4′-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase, Biochem. J. 224, 617-621.
    • (1984) Biochem. J. , vol.224 , pp. 617-621
    • McIntire, W.S.1    Hopper, D.J.2    Craig, J.C.3    Everhart, E.T.4    Webster, R.V.5    Causer, M.J.6    Singer, T.P.7
  • 8
    • 0021864826 scopus 로고
    • p-Cresol methylhydroxylase: Assay and general properties
    • McIntire, W. S., Hopper, D. J. & Singer, T. P. (1985) p-Cresol methylhydroxylase: assay and general properties, Biochem. J. 228, 325-335.
    • (1985) Biochem. J. , vol.228 , pp. 325-335
    • McIntire, W.S.1    Hopper, D.J.2    Singer, T.P.3
  • 9
    • 0031571090 scopus 로고    scopus 로고
    • Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: The shape of the active-site cavity controls substrate specificity
    • Mattevi, A., Fraaije, M. W., Mozzarelli, A., Olivi, L., Coda, A. & van Berkel, W. J. H. (1997) Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity, Structure 5, 907-920.
    • (1997) Structure , vol.5 , pp. 907-920
    • Mattevi, A.1    Fraaije, M.W.2    Mozzarelli, A.3    Olivi, L.4    Coda, A.5    Van Berkel, W.J.H.6
  • 10
    • 0026071385 scopus 로고
    • Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0 Å resolution
    • Mathews, F. S., Chen, Z.-W., Bellamy, H. D. & McIntire, W. S. (1991) Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0 Å resolution, Biochemistry 30, 238-247.
    • (1991) Biochemistry , vol.30 , pp. 238-247
    • Mathews, F.S.1    Chen, Z.-W.2    Bellamy, H.D.3    McIntire, W.S.4
  • 11
    • 0029562133 scopus 로고
    • The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase
    • Kim, J., Fuller, J. H., Kuusk, V., Cunane, L., Chen, Z., Mathews, F. S. & McIntire, W. S. (1995) The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase, J. Biol. Chem. 270, 31 202-31 209.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31202-31209
    • Kim, J.1    Fuller, J.H.2    Kuusk, V.3    Cunane, L.4    Chen, Z.5    Mathews, F.S.6    McIntire, W.S.7
  • 12
    • 2642708409 scopus 로고    scopus 로고
    • Molecular cloning, sequencing and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase
    • Benen, J. A. E., Sánchez-Torres, P., Wagemaker, M. J. M., Fraaije, M. W., van Berkel, W. J. H. & Visser, J. (1998) Molecular cloning, sequencing and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase, J. Biol. Chem. 273, 7865-7872.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7865-7872
    • Benen, J.A.E.1    Sánchez-Torres, P.2    Wagemaker, M.J.M.3    Fraaije, M.W.4    Van Berkel, W.J.H.5    Visser, J.6
  • 13
    • 2642662192 scopus 로고    scopus 로고
    • Vanillyl-alcohol oxidase from Penicillium simplicissimum: Reactivity with p-cresol and preliminary structural analysis
    • Stevenson, K., Massey, V. & Williams, C., eds University Press, Calgary
    • Fraaije, M. W., Drijfhout, F., Meulenbeld, G. H., van Berkel, W. J. H. & Mattevi, A. (1997) Vanillyl-alcohol oxidase from Penicillium simplicissimum: reactivity with p-cresol and preliminary structural analysis, in Flavins and flavoproteins XII (Stevenson, K., Massey, V. & Williams, C., eds) pp. 261-264, University Press, Calgary.
    • (1997) Flavins and Flavoproteins , vol.12 , pp. 261-264
    • Fraaije, M.W.1    Drijfhout, F.2    Meulenbeld, G.H.3    Van Berkel, W.J.H.4    Mattevi, A.5
  • 14
    • 78651157670 scopus 로고
    • Kinetics and mechanism of action of glucose oxidase
    • Gibson, Q. H., Swoboda, B. E. P. & Massey, V. (1964) Kinetics and mechanism of action of glucose oxidase, J. Biol. Chem. 239, 3927-3934.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3927-3934
    • Gibson, Q.H.1    Swoboda, B.E.P.2    Massey, V.3
  • 16
    • 0017227025 scopus 로고
    • The hydroxylation of p-cresol and its conversion to p-hydroxybenzaldehyde in Pseudomonas putida
    • Hopper, D. J. (1976) The hydroxylation of p-cresol and its conversion to p-hydroxybenzaldehyde in Pseudomonas putida, Biochem. Biophys. Res. Commun. 69, 462-468.
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 462-468
    • Hopper, D.J.1
  • 17
    • 0016749447 scopus 로고
    • Determination of dissociation constants and specific rate constants of enzyme-subsirate (or protein-ligand) interactions from rapid reaction kinetic data
    • Strickland, S., Palmer, G. & Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-subsirate (or protein-ligand) interactions from rapid reaction kinetic data, J. Biol. Chem. 250, 4048-4052.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4048-4052
    • Strickland, S.1    Palmer, G.2    Massey, V.3
  • 18
    • 0031054686 scopus 로고    scopus 로고
    • On the mechanism of D-amino acid oxidase
    • Pollegioni, L., Blodig, W. & Ghisla, S. (1997) On the mechanism of D-amino acid oxidase, J. Biol. Chem. 272, 4924-4934.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4924-4934
    • Pollegioni, L.1    Blodig, W.2    Ghisla, S.3
  • 19
    • 0028899066 scopus 로고
    • The influence of 4-alkyl substituents on the formation and reactivity of 2-methoxy-quinone methides: Evidence that the extended π-conjugation dramatically stabilizes the quinone methide formed from eugenol
    • Bolton, J. L., Comeau, E. & Vukomanovic, V. (1995) The influence of 4-alkyl substituents on the formation and reactivity of 2-methoxy-quinone methides: evidence that the extended π-conjugation dramatically stabilizes the quinone methide formed from eugenol, Chem. Biol. Interact. 95, 279-290.
    • (1995) Chem. Biol. Interact. , vol.95 , pp. 279-290
    • Bolton, J.L.1    Comeau, E.2    Vukomanovic, V.3
  • 20
    • 0030034847 scopus 로고    scopus 로고
    • Mechanism of isomerization of 4-O-propyl-quinone to its tautomeric p-quinone methide
    • Bolton, J. L., Wu, H. M. & Hu, L. Q. (1996) Mechanism of isomerization of 4-O-propyl-quinone to its tautomeric p-quinone methide, Chem. Res. Toxicol. 9, 109-113.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 109-113
    • Bolton, J.L.1    Wu, H.M.2    Hu, L.Q.3
  • 21
    • 0018787599 scopus 로고
    • Covalent adducts of lactate oxidase
    • Ghisla, S., Massey, V. & Choong, Y. S. (1979) Covalent adducts of lactate oxidase, J. Biol. Chem. 254, 10662-10669.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10662-10669
    • Ghisla, S.1    Massey, V.2    Choong, Y.S.3
  • 22
    • 0019332641 scopus 로고
    • Studies on the catalytic mechanism of lactate oxidase
    • Ghisla, S. & Massey, V. (1980) Studies on the catalytic mechanism of lactate oxidase, J. Biol. Chem. 255, 5688-5696.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5688-5696
    • Ghisla, S.1    Massey, V.2
  • 23
    • 0031054970 scopus 로고    scopus 로고
    • Identification of the naturally occurring flavin of nitroalkane oxidase from Fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form
    • Gadda, G., Edmondson, D. E., Russell, D. H. & Fitzpatrick, P. F. (1997) Identification of the naturally occurring flavin of nitroalkane oxidase from Fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form, J. Biol. Chem. 272, 5563-5570.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5563-5570
    • Gadda, G.1    Edmondson, D.E.2    Russell, D.H.3    Fitzpatrick, P.F.4
  • 24
    • 0023668302 scopus 로고
    • Steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect in the reaction catalyzed by p-cresol methylhydroxylase
    • McIntire, W. S., Hopper, D. S. & Singer, T. P. (1987) Steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect in the reaction catalyzed by p-cresol methylhydroxylase, Biochemistry 26, 4107-4117.
    • (1987) Biochemistry , vol.26 , pp. 4107-4117
    • McIntire, W.S.1    Hopper, D.S.2    Singer, T.P.3
  • 25
    • 0024430224 scopus 로고
    • The purification and characterization of 4-ethylphenol methylhydroxylase, a flavoprotein from Pseudomonas putida JD1
    • Reeve, C. D., Carver, M. A. & Hopper, D. J. (1989) The purification and characterization of 4-ethylphenol methylhydroxylase, a flavoprotein from Pseudomonas putida JD1, Biochem. J. 263, 431-437.
    • (1989) Biochem. J. , vol.263 , pp. 431-437
    • Reeve, C.D.1    Carver, M.A.2    Hopper, D.J.3


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