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Volumn 180, Issue 21, 1998, Pages 5646-5651

Regio- and stereospecific conversion of 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL OXIDASE; ALKYLPHENOL; VANILLIN;

EID: 0031740420     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.21.5646-5651.1998     Document Type: Article
Times cited : (43)

References (16)
  • 1
    • 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., P. Sénchez-Torres, M. Wagemaker, M. W. Fraaije, W. J. H. van Berkel, and J. Visser. 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    Sénchez-Torres, P.2    Wagemaker, M.3    Fraaije, M.W.4    Van Berkel, W.J.H.5    Visser, J.6
  • 2
    • 0026665175 scopus 로고
    • Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum: A novel aromatic alcohol oxidase containing covalently bound FAD
    • De Jong, E., W. J. H. van Berkel, R. P. van der Zwan, and J. A. M. de Bont. 1992. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum: a novel aromatic alcohol oxidase containing covalently bound FAD. 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
    • 0040077039 scopus 로고
    • Studies on glycolate oxidase from pea leaves: Determination of stereospecificity and mode of inhibition by α-hydroxybutynoate
    • Fendrich, G., and S. Ghisla. 1982. Studies on glycolate oxidase from pea leaves: determination of stereospecificity and mode of inhibition by α-hydroxybutynoate. Biochim. Biophys. Acta 702:242-248.
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 242-248
    • Fendrich, G.1    Ghisla, S.2
  • 5
    • 0028852139 scopus 로고
    • Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum: Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols
    • Fraaije, M. W., C. Veeger, and W. J. H. van Berkel. 1995. Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum: evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols. 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
    • 0030999852 scopus 로고    scopus 로고
    • Enigmatic gratuitous induction of the covalent flavoprotein vanillyl-alcohol oxidase in Penicillium simplicissimum
    • Fraaije, M. W., M. Pikkemaat, and W. J. H. van Berkel. 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
  • 7
    • 0030739371 scopus 로고    scopus 로고
    • Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase: Evidence for formation of a p-quinone methide intermediate
    • Fraaije, M. W., and W. J. H. van Berkel. 1997. Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase: evidence for formation of a p-quinone methide intermediate. J. Biol. Chem. 272:18111-18116.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18111-18116
    • Fraaije, M.W.1    Van Berkel, W.J.H.2
  • 10
    • 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
  • 11
    • 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., M. W. Fraaije, A. Mozzarelli, L. Olivi, A. Coda, and W. J. H. van Berkel. 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
  • 12
    • 0021666137 scopus 로고
    • Stereochemistry of 1-(4′-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase
    • McIntire, W. S., D. J. Hopper, J. C. Craig, E. T. Everthart, R. V. Webster, M. J. Causer, and T. P. Singer. 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    Everthart, E.T.4    Webster, R.V.5    Causer, M.J.6    Singer, T.P.7
  • 13
    • 0037560441 scopus 로고
    • The chemical and stereochemical course of oxidation of 4-ethylphenol and other 4-alkylphenols by p-cresol methylhydroxylase
    • D. E. Edmondson and D. B. McCormick (ed.), Walter de Gruyter, Berlin, Germany
    • McIntire, W. S., and C. Bohmont. 1987. The chemical and stereochemical course of oxidation of 4-ethylphenol and other 4-alkylphenols by p-cresol methylhydroxylase, p. 677-686. In D. E. Edmondson and D. B. McCormick (ed.), Flavins and flavoproteins IX. Walter de Gruyter, Berlin, Germany.
    • (1987) Flavins and Flavoproteins IX , pp. 677-686
    • McIntire, W.S.1    Bohmont, C.2
  • 14
    • 0023822940 scopus 로고
    • 2-Octenoyl coenzyme a is a mechanism based inhibitor of pig kidney medium-chain acyl coenzyme a dehydrogenase: Isolation of a target peptide
    • Powell, P. J., and C. Thorpe. 1988. 2-Octenoyl coenzyme A is a mechanism based inhibitor of pig kidney medium-chain acyl coenzyme A dehydrogenase: isolation of a target peptide. Biochemistry 27:8022-8028.
    • (1988) Biochemistry , vol.27 , pp. 8022-8028
    • Powell, P.J.1    Thorpe, C.2
  • 15
    • 0024430224 scopus 로고
    • The purification and characterization of 4-ethylphenol methylenehydroxylase, a flavoenzyme from Pseudomonas putida JD1
    • Reeve, C. D., M. A. Carver, and D. J. Hopper. 1989. The purification and characterization of 4-ethylphenol methylenehydroxylase, a flavoenzyme 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
  • 16
    • 15644362940 scopus 로고    scopus 로고
    • February 1997. Process for producing 4-hydroxycinnamyl alcohols. European patent 0710289B1
    • van Berkel, W. J. H., M. W. Fraaije, and E. de Jong. February 1997. Process for producing 4-hydroxycinnamyl alcohols. European patent 0710289B1.
    • Van Berkel, W.J.H.1    Fraaije, M.W.2    De Jong, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.