메뉴 건너뛰기




Volumn 580, Issue 14, 2006, Pages 3445-3450

Conversion of hydroxyphenylpyruvate dioxygenases into hydroxymandelate synthases by directed evolution

Author keywords

Dioxygenase; Enzyme mechanism; Hydroxyphenylglycine; Non proteinogenic amino acids; Non ribosomal peptide synthesis; Protein engineering

Indexed keywords

4 HYDROXYPHENYLPYRUVATE DIOXYGENASE; HYDROXYMANDELATE SYNTHASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 33646901887     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.05.018     Document Type: Article
Times cited : (25)

References (16)
  • 1
    • 9744253076 scopus 로고    scopus 로고
    • 4-Hydroxyphenylpyruvate dioxygenase
    • Moran G.R. 4-Hydroxyphenylpyruvate dioxygenase. Arch. Biochem. Biophys. 433 (2005) 117-128
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 117-128
    • Moran, G.R.1
  • 2
    • 0026675589 scopus 로고
    • Treatment of hereditary tyrosinaemia type I by inhibition of 4-hydroxyphenylpyruvate dioxygenase
    • Lindstedt S., Holme E., Lock E.A., Hjalmarson O., and Strandvik B. Treatment of hereditary tyrosinaemia type I by inhibition of 4-hydroxyphenylpyruvate dioxygenase. Lancet 340 (1992) 813-817
    • (1992) Lancet , vol.340 , pp. 813-817
    • Lindstedt, S.1    Holme, E.2    Lock, E.A.3    Hjalmarson, O.4    Strandvik, B.5
  • 4
    • 0034616852 scopus 로고    scopus 로고
    • Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine
    • Choroba O.W., Williams D.H., and Spencer J.B. Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 122 (2000) 5389-5390
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5389-5390
    • Choroba, O.W.1    Williams, D.H.2    Spencer, J.B.3
  • 5
    • 0034523992 scopus 로고    scopus 로고
    • Biosynthesis of l-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics
    • Hubbard B.K., Thomas M.G., and Walsh C.T. Biosynthesis of l-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 7 (2000) 931-942
    • (2000) Chem. Biol. , vol.7 , pp. 931-942
    • Hubbard, B.K.1    Thomas, M.G.2    Walsh, C.T.3
  • 6
    • 0037450076 scopus 로고    scopus 로고
    • Vancomycin assembly: nature's way
    • Hubbard B.K., and Walsh C.T. Vancomycin assembly: nature's way. Angew Chem. 42 (2003) 730-756
    • (2003) Angew Chem. , vol.42 , pp. 730-756
    • Hubbard, B.K.1    Walsh, C.T.2
  • 7
    • 0033566995 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway
    • Serre L., Sailland A., Sy D., Boudec P., Rolland A., Pebay-Peyroula E., and Cohen-Addad C. Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway. Struct. Fold Des. 7 (1999) 977-988
    • (1999) Struct. Fold Des. , vol.7 , pp. 977-988
    • Serre, L.1    Sailland, A.2    Sy, D.3    Boudec, P.4    Rolland, A.5    Pebay-Peyroula, E.6    Cohen-Addad, C.7
  • 8
    • 1942437656 scopus 로고    scopus 로고
    • The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase
    • Fritze I.M., Linden L., Freigang J., Auerbach G., Huber R., and Steinbacher S. The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase. Plant Physiol. 134 (2004) 1388-1400
    • (2004) Plant Physiol. , vol.134 , pp. 1388-1400
    • Fritze, I.M.1    Linden, L.2    Freigang, J.3    Auerbach, G.4    Huber, R.5    Steinbacher, S.6
  • 9
    • 2542568185 scopus 로고    scopus 로고
    • Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC
    • Brownlee J.M., Johnson-Winters K., Harrison D.H., and Moran G.R. Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC. Biochemistry 43 (2004) 6370-6377
    • (2004) Biochemistry , vol.43 , pp. 6370-6377
    • Brownlee, J.M.1    Johnson-Winters, K.2    Harrison, D.H.3    Moran, G.R.4
  • 10
    • 4043073398 scopus 로고    scopus 로고
    • Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases
    • Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., and Walsh T.A. Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases. Biochemistry 43 (2004) 10414-10423
    • (2004) Biochemistry , vol.43 , pp. 10414-10423
    • Yang, C.1    Pflugrath, J.W.2    Camper, D.L.3    Foster, M.L.4    Pernich, D.J.5    Walsh, T.A.6
  • 12
    • 0027965019 scopus 로고
    • A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli
    • Denoya C.D., Skinner D.D., and Morgenstern M.R. A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli. J. Bacteriol. 176 (1994) 5312-5319
    • (1994) J. Bacteriol. , vol.176 , pp. 5312-5319
    • Denoya, C.D.1    Skinner, D.D.2    Morgenstern, M.R.3
  • 13
    • 1642494902 scopus 로고    scopus 로고
    • Engineering p-hydroxyphenylpyruvate dioxygenase to a p-hydroxymandelate synthase and evidence for the proposed benzene oxide intermediate in homogentisate formation
    • Gunsior M., Ravel J., Challis G.L., and Townsend C.A. Engineering p-hydroxyphenylpyruvate dioxygenase to a p-hydroxymandelate synthase and evidence for the proposed benzene oxide intermediate in homogentisate formation. Biochemistry 43 (2004) 663-674
    • (2004) Biochemistry , vol.43 , pp. 663-674
    • Gunsior, M.1    Ravel, J.2    Challis, G.L.3    Townsend, C.A.4
  • 14
    • 0037465347 scopus 로고    scopus 로고
    • (4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition
    • Johnson-Winters K., Purpero V.M., Kavana M., Nelson T., and Moran G.R. (4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition. Biochemistry 42 (2003) 2072-2080
    • (2003) Biochemistry , vol.42 , pp. 2072-2080
    • Johnson-Winters, K.1    Purpero, V.M.2    Kavana, M.3    Nelson, T.4    Moran, G.R.5
  • 15
    • 0035929105 scopus 로고    scopus 로고
    • Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics
    • Li T.L., Choroba O.W., Charles E.H., Sandercock A.M., Williams D.H., and Spencer J.B. Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics. Chem. Commun. 18 (2001) 1752-1753
    • (2001) Chem. Commun. , vol.18 , pp. 1752-1753
    • Li, T.L.1    Choroba, O.W.2    Charles, E.H.3    Sandercock, A.M.4    Williams, D.H.5    Spencer, J.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.