메뉴 건너뛰기




Volumn 149, Issue 11, 2003, Pages 3321-3330

(De)regulation of key enzyme steps in the shikimate pathway and phenylalanine-specific pathway of the actinomycete Amycolatopsis methanolica

Author keywords

[No Author keywords available]

Indexed keywords

2 DEHYDRO 3 DEOXYPHOSPHOHEPTONATE ALDOLASE; 4 FLUOROPHENYLALANINE; CHORISMATE MUTASE; GLUCOSE; PHENYLALANINE; PREPHENATE DEHYDRATASE; SHIKIMIC ACID; TRYPTOPHAN; TYROSINE;

EID: 0344443205     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26494-0     Document Type: Article
Times cited : (25)

References (39)
  • 2
    • 0030029183 scopus 로고    scopus 로고
    • Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase
    • Alves, A. M., Meijer, W. G., Vrijbloed, J. W. & Dijkhuizen, L. (1996). Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase. J Bacteriol 178, 149-155.
    • (1996) J. Bacteriol. , vol.178 , pp. 149-155
    • Alves, A.M.1    Meijer, W.G.2    Vrijbloed, J.W.3    Dijkhuizen, L.4
  • 3
    • 0037063517 scopus 로고    scopus 로고
    • Characterization of the early stage aminoshikimate pathway in the formation of 3-amino-5-hydroxybenzoic acid: The RifN protein specifically converts kanosamine into kanosamine 6-phosphate
    • Arakawa, K., Muller, R., Mahmud, T., Yu, T. W. & Floss, H. G. (2002). Characterization of the early stage aminoshikimate pathway in the formation of 3-amino-5-hydroxybenzoic acid: the RifN protein specifically converts kanosamine into kanosamine 6-phosphate. J Am Chem Soc 124, 10644-10645.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10644-10645
    • Arakawa, K.1    Muller, R.2    Mahmud, T.3    Yu, T.W.4    Floss, H.G.5
  • 4
    • 13144258781 scopus 로고    scopus 로고
    • Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699
    • 9 other authors
    • August, P. R., Tang, L., Yoon, Y. J. & 9 other authors (1998). Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699. Chem Biol 5, 69-79.
    • (1998) Chem. Biol. , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2    Yoon, Y.J.3
  • 5
    • 0025581736 scopus 로고
    • The shikimate pathway. A metabolic tree with many branches
    • Bentley, R. (1990). The shikimate pathway. A metabolic tree with many branches. Crit Rev Biochem Mol Biol 25, 307-384.
    • (1990) Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 307-384
    • Bentley, R.1
  • 6
    • 0037046560 scopus 로고    scopus 로고
    • Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
    • 40 other authors
    • Bentley, S. D., Chater, K. F., Cerdeno-Tarraga, A. M. & 40 other authors (2002). Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417, 141-147.
    • (2002) Nature , vol.417 , pp. 141-147
    • Bentley, S.D.1    Chater, K.F.2    Cerdeno-Tarraga, A.M.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0033118217 scopus 로고    scopus 로고
    • Biosynthesis of ansatrienin (mycotrienin) and naphthomycin. Identification and analysis of two separate biosynthetic gene clusters in Streptomyces collinus Tu 1892
    • Chen, S., von Bamberg, D., Hale, V., Breuer, M., Hardt, B., Muller, R., Floss, H. G., Reynolds, K. A. & Leistner, E. (1999). Biosynthesis of ansatrienin (mycotrienin) and naphthomycin. Identification and analysis of two separate biosynthetic gene clusters in Streptomyces collinus Tu 1892. Eur J Biochem 261, 98-107.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 98-107
    • Chen, S.1    von Bamberg, D.2    Hale, V.3    Breuer, M.4    Hardt, B.5    Muller, R.6    Floss, H.G.7    Reynolds, K.A.8    Leistner, E.9
  • 9
    • 0011866174 scopus 로고
    • Phenylalanine and tyrosine metabolism in the facultative methylotroph Nocardia sp. 239
    • de Boer, L., Harder, W. & Dijkhuizen, L. (1988). Phenylalanine and tyrosine metabolism in the facultative methylotroph Nocardia sp. 239. Arch Microbiol 149, 459-465.
    • (1988) Arch. Microbiol. , vol.149 , pp. 459-465
    • de Boer, L.1    Harder, W.2    Dijkhuizen, L.3
  • 10
    • 0038675755 scopus 로고
    • Regulation of aromatic amino acid biosynthesis in the ribulose monophosphate cycle methylotroph Nocardia sp. 239
    • de Boer, L., Vrijbloed, J. W., Grobben, G. & Dijkhuizen, L. (1989). Regulation of aromatic amino acid biosynthesis in the ribulose monophosphate cycle methylotroph Nocardia sp. 239. Arch Microbiol 151, 319-325.
    • (1989) Arch. Microbiol. , vol.151 , pp. 319-325
    • de Boer, L.1    Vrijbloed, J.W.2    Grobben, G.3    Dijkhuizen, L.4
  • 11
    • 0025340932 scopus 로고
    • Biosynthesis of aromatic amino acids in Nocardia sp. 239: Effects of amino acid analogues on growth and regulatory enzymes
    • de Boer, L., Grobben, G., Vrijbloed, J. W. & Dijkhuizen, L. (1990). Biosynthesis of aromatic amino acids in Nocardia sp. 239: effects of amino acid analogues on growth and regulatory enzymes. Appl Microbiol Biotechnol 33, 183-189.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 183-189
    • de Boer, L.1    Grobben, G.2    Vrijbloed, J.W.3    Dijkhuizen, L.4
  • 12
    • 0015523331 scopus 로고
    • Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties
    • Dopheide, T. A., Crewther, P. & Davidson, B. E. (1972). Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties. J Biol Chem 247, 4447-4452.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4447-4452
    • Dopheide, T.A.1    Crewther, P.2    Davidson, B.E.3
  • 13
    • 0028971095 scopus 로고
    • Chorismate mutase and 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the methylotrophic actinomycete Amycolatopsis methanolica
    • Euverink, G. J., Hessels, G. I., Franke, C. & Dijkhuizen, L. (1995a). Chorismate mutase and 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the methylotrophic actinomycete Amycolatopsis methanolica. Appl Environ Microbiol 61, 3796-3803.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3796-3803
    • Euverink, G.J.1    Hessels, G.I.2    Franke, C.3    Dijkhuizen, L.4
  • 14
    • 0029012617 scopus 로고
    • Prephenate dehydratase of the actinomycete Amycolatopsis methanolica: Purification and characterization of wild-type and deregulated mutant proteins
    • Euverink, G. J., Wolters, D. J. & Dijkhuizen, L. (1995b). Prephenate dehydratase of the actinomycete Amycolatopsis methanolica: purification and characterization of wild-type and deregulated mutant proteins. Biochem J 308, 313-320.
    • (1995) Biochem. J. , vol.308 , pp. 313-320
    • Euverink, G.J.1    Wolters, D.J.2    Dijkhuizen, L.3
  • 15
    • 0030002925 scopus 로고    scopus 로고
    • Isolation and analysis of mutants of the methylotrophic actinomycete Amycolatopsis methanolica blocked in aromatic amino acid biosynthesis
    • Euverink, G.-J. W., Vrijbloed, J. W., Hessels, G. I. & Dijkhuizen, L. (1996). Isolation and analysis of mutants of the methylotrophic actinomycete Amycolatopsis methanolica blocked in aromatic amino acid biosynthesis. FEMS Microbiol Lett 136, 275-281.
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 275-281
    • Euverink, G.-J.W.1    Vrijbloed, J.W.2    Hessels, G.I.3    Dijkhuizen, L.4
  • 16
    • 0034972509 scopus 로고    scopus 로고
    • Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris
    • Gosset, G., Bonner, C. A. & Jensen, R. A. (2001). Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris. J Bacteriol 183, 4061-4070.
    • (2001) J. Bacteriol. , vol.183 , pp. 4061-4070
    • Gosset, G.1    Bonner, C.A.2    Jensen, R.A.3
  • 17
    • 0034775265 scopus 로고    scopus 로고
    • The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a mono-modular non-ribosomal peptide synthetase gene
    • He, J., Magarvey, N., Piraee, M. & Vining, L. C. (2001). The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a mono-modular non-ribosomal peptide synthetase gene. Microbiology 147, 2817-2829.
    • (2001) Microbiology , vol.147 , pp. 2817-2829
    • He, J.1    Magarvey, N.2    Piraee, M.3    Vining, L.C.4
  • 18
    • 0033925731 scopus 로고    scopus 로고
    • Primary metabolism and its control in streptomycetes: A most unusual group of bacteria
    • Hodgson, D. A. (2000). Primary metabolism and its control in streptomycetes: a most unusual group of bacteria. Adv Microb Physiol 42, 47-238.
    • (2000) Adv. Microb. Physiol. , vol.42 , pp. 47-238
    • Hodgson, D.A.1
  • 21
    • 9444271749 scopus 로고    scopus 로고
    • Biosynthesis of 3-amino-5-hydroxybenzoic acid, the precursor of mC(7)N units in ansamycin antibiotics
    • 8 other authors
    • Kim, C. G., Kirschning, A., Bergon, P. & 8 other authors (1996b). Biosynthesis of 3-amino-5-hydroxybenzoic acid, the precursor of mC(7)N units in ansamycin antibiotics. J Am Chem Soc 118, 7486-7491.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7486-7491
    • Kim, C.G.1    Kirschning, A.2    Bergon, P.3
  • 22
    • 0033180292 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs, A. R. (1999). The biosynthesis of shikimate metabolites. Nat Prod Rep 16, 525-560.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 525-560
    • Knaggs, A.R.1
  • 23
    • 0017864182 scopus 로고
    • 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli
    • McCandliss, R. J., Poling, M. D. & Herrmann, K. M. (1978). 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli. J Biol Chem 253, 4259-4265.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4259-4265
    • McCandliss, R.J.1    Poling, M.D.2    Herrmann, K.M.3
  • 24
    • 0039001059 scopus 로고
    • Improved double-stranded DNA sequencing using the linear polymerase chain reaction
    • Murray, V. (1989). Improved double-stranded DNA sequencing using the linear polymerase chain reaction. Nucleic Acids Res 17, 8889.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8889
    • Murray, V.1
  • 25
    • 0026643267 scopus 로고
    • Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase
    • Nelms, J., Edwards, R. M., Warwick, J. & Fotheringham, I. (1992). Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase. Appl Environ Microbiol 58, 2592-2598.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2592-2598
    • Nelms, J.1    Edwards, R.M.2    Warwick, J.3    Fotheringham, I.4
  • 26
    • 0017696820 scopus 로고
    • Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa
    • Patel, N., Pierson, D. L. & Jensen, R. A. (1977). Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa. J Biol Chem 252, 5839-5846.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5839-5846
    • Patel, N.1    Pierson, D.L.2    Jensen, R.A.3
  • 27
    • 0028834892 scopus 로고
    • Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84
    • Pierson, L. S., Gaffney, T., Lam, S. & Gong, F. (1995). Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84. FEMS Microbiol Lett 134, 299-307.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 299-307
    • Pierson, L.S.1    Gaffney, T.2    Lam, S.3    Gong, F.4
  • 28
    • 0033592422 scopus 로고    scopus 로고
    • Regulation of phenylalanine biosynthesis. Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein
    • Pohnert, G., Zhang, S., Husain, A., Wilson, D. B. & Ganem, B. (1999). Regulation of phenylalanine biosynthesis. Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein. Biochemistry 38, 12212-12217.
    • (1999) Biochemistry , vol.38 , pp. 12212-12217
    • Pohnert, G.1    Zhang, S.2    Husain, A.3    Wilson, D.B.4    Ganem, B.5
  • 29
    • 0026065718 scopus 로고
    • Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli
    • Ray, J. M. & Bauerle, R. (1991). Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. J Bacteriol 173, 1894-1901.
    • (1991) J. Bacteriol. , vol.173 , pp. 1894-1901
    • Ray, J.M.1    Bauerle, R.2
  • 31
    • 0017114285 scopus 로고
    • 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli
    • Schoner, R. & Herrmann, K. M. (1976). 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. J Biol Chem 251, 5440-5447.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5440-5447
    • Schoner, R.1    Herrmann, K.M.2
  • 32
    • 0021125701 scopus 로고
    • The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Shultz, J., Hermodson, M. A., Garner, C. C. & Herrmann, K. M. (1984). The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J Biol Chem 259, 9655-9661.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9655-9661
    • Shultz, J.1    Hermodson, M.A.2    Garner, C.C.3    Herrmann, K.M.4
  • 33
    • 0034084373 scopus 로고    scopus 로고
    • Stigmatella aurantiaca Sg a15 carries genes encoding type I and type II 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases: Involvement of a type II synthase in aurachin biosynthesis
    • Silakowski, B., Kunze, B. & Muller, R. (2000). Stigmatella aurantiaca Sg a15 carries genes encoding type I and type II 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases: involvement of a type II synthase in aurachin biosynthesis. Arch Microbiol 173, 403-411.
    • (2000) Arch. Microbiol. , vol.173 , pp. 403-411
    • Silakowski, B.1    Kunze, B.2    Muller, R.3
  • 34
    • 0018854095 scopus 로고
    • Purification and properties of bifunctional 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase-chorismate mutase component A from Brevibacterium flavum
    • Sugimoto, S. & Shiio, I. (1980). Purification and properties of bifunctional 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase-chorismate mutase component A from Brevibacterium flavum. J Biochem 87, 881-890.
    • (1980) J. Biochem. , vol.87 , pp. 881-890
    • Sugimoto, S.1    Shiio, I.2
  • 36
    • 0028853508 scopus 로고
    • Molecular cloning with a pMEA300-derived shuttle vector and characterization of the Amycolatopsis methanolica prephenate dehydratase gene
    • Vrijbloed, J. W., van Hylckama Vlieg, J., van der Put, N. M., Hessels, G. I. & Dijkhuizen, L. (1995). Molecular cloning with a pMEA300-derived shuttle vector and characterization of the Amycolatopsis methanolica prephenate dehydratase gene. J Bacteriol 177, 6666-6669.
    • (1995) J. Bacteriol. , vol.177 , pp. 6666-6669
    • Vrijbloed, J.W.1    van Hylckama Vlieg, J.2    van der Put, N.M.3    Hessels, G.I.4    Dijkhuizen, L.5
  • 37
    • 0029846030 scopus 로고    scopus 로고
    • Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa
    • Walker, G. E., Dunbar, B., Hunter, I. S., Nimmo, H. G. & Coggins, J. R. (1996). Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa. Microbiology 142, 1973-1982.
    • (1996) Microbiology , vol.142 , pp. 1973-1982
    • Walker, G.E.1    Dunbar, B.2    Hunter, I.S.3    Nimmo, H.G.4    Coggins, J.R.5
  • 38
    • 0035918169 scopus 로고    scopus 로고
    • Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in Amycolatopsis mediterranei S699
    • Yu, T. W., Muller, R., Muller, M., Zhang, X., Draeger, G., Kim, C. G., Leistner, E. & Floss, H. G. (2001). Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in Amycolatopsis mediterranei S699. J Biol Chem 276, 12546-12555.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12546-12555
    • Yu, T.W.1    Muller, R.2    Muller, M.3    Zhang, X.4    Draeger, G.5    Kim, C.G.6    Leistner, E.7    Floss, H.G.8
  • 39
    • 0032513052 scopus 로고    scopus 로고
    • Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins
    • Zhang, S., Pohnert, G., Kongsaeree, P., Wilson, D. B., Clardy, J. & Ganem, B. (1998). Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. J Biol Chem 273,
    • (1998) J. Biol. Chem. , vol.273 , pp. 6248-6253
    • Zhang, S.1    Pohnert, G.2    Kongsaeree, P.3    Wilson, D.B.4    Clardy, J.5    Ganem, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.