메뉴 건너뛰기




Volumn 373, Issue 3, 2003, Pages 909-916

The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase

Author keywords

Aspartate racemase; Cyanobacteria; Glutamate racemase; Microcystin; Microcystis aeruginosa; Non ribosomal peptide

Indexed keywords

BACTERIA; BIOSYNTHESIS; CHROMATOGRAPHIC ANALYSIS; ENZYMES;

EID: 0042068174     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030396     Document Type: Article
Times cited : (47)

References (23)
  • 2
    • 0025333146 scopus 로고
    • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants
    • MacKintosh, C., Beattie, K. A., Klumpp, S., Cohen, P. and Codd, G. A. (1990) Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Lett. 264, 187-192
    • (1990) FEBS Lett. , vol.264 , pp. 187-192
    • MacKintosh, C.1    Beattie, K.A.2    Klumpp, S.3    Cohen, P.4    Codd, G.A.5
  • 3
    • 0343196710 scopus 로고    scopus 로고
    • Neoplastic nodular formation in mouse liver induced by repeated intraperitoneal injections of microcystin-LR
    • Ito, E., Kondo, F., Terao, K. and Harada, K-I. (1997) Neoplastic nodular formation in mouse liver induced by repeated intraperitoneal injections of microcystin-LR. Toxicon 35, 1453-1457
    • (1997) Toxicon , vol.35 , pp. 1453-1457
    • Ito, E.1    Kondo, F.2    Terao, K.3    Harada, K.-I.4
  • 4
    • 0036617994 scopus 로고    scopus 로고
    • Relationship between microcystin in drinking water and colorectal cancer
    • Zhou, L., Yu, H. and Chen, K. (2002) Relationship between microcystin in drinking water and colorectal cancer. Biomed. Environ. Sci. 15, 166-171
    • (2002) Biomed. Environ. Sci. , vol.15 , pp. 166-171
    • Zhou, L.1    Yu, H.2    Chen, K.3
  • 5
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: An integrated peptide-polyketide synthetase system
    • Tillett, B., Dittmann, E., Erhard, M., von Döhren, H., Börner, T. and Neilan, B. A. (2000) Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: an integrated peptide-polyketide synthetase system. Chem. Biol. 7, 753-764
    • (2000) Chem. Biol. , vol.7 , pp. 753-764
    • Tillett, B.1    Dittmann, E.2    Erhard, M.3    Von Döhren, H.4    Börner, T.5    Neilan, B.A.6
  • 6
    • 0032873121 scopus 로고    scopus 로고
    • Genetic analysis of the peptide synthetase genes for a cyclic heptapeptide microcystin in Microcystis spp.
    • Tokyo
    • Nishizawa, T., Asayama, M., Fujii, K., Harada, K. and Shirai, M. (2000) Genetic analysis of the peptide synthetase genes for a cyclic heptapeptide microcystin in Microcystis spp. J. Biochem. (Tokyo) 126, 520-529
    • (2000) J. Biochem. , vol.126 , pp. 520-529
    • Nishizawa, T.1    Asayama, M.2    Fujii, K.3    Harada, K.4    Shirai, M.5
  • 7
    • 0034115536 scopus 로고    scopus 로고
    • Polyketide synthase gene coupled to the peptide synthetase module involved in the biosynthesis of the cyclic heptapeptide microcystin
    • Tokyo
    • Nishizawa, T., Ueda, A., Asayama, M., Fujii, K., Harada, K., Ochi, K. and Shirai, M. (2000) Polyketide synthase gene coupled to the peptide synthetase module involved in the biosynthesis of the cyclic heptapeptide microcystin. J. Biochem. (Tokyo) 127, 779-789
    • (2000) J. Biochem. , vol.127 , pp. 779-789
    • Nishizawa, T.1    Ueda, A.2    Asayama, M.3    Fujii, K.4    Harada, K.5    Ochi, K.6    Shirai, M.7
  • 8
    • 0035016977 scopus 로고    scopus 로고
    • Cyclic heptapeptide microcystin biosynthesis requires the glutamate racemase gene
    • Nishizawa, T., Asayama, M. and Shirai, M. (2001) Cyclic heptapeptide microcystin biosynthesis requires the glutamate racemase gene. Microbiology 147, 1235-1241
    • (2001) Microbiology , vol.147 , pp. 1235-1241
    • Nishizawa, T.1    Asayama, M.2    Shirai, M.3
  • 9
    • 0018409915 scopus 로고
    • Generic assignment, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., Desrulles, J., Waterbury, J. B., Herdman, M. and Stanier, R. Y. (1979) Generic assignment, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 11, 1-61
    • (1979) J. Gen. Microbiol. , vol.11 , pp. 1-61
    • Rippka, R.1    Desrulles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 11
    • 0002937356 scopus 로고
    • Tests on nif probes and DNA hybridization
    • Franche, X. and Damerval, T. G. (1988) Tests on nif probes and DNA hybridization. Methods Enzymol 167, 803-808
    • (1988) Methods Enzymol. , vol.167 , pp. 803-808
    • Franche, X.1    Damerval, T.G.2
  • 12
    • 0034857464 scopus 로고    scopus 로고
    • Characterization of the Cph1 holo-phytochrome from Synechocystis sp. PCC 6803
    • Hübschmann, T, Börner, T., Hartmann, E. and Lamparter, T. (2001) Characterization of the Cph1 holo-phytochrome from Synechocystis sp. PCC 6803. Eur. J Biochem. 268, 2055-2063
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2055-2063
    • Hübschmann, T.1    Börner, T.2    Hartmann, E.3    Lamparter, T.4
  • 13
    • 0000340883 scopus 로고    scopus 로고
    • Vectors of the complementation analysis of cyanobacterial mutants
    • Zinchenko, V. V., Piven, I. V., Melnik, V. A. and Shestakov, S. V. (1999) Vectors of the complementation analysis of cyanobacterial mutants. Russ. J. Genet. 35, 228-232
    • (1999) Russ. J. Genet. , vol.35 , pp. 228-232
    • Zinchenko, V.V.1    Piven, I.V.2    Melnik, V.A.3    Shestakov, S.V.4
  • 14
    • 0024240748 scopus 로고
    • Conjugal transfer of DNA to cyanobacteria
    • Elhai, J. and Wolk, C. P. (1988) Conjugal transfer of DNA to cyanobacteria. Methods Enzymol. 167, 747-754
    • (1988) Methods Enzymol. , vol.167 , pp. 747-754
    • Elhai, J.1    Wolk, C.P.2
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram 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
  • 17
    • 0027155359 scopus 로고
    • Isotope effects and the identification of catalytic residues in the reaction catalysed by glutamate racemase
    • Tanner, M. E., Gallo, K. A. and Knowles, J. R. (1993) Isotope effects and the identification of catalytic residues in the reaction catalysed by glutamate racemase. Biochemistry 32, 3998-4006
    • (1993) Biochemistry , vol.32 , pp. 3998-4006
    • Tanner, M.E.1    Gallo, K.A.2    Knowles, J.R.3
  • 18
    • 0036301494 scopus 로고    scopus 로고
    • Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization
    • Liu, L., Iwata, K., Kita, A., Kawarabayasi, Y., Yohda, M. and Miki, K. (2002) Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization. J. Mol. Biol. 319, 479-489
    • (2002) J. Mol. Biol. , vol.319 , pp. 479-489
    • Liu, L.1    Iwata, K.2    Kita, A.3    Kawarabayasi, Y.4    Yohda, M.5    Miki, K.6
  • 19
    • 0035967535 scopus 로고    scopus 로고
    • Active site residues of glutamate racemase
    • Glavas, S. and Tanner, M. E. (2001) Active site residues of glutamate racemase. Biochemistry 40, 6199-6204
    • (2001) Biochemistry , vol.40 , pp. 6199-6204
    • Glavas, S.1    Tanner, M.E.2
  • 20
    • 0033559990 scopus 로고    scopus 로고
    • Construction and characterization of a functional mutant of Synechocystis 6803 harbouring a eukaryotic PSII-H subunit
    • Chiaramonte, S., Giacometti, G. M. and Bergantino, E. (1999) Construction and characterization of a functional mutant of Synechocystis 6803 harbouring a eukaryotic PSII-H subunit. Eur. J. Biochem. 260, 833-843
    • (1999) Eur. J. Biochem. , vol.260 , pp. 833-843
    • Chiaramonte, S.1    Giacometti, G.M.2    Bergantino, E.3
  • 21
    • 0026655552 scopus 로고
    • Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase
    • Yamauchi, T., Choi, S. Y., Okada, H., Yohda, M., Kumagai, H., Esaki, N. and Soda, K. (1992) Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase. J. Biol Chem. 267, 18361-18364
    • (1992) J. Biol Chem. , vol.267 , pp. 18361-18364
    • Yamauchi, T.1    Choi, S.Y.2    Okada, H.3    Yohda, M.4    Kumagai, H.5    Esaki, N.6    Soda, K.7
  • 22
    • 0031778765 scopus 로고    scopus 로고
    • Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-γ-glutamate
    • Tokyo
    • Ashiuchi, M., Tani, K., Soda, K. and Misono, H. (1998) Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-γ-glutamate. J. Biochem. (Tokyo) 123, 1156-1163
    • (1998) J. Biochem. , vol.123 , pp. 1156-1163
    • Ashiuchi, M.1    Tani, K.2    Soda, K.3    Misono, H.4
  • 23
    • 0023643132 scopus 로고
    • Partial purification and specificity studies of the D-glutamate-adding and D-alanyk-D-alanine-adding enzymes from Escherichia coli K12
    • Michaud, C., Blanot, D., Flouret, B. and van Heijenoort, J. (1987) Partial purification and specificity studies of the D-glutamate-adding and D-alanyk-D-alanine-adding enzymes from Escherichia coli K12. Eur. J. Biochem. 166, 631-637
    • (1987) Eur. J. Biochem. , vol.166 , pp. 631-637
    • Michaud, C.1    Blanot, D.2    Flouret, B.3    Van Heijenoort, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.