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Volumn 378, Issue 3-4, 1997, Pages 207-210

Feedback Inhibition of Dihydrodipicolinate Synthase Enzymes by L-Lysine

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE;

EID: 1842372714     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.3-4.207     Document Type: Article
Times cited : (20)

References (25)
  • 1
    • 0021245679 scopus 로고
    • Lysine biosynthesis in Methanobacterium thermoautotropi-cum is by the diamino pimelic-acid pathway
    • Bakhiet, N., Forney, F. W., Stahly, D. R. and Daniels, L. (1984). Lysine biosynthesis in Methanobacterium thermoautotropi-cum is by the diamino pimelic-acid pathway. Current Microbiol. 70, 195-198.
    • (1984) Current Microbiol. , vol.70 , pp. 195-198
    • Bakhiet, N.1    Forney, F.W.2    Stahly, D.R.3    Daniels, L.4
  • 2
    • 0023002781 scopus 로고
    • Regulation of the enzymes of lysine biosynthesis in Bacillus sphaericus NCTC 9602 during vegetative growth
    • Bartlett, A. T. M., and White, R. J. (1986). Regulation of the enzymes of lysine biosynthesis in Bacillus sphaericus NCTC 9602 during vegetative growth. J. Gen. Microbiol. 732, 3169-3177.
    • (1986) J. Gen. Microbiol. , vol.732 , pp. 3169-3177
    • Bartlett, A.T.M.1    White, R.J.2
  • 3
    • 0031012162 scopus 로고    scopus 로고
    • Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by x-ray crystallography and NMR-spectroscopy
    • Bückling, S., Renner, C., Laber, B., Pohlenz, H.-D., Holak, T.A., and Huber, R. (1997). Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by x-ray crystallography and NMR-spectroscopy. Biochemistry 36, 24-33.
    • (1997) Biochemistry , vol.36 , pp. 24-33
    • Bückling, S.1    Renner, C.2    Laber, B.3    Pohlenz, H.-D.4    Holak, T.A.5    Huber, R.6
  • 4
    • 0030293719 scopus 로고    scopus 로고
    • Engineering of the aspartate family biosynthetic pathway in bariey {Hordeum vulgare L.) by transformation with heterologous genes encoding feed-back-insensitive aspartate kinase and dihydrodipicolinate synthase
    • Brinch-Pedersn, H., Galili, G., Knudsen, S., and Holm, R. B. (1996). Engineering of the aspartate family biosynthetic pathway in bariey {Hordeum vulgare L.) by transformation with heterologous genes encoding feed-back-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 32, 611-620.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 611-620
    • Brinch-Pedersn, H.1    Galili, G.2    Knudsen, S.3    Holm, R.B.4
  • 5
    • 0024145176 scopus 로고
    • Regulation of enzymes of lysine biosynthesis in Coryne-bacterium glutamicum
    • Cremer, J., Treptow, C., Eggeling, L., and Sahm, H. (1988). Regulation of enzymes of lysine biosynthesis in Coryne-bacterium glutamicum. J. Gen. Microbiol. 134, 3221-3229.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 3221-3229
    • Cremer, J.1    Treptow, C.2    Eggeling, L.3    Sahm, H.4
  • 6
    • 0001692779 scopus 로고
    • Purification and characterization of dihydrodipicolinate synthase from pea
    • Dereppe, C., Bold, G., Ghisalba, O., Ebert, E., and Schär, H.-P. (1992). Purification and characterization of dihydrodipicolinate synthase from pea. Plant Physiol. 98, 813-821.
    • (1992) Plant Physiol. , vol.98 , pp. 813-821
    • Dereppe, C.1    Bold, G.2    Ghisalba, O.3    Ebert, E.4    Schär, H.-P.5
  • 8
    • 0001524023 scopus 로고
    • Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris
    • Frankard, V., Ghislain, M., and Jacobs, M. (1992). Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris. Plant Physiol. 99, 1285-1293.
    • (1992) Plant Physiol. , vol.99 , pp. 1285-1293
    • Frankard, V.1    Ghislain, M.2    Jacobs, M.3
  • 9
    • 0001693369 scopus 로고
    • Dihydrodipicolinate synthase of Nicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway
    • Ghislain, M., Frankard, V., and Jacobs, M. (1990). Dihydrodipicolinate synthase of Nicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway. Planta 180, 480-486.
    • (1990) Planta , vol.180 , pp. 480-486
    • Ghislain, M.1    Frankard, V.2    Jacobs, M.3
  • 10
    • 0029394916 scopus 로고
    • A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris, leads to lysine overproduction
    • Ghislain, M., Frankard, V., and Jacobs, M. (1995). A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris, leads to lysine overproduction. Plant J. 8, 733-743.
    • (1995) Plant J. , vol.8 , pp. 733-743
    • Ghislain, M.1    Frankard, V.2    Jacobs, M.3
  • 11
    • 0016656134 scopus 로고
    • Regulation of dihydrodipicolinate synthase during growth and sporulation of Bacillus cereus
    • Hoganson, D.A., and Stahly, D.P. (1975). Regulation of dihydrodipicolinate synthase during growth and sporulation of Bacillus cereus. J. Bacterid. 124, 1344-1350.
    • (1975) J. Bacterid. , vol.124 , pp. 1344-1350
    • Hoganson, D.A.1    Stahly, D.P.2
  • 12
    • 0001285394 scopus 로고
    • Purification and characterization of dihydrodipicolinate synthase from wheat suspension cell cultures
    • Kumpaisal, R., Hashimoto, T., and Yamada, Y. (1987). Purification and characterization of dihydrodipicolinate synthase from wheat suspension cell cultures. Plant Physiol. 85, 145-151.
    • (1987) Plant Physiol. , vol.85 , pp. 145-151
    • Kumpaisal, R.1    Hashimoto, T.2    Yamada, Y.3
  • 13
    • 0026486643 scopus 로고
    • Escherichia coli dihydrodipicolinate synthase: identification of the active site and crystallisation
    • Laber, B., Gomis-Ruth, X., Romao, M.J., and Huber, R. (1992). Escherichia coli dihydrodipicolinate synthase: identification of the active site and crystallisation. Biochem. J. 288, 291-295.
    • (1992) Biochem. J. , vol.288 , pp. 291-295
    • Laber, B.1    Gomis-Ruth, X.2    Romao, M.J.3    Huber, R.4
  • 14
    • 0010741906 scopus 로고
    • Regulation of lysine and threonine synthesis in carrot cell suspension cultures and whole carrot roots
    • Matthews, B.R., and Widholm, J.M. (1978). Regulation of lysine and threonine synthesis in carrot cell suspension cultures and whole carrot roots. Planta 747, 315-321.
    • (1978) Planta , vol.747 , pp. 315-321
    • Matthews, B.R.1    Widholm, J.M.2
  • 15
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution
    • Minalaldt, C., Korndorfer, I., and Huber, R. (1995). The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. J. Mol. Biol. 246, 227-239.
    • (1995) J. Mol. Biol. , vol.246 , pp. 227-239
    • Minalaldt, C.1    Korndorfer, I.2    Huber, R.3
  • 16
    • 0002378472 scopus 로고
    • Lysine overproducer mutants with an altered dihydrodipicolinate synthase from protoplast culture of Nicotiana sylvestris
    • Negrutiu, I., Cattoir-Reynaerts, V., Verbruggen, I., and Jacobs, M. (1984). Lysine overproducer mutants with an altered dihydrodipicolinate synthase from protoplast culture of Nicotiana sylvestris. Theor. Appl. Genet. 68, 11-20.
    • (1984) Theor. Appl. Genet. , vol.68 , pp. 11-20
    • Negrutiu, I.1    Cattoir-Reynaerts, V.2    Verbruggen, I.3    Jacobs, M.4
  • 17
    • 0026903342 scopus 로고
    • Regulation of lysine synthesis in transgenic potato plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts
    • Perl, A., Shaul, O., and Galili, G. (1992). Regulation of lysine synthesis in transgenic potato plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts. Plant Mol. Biol. 19, 815-823.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 815-823
    • Perl, A.1    Shaul, O.2    Galili, G.3
  • 18
    • 0001188552 scopus 로고
    • Increased lysine synthesis in transgenic tobacco plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts
    • Shaul, O., and Galili, G. (1991). Increased lysine synthesis in transgenic tobacco plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts. Plant J. 2, 203-209.
    • (1991) Plant J. , vol.2 , pp. 203-209
    • Shaul, O.1    Galili, G.2
  • 20
    • 0028035794 scopus 로고
    • Regulation of dihydrodipicolinate synthase and diaminopimelate decarboxylase activity in Bacillus stearothermophilus
    • Selli, A., Crociani, R., Di Gioia, D., Fava, F., Crisetig, G., and Matteuzi, D. (1994). Regulation of dihydrodipicolinate synthase and diaminopimelate decarboxylase activity in Bacillus stearothermophilus. Ital. J. Biochem. 4, 29-35.
    • (1994) Ital. J. Biochem. , vol.4 , pp. 29-35
    • Selli, A.1    Crociani, R.2    Di Gioia, D.3    Fava, F.4    Crisetig, G.5    Matteuzi, D.6
  • 21
    • 0014664053 scopus 로고
    • Dihydrodipicolinate synthase of Bacillus li-cheniformis
    • Stahly, D.R. (1969). Dihydrodipicolinate synthase of Bacillus li-cheniformis. Biochim. Biophys. Acta 797, 439-451.
    • (1969) Biochim. Biophys. Acta , vol.797 , pp. 439-451
    • Stahly, D.R.1
  • 22
    • 0017871994 scopus 로고
    • Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum
    • Tosaka, O., and Takinami, K. (1978). Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum. Agric. Biol. Chem. 42, 95-100.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 95-100
    • Tosaka, O.1    Takinami, K.2
  • 23
    • 0001737949 scopus 로고
    • Spinach leaf dihydrodipicolinate synthase: partial purification and characterization
    • Wallsgrove, R.M., and Mazelis, M. (1981). Spinach leaf dihydrodipicolinate synthase: partial purification and characterization. Phytochem. 20, 2651-2655.
    • (1981) Phytochem , vol.20 , pp. 2651-2655
    • Wallsgrove, R.M.1    Mazelis, M.2
  • 24
    • 0014707216 scopus 로고
    • Partial purification and characterization of dihydrodipicolinic acid synthase from sporulating Bacillus megaterium
    • Webster, R. H., and Lechowich, R. V. (1970). Partial purification and characterization of dihydrodipicolinic acid synthase from sporulating Bacillus megaterium. J. Bacterid. 707, 118-126.
    • (1970) J. Bacterid. , vol.707 , pp. 118-126
    • Webster, R.H.1    Lechowich, R.V.2
  • 25
    • 0016271651 scopus 로고
    • Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis
    • Yakamura, R., Ikeda, Y., Kimura, K., and Sasakawa, T. (1974). Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis. J. Biochem. 76, 611-621.
    • (1974) J. Biochem. , vol.76 , pp. 611-621
    • Yakamura, R.1    Ikeda, Y.2    Kimura, K.3    Sasakawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.