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Volumn 65, Issue 6, 2001, Pages 1391-1394

Characterization of aspartate kinase III of Bacillus subtilis

Author keywords

Aspartate kinase; Bacillus subtilis; Concerted inhibition

Indexed keywords

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 0035378128     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.1391     Document Type: Article
Times cited : (14)

References (20)
  • 1
    • 0000993235 scopus 로고
    • Amino acid biosynthesis and its regulation
    • Umbarger, H. E., Amino acid biosynthesis and its regulation. Annu. Rev. Biochem., 41, 533-606 (1978).
    • (1978) Annu. Rev. Biochem. , vol.41 , pp. 533-606
    • Umbarger, H.E.1
  • 3
    • 0017370709 scopus 로고
    • Subunit structure of the methionine-repressible aspartokinase II-homoserine dehydrogenase II from Escherichia coli K12
    • Dautry-Varsat, A., Sibilli-Weill, L., and Cohen, G. N., Subunit structure of the methionine-repressible aspartokinase II-homoserine dehydrogenase II from Escherichia coli K12. Eur. J. Biochem., 76, 1-6 (1977).
    • (1977) Eur. J. Biochem. , vol.76 , pp. 1-6
    • Dautry-Varsat, A.1    Sibilli-Weill, L.2    Cohen, G.N.3
  • 4
    • 0015711917 scopus 로고
    • Subunit structure of aspartokinase 3 of Escherichia coli K12
    • Richaud. C., Mazat. J. P., Gros. C., and Patte, J. C., Subunit structure of aspartokinase 3 of Escherichia coli K12. Eur. J. Biochem., 40, 619-29 (1973).
    • (1973) Eur. J. Biochem. , vol.40 , pp. 619-629
    • Richaud, C.1    Mazat, J.P.2    Gros, C.3    Patte, J.C.4
  • 5
    • 0027400945 scopus 로고
    • Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I
    • Omori, K. and Komatsubara, S., Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I. J. Bacteriol., 175, 959-965 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 959-965
    • Omori, K.1    Komatsubara, S.2
  • 6
    • 0029005745 scopus 로고
    • An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus
    • Nishiyama, M., Kukimoto, M., Beppu, T., and Horinouchi, S., An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus. Microbiology, 141, 1211-1219 (1995).
    • (1995) Microbiology , vol.141 , pp. 1211-1219
    • Nishiyama, M.1    Kukimoto, M.2    Beppu, T.3    Horinouchi, S.4
  • 7
    • 0023664597 scopus 로고
    • Nucleotide sequence of the overlapping genes for the subunits of Bacillus subtilis aspartokinase II and their control regions
    • Chen, N. Y., Hu, F. M., and Paulus, H., Nucleotide sequence of the overlapping genes for the subunits of Bacillus subtilis aspartokinase II and their control regions. J. Biol. Chem., 262, 8787-8798 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 8787-8798
    • Chen, N.Y.1    Hu, F.M.2    Paulus, H.3
  • 8
    • 0025802142 scopus 로고
    • Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum
    • Kalinowski, J., Cremer, J., Bachmann, B., Eggeling, L., Sahm, H., and Puhler, A., Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. Mol. Microbiol., 5, 1197-1204 (1991).
    • (1991) Mol. Microbiol. , vol.5 , pp. 1197-1204
    • Kalinowski, J.1    Cremer, J.2    Bachmann, B.3    Eggeling, L.4    Sahm, H.5    Puhler, A.6
  • 9
    • 0032808182 scopus 로고    scopus 로고
    • Kinetic and mutation analysis of aspartate kinase from Thermus flavus
    • Kobashi, N., Nishiyama, M., and Tanokura, T., Kinetic and mutation analysis of aspartate kinase from Thermus flavus. J. Bioscien. Bioeng., 87, 739-745 (1999).
    • (1999) J. Bioscien. Bioeng. , vol.87 , pp. 739-745
    • Kobashi, N.1    Nishiyama, M.2    Tanokura, T.3
  • 10
    • 0025165007 scopus 로고
    • Aspartokinase III, a new isozyme in Bacillus subtilis 168
    • Graves, L., M. and Switzer, R., L., Aspartokinase III, a new isozyme in Bacillus subtilis 168. J. Bacteriol., 172, 218-223 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 218-223
    • Graves, L.M.1    Switzer, R.L.2
  • 11
    • 0025014844 scopus 로고
    • Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168
    • Zhang, J. J., Hu, F. M., Chen, N. Y., and Paulus, H., Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168. J. Bacteriol., 172, 701-708 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 701-708
    • Zhang, J.J.1    Hu, F.M.2    Chen, N.Y.3    Paulus, H.4
  • 12
    • 0027309277 scopus 로고
    • Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase
    • Chen, N. Y., Jiang, S. Q., Klein, D. A., and Paulus, H., Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J. Biol. Chem., 268, 9448-9465 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 9448-9465
    • Chen, N.Y.1    Jiang, S.Q.2    Klein, D.A.3    Paulus, H.4
  • 13
    • 0027201142 scopus 로고
    • Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon
    • Follettie, M. T., Peoples, O. P., Agoropoulou, C., and Sinskey, A. J., Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon. J. Bacteriol., 175, 4096-4103 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 4096-4103
    • Follettie, M.T.1    Peoples, O.P.2    Agoropoulou, C.3    Sinskey, A.J.4
  • 14
    • 0023916543 scopus 로고
    • Mechanism of expression of the overlapping genes of Bacillus subtilis aspartokinase II
    • Chen, N.-H. and Paulus, H., Mechanism of expression of the overlapping genes of Bacillus subtilis aspartokinase II. J. Biol. Chem., 263, 9526-9532 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 9526-9532
    • Chen, N.-H.1    Paulus, H.2
  • 17
    • 0001782583 scopus 로고
    • β-aspartate kinase and β-aspartyl phosphate
    • Black, S. and Wright, N. G., β-aspartate kinase and β-aspartyl phosphate. J. Biol. Chem., 213, 27-38 (1954).
    • (1954) J. Biol. Chem. , vol.213 , pp. 27-38
    • Black, S.1    Wright, N.G.2
  • 18
    • 0014529535 scopus 로고
    • Concerted inhibition and its reversal by end products of aspartate kinase in Brevibacterium flavum
    • Shiio, I. and Miyajima, R., Concerted inhibition and its reversal by end products of aspartate kinase in Brevibacterium flavum. J. Biochem., 65, 849-859 (1969).
    • (1969) J. Biochem. , vol.65 , pp. 849-859
    • Shiio, I.1    Miyajima, R.2
  • 19
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W., Statistical analysis of enzyme kinetic data. Methods Enzymol., 63, 103-138 (1979).
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 20
    • 0025043652 scopus 로고
    • The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli
    • Angeles, T. S. and Viola, R. E., The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli. Arch. Biochem. Biophys., 283, 96-101 (1990).
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 96-101
    • Angeles, T.S.1    Viola, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.