Literature DB >> 2165481

Desensitization of Bacillus subtilis aspartokinase I to allosteric inhibition by meso-diaminopimelate allows aspartokinase I to function in amino acid biosynthesis during exponential growth.

J J Zhang1, H Paulus.   

Abstract

Strains of Bacillus subtilis deficient in aspartokinases II and III are unable to grow in the absence of lysine, methionine, and threonine, although they have normal levels of aspartokinase I (J.J. Zhang, F.M. Hu, N.Y. Chen, and H. Paulus, J. Bacteriol. 172:701-708, 1990). Revertants with the ability to grow in the absence of lysine and methionine had an altered aspartokinase I, which was insensitive to feedback inhibition by meso-diaminopimelate. This suggests that inhibition by meso-diaminopimelate limits the ability of aspartokinase I to function in amino acid biosynthesis.

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Year:  1990        PMID: 2165481      PMCID: PMC213305          DOI: 10.1128/jb.172.8.4690-4693.1990

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  7 in total

1.  REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS.

Authors:  C Anagnostopoulos; J Spizizen
Journal:  J Bacteriol       Date:  1961-05       Impact factor: 3.490

2.  Biosynthesis of dipicolinic acid in Bacillus subtilis.

Authors:  L A Chasin; J Szulmajster
Journal:  Biochem Biophys Res Commun       Date:  1967-12-15       Impact factor: 3.575

3.  Regulation of aspartokinase in Bacillus subtilis. The separation and properties of two isofunctional enzymes.

Authors:  A Rosner; H Paulus
Journal:  J Biol Chem       Date:  1971-05-10       Impact factor: 5.157

4.  Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine.

Authors:  A Rosner
Journal:  J Bacteriol       Date:  1975-01       Impact factor: 3.490

5.  Cloning and structure of the gene for the subunits of aspartokinase II from Bacillus subtilis.

Authors:  R P Bondaryk; H Paulus
Journal:  J Biol Chem       Date:  1985-01-10       Impact factor: 5.157

6.  Aspartokinase III, a new isozyme in Bacillus subtilis 168.

Authors:  L M Graves; R L Switzer
Journal:  J Bacteriol       Date:  1990-01       Impact factor: 3.490

7.  Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168.

Authors:  J J Zhang; F M Hu; N Y Chen; H Paulus
Journal:  J Bacteriol       Date:  1990-02       Impact factor: 3.490

  7 in total
  4 in total

Review 1.  Cohesion group approach for evolutionary analysis of aspartokinase, an enzyme that feeds a branched network of many biochemical pathways.

Authors:  Chien-Chi Lo; Carol A Bonner; Gary Xie; Mark D'Souza; Roy A Jensen
Journal:  Microbiol Mol Biol Rev       Date:  2009-12       Impact factor: 11.056

2.  Analysis and manipulation of aspartate pathway genes for L-lysine overproduction from methanol by Bacillus methanolicus.

Authors:  Ingemar Nærdal; Roman Netzer; Trond E Ellingsen; Trygve Brautaset
Journal:  Appl Environ Microbiol       Date:  2011-07-01       Impact factor: 4.792

3.  Overexpression of wild-type aspartokinase increases L-lysine production in the thermotolerant methylotrophic bacterium Bacillus methanolicus.

Authors:  Oyvind M Jakobsen; Trygve Brautaset; Kristin F Degnes; Tonje M B Heggeset; Simone Balzer; Michael C Flickinger; Svein Valla; Trond E Ellingsen
Journal:  Appl Environ Microbiol       Date:  2008-12-05       Impact factor: 4.792

4.  Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp.

Authors:  F J Schendel; M C Flickinger
Journal:  Appl Environ Microbiol       Date:  1992-09       Impact factor: 4.792

  4 in total

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