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Aspartate kinase

Aspartate kinase [EC 2.T.2.4], also known as asparto-kinase, catalyzes the reaction of aspartate with ATP to produce 4-phosphoaspartate and ADP. The enzyme isolated from E. coli is a multifunctional protein, also exhibiting the ability to catalyze the reaction of homoserine with NAD(P) to produce aspartate 4-semialdehyde and NAD(P)H (that is, the activity of homoserine dehydrogenase, EC 1.1.1.3). [Pg.69]

ASPARTYLCLUCOSAMINIDASE ASPARTATE AMINOTRANSFERASE ASPARTATE AMMONIA-LYASE ASPARTATE CARBAMOYLTRANSFERASE ASPARTATE a-DECARBOXYLASE ASPARTATE /3-DECARBOXYLASE ASPARTATE KINASE d-ASPARTATE OXIDASE ASPARTATE RACEMASE... [Pg.724]

CYSTATHIONINE y-LYASE HOMOSERINE DEHYDROGENASE ASPARTATE KINASE HOMOSERINE SUCCINYLTRANSFERASE HomotopIc,... [Pg.749]

LT-aspartokinase <10> (<10> lysine-threonine-sensitive isoenzyme [3]) [3] aspartate kinase (phosphorylating) aspartate kinase III <11> [33] aspartic kinase... [Pg.314]

Shewry, P.R. Miflin, B.J. Properties and regulation of aspartate kinase from barley seedlings (Hordeum vulgare L.). Plant Physiol., 59, 69-73 (1977)... [Pg.330]

Kochhar, S. Kochhar, V.K. Sane, P.V. Isolation, characterization and regulation of isoenzymes of aspartate kinase differentially sensitive to calmodulin from spinach leaves. Biochim. Biophys. Acta, 880, 220-225 (1986)... [Pg.331]

Relton, J.M. Bonner, P.L.R. Wallsgrove, R.M. Lea, P.J. Physical and kinetic properties of lysine-sensitive aspartate kinase purified from carrot cell suspension culture. Biochim. Biophys. Acta, 953, 48-60 (1988)... [Pg.331]

Dotson, S.B. Somers, D.A. Gengenbach, B.G. Purification and characterization of lysine-sensitive aspartate kinase from maize cell cultures. Plant Physiol., 91, 1602-1608 (1989)... [Pg.331]

Azevedo, R.A. Smith, R.J. Lea, P.J. Aspartate kinase regulation in maize Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. Phytochemistry, 31, 3731-3734 (1992)... [Pg.331]

Heremans, B. Jacobs, M. A mutant of Arabidopsis thaliana (L.) Heynh. with modified control of aspartate kinase by threonine. Biochem. Genet., 35, 139-153 (1997)... [Pg.331]

Arevalo-Rodriguez, M. Calderon, I.L. Holmberg, S. Mutations that cause threonine sensitivity identify catalytic and regulatory regions of the aspartate kinase of Saccharomyces cerevisiae. Yeast, 15, 1331-1345 (1999)... [Pg.331]

Kobashi, N. Nishiyama, M. Tanokura, M. Kinetic and mutation analyses of aspartate kinase from Thermus flavus. J. Biosci. Bioeng., 87, 739-745 (1999)... [Pg.331]

Lugli, J. Gaziola, S.A. Azevedo, R.A. Effects of calcium, S-adenosylmethio-nine, S-(2-aminoethyl)-L-cysteine, methionine, valine and salt concentration on rice aspartate kinase isoenzymes. Plant Sci., 150, 51-58 (2000)... [Pg.331]

Kobashi, N. Nishiyama, M. Yamane, H. Characterization of aspartate kinase III of Bacillus subtilis. Biosci. Biotechnol. Biochem., 65, 1391-1394 (2001)... [Pg.332]

Paris, S. Wessel, P.M. Dumas, R. Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana. Protein Expr. Purif., 24, 105-110 (2002)... [Pg.332]

Paris, S. Viemon, C. Curien, G. Dumas, R. Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine. J. Biol. Chem., 278, 5361-5366 (2003)... [Pg.332]

Nomura et al. (1987a) attempted to minimize product inhibitory effect on the aspartate kinase step in lysine biosynthesis and enhance L-lysine production from Brevibacterium Jlavum QL-5 using a combined ED-F system. However, lysine production was not statistically different from that obtained in diffusion dialysis fermentation and about 20% greater than that achieved during conventional fermentation, thus making practically ineffective such a use of ED. [Pg.340]

The L-threonine biosynthetic pathway consists of five enzymatic steps from L-aspartate. E. coli has three aspartate kinase isoenzymes, key enzymes which catalyze the first reaction of the L-threonine biosynthetic pathway. The aspartate kinase isoenzymes I, II, and III encoded by the thrA, metL, and lysC genes, respectively, are affected by feedback inhibition by L-threonine, L-methionine, and L-lysine, respectively. C. glutamicum has only one aspartate kinase encoded by the lysC gene, which is subjected to feedback inhibition by L-lysine and... [Pg.7]

See other pages where Aspartate kinase is mentioned: [Pg.424]    [Pg.69]    [Pg.725]    [Pg.314]    [Pg.314]    [Pg.315]    [Pg.316]    [Pg.316]    [Pg.317]    [Pg.318]    [Pg.319]    [Pg.320]    [Pg.321]    [Pg.322]    [Pg.323]    [Pg.324]    [Pg.325]    [Pg.326]    [Pg.327]    [Pg.327]    [Pg.327]    [Pg.328]    [Pg.329]    [Pg.330]    [Pg.331]    [Pg.331]    [Pg.332]    [Pg.330]    [Pg.331]   
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See also in sourсe #XX -- [ Pg.1143 , Pg.1144 ]

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See also in sourсe #XX -- [ Pg.151 ]

See also in sourсe #XX -- [ Pg.68 ]



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