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Homoserine kinase

As mentioned earlier, L-threonine production can be enhanced by engineering the export or uptake system. An efficient L-threonine producer strain of E. coli KY10935, which was derived from the wild-type strain by multiple rounds of random mutation and selection, was able to produce 100 g L-1 L-threonine after 77 h cultivation [53]. In this strain, the two key enzymes in the L-threonine biosynthesis (homoserine dehydrogenase and homoserine kinase) were identified to be still inhibited by much lower intracellular concentrations of L-threonine than... [Pg.11]

A more direct y replacement of the hydroxyl of homocysteine or 0-phosphohomoserine by a sulfide ion has also been reported for both Neurospora and green plants.Methylation of homocysteine to methionine (Fig. 24-13) has been considered previously, as has the conversion of homoserine to threonine by homoserine kinase and the PLP-dependent threonine synthase (p. 746, Fig. i4-7).254-255a standard PLP-requiring P elimination converts threonine to 2-oxobutyrate, a precursor to isoleucine (Fig. 24-13). ... [Pg.470]

R234C <4> (<4>, no observable homoserine kinase activity, the ATPase activity is nearly 20times that of the wild-type enzyme at pH 8.0. 7fold increase... [Pg.30]

Aarnes, H. Homoserine kinase from barley seedlings. Plant Sci. Lett., 7, 187-194 (1976)... [Pg.31]

Baum, H.J. Madison, J.T. Thompson, J.E Feedback inhibition of homoserine kinase from radish leaves. Phytochemistry, 22, 2409-2412 (1983)... [Pg.31]

Shames, S.L. Wedler, RC. Homoserine kinase of Escherichia coli kinetic mechanism and inhibition by L-aspartate semialdehyde. Arch. Biochem. Biophys., 235, 359-370 (1984)... [Pg.31]

Finkelnburg, B. Klemme, J.H. Homoserine kinase from phototrophic bacterium RhodospirUlum rubrum is not sensitive to feedback inhibition by l-Thr. FEMS Microbiol. Lett., 48, 93-96 (1987)... [Pg.32]

Theze, J. Kleidman, L. Saint Girons, L Homoserine kinase from Escherichia coli K-12 properties, inhibition by L-threonine, and regulation of biosynthesis. J. Bacteriol., 118, 577-581 (1974)... [Pg.32]

Miyajima, R. Shiio, I. Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. V. Properties of homoserine kinase. J. Bio-chem., 71, 219-226 (1972)... [Pg.32]

Riesmeier, J. Klonus, A.-K. Pohlenz, H.-D. Purification to homogeneity and characterization of homoserine kinase from wheat germ. Phytochemistry, 32, 581-584 (1993)... [Pg.32]

Ramos, C. Delgado, M.A. Calderon, I.L. Inhibition by different amino acids of the aspartate kinase and the homoserine kinase of the yeast Sac-charomyces cerevisiae. FEBS Lett., 278, 123-126 (1991)... [Pg.32]

Mannhaupt, G. Pohlenz, H.D. Seefluth, A.K. Pilz, U. Feldmann, H. Yeast homoserine kinase. Characteristics of the corresponding gene, THRl, and the purified enzyme, and evolutionary relationships with other enzymes of threonine metabolism. Eur. J. Biochem., 191, 115-122 (1990)... [Pg.32]

Burr, B. Walker, J. Truffa-Bachi, R Cohen, G.N. Homoserine kinase from Escherichia coli K12. Eur. J. Biochem., 62, 519-526 (1976)... [Pg.32]

Huo, X. Viola, R.E. Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli. Biochemistry, 35, 16180-16185 (1996)... [Pg.32]

Lee, M. Leustek, T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys., 372, 135-142 (1999)... [Pg.32]

Zhou, T. Daugherty, M. Grishin, N.V Osterman, A.L. Zhang, H. Structure and mechanism of homoserine kinase prototype for the GHMP kinase superfamily. Structure Fold Des., 8, 1247-1257 (2000)... [Pg.32]

Krishna, S.S. Zhou, T. Daugherty, M. Osterman, A. Zhang, H. Structural basis for the catalysis and substrate specificity of homoserine kinase. Biochemistry, 40, 10810-10818 (2001)... [Pg.32]

Patte, J.C. Clepet, C. Bally, M. Borne, R Mejean, V Foglino, M. ThrH, a homoserine kinase isozyme with in vivo phosphoserine phosphatase activity in Pseudomonas aeruginosa. Microbiology, 145, 845-853 (1999)... [Pg.32]

CQGG13 6 Aspart-ate-semialdeliyde dehydrogenase COGG46G Homoserine dehydrogenase CQGGG83 Homoserine kinase CQGG 98 Threonine synthase... [Pg.371]

Biosynthesis Thr belongs biogenetically to the Asp group and is formed from Asp. The direct precursor is L- homoserine, which also forms Met via cystathionine and homocysteine. Homoserine is first converted to 0-phosphohomoserine by ATP under the action of homoserine kinase (EC 2.7.1.39) and then by threonine synthase (EC 4.2.99.2) to Thr. Thr is a component of glycoproteins. It frequently occurs in the free form, see also L-serine. [Pg.650]

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