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Methionine threonine plus lysine

The pathway of biosynthesis of L-lysine and L-threonine in Corynebacterium glutamicum is shown in Fig. 1. The first step, the formation of phosphoaspartate from aspartate, is catalyzed by aspertokinase and this enzyme is susceptible to the concerted feedback inhibition by L-lysine and L-threonine. The auxotrophic mutant of homoserine (or threonine plus methionine), lacking homoserine dehydrogenase, was constructed and found to produce L-lysine in the culture medium. Second, the mutants which show the threonine or methionine sensitive phenotype caused by the mutation on homoserine dehydrogenase (low activity) was also found to produce appreciable amounts of L-lysine in the culture medium. Furthermore, a lysine analogue (S-aminoethylcysteine) resistant mutant was obtained as an L-lysine producer and in this strain aspartokinase was insensitive to the feedback inhibition. [Pg.75]

Figure 2, The biosynthesis of lysine, methionine, threonine, and isoleucine in E. coli and S. marcescens. Solid arrows, steps catalyzed by enzymes repressed by lysine. Broken arrows, steps catalyzed by enzymes repressed by methionine. Open arrows, steps catalyzed by enzymes repressed by threonine plus isoleucine. Open, dashed arrows, steps catalyzed by enzymes controlled as described in Figure 1. Structural genes indicated in italics. Dashed lines indicate reactions controlled by endproduct inhibition. Reproduced, with permission, from Ref. 57. Copyright 1975, American... Figure 2, The biosynthesis of lysine, methionine, threonine, and isoleucine in E. coli and S. marcescens. Solid arrows, steps catalyzed by enzymes repressed by lysine. Broken arrows, steps catalyzed by enzymes repressed by methionine. Open arrows, steps catalyzed by enzymes repressed by threonine plus isoleucine. Open, dashed arrows, steps catalyzed by enzymes controlled as described in Figure 1. Structural genes indicated in italics. Dashed lines indicate reactions controlled by endproduct inhibition. Reproduced, with permission, from Ref. 57. Copyright 1975, American...
Pea.nuts, The proteins of peanuts are low in lysine, threonine, cystine plus methionine, and tryptophan when compared to the amino acid requirements for children but meet the requirements for adults (see Table 3). Peanut flour can be used to increase the nutritive value of cereals such as cornmeal but further improvement is noted by the addition of lysine (71). The trypsin inhibitor content of raw peanuts is about one-fifth that of raw soybeans, but this concentration is sufficient to cause hypertrophy (enlargement) of the pancreas in rats. The inhibitors of peanuts are largely inactivated by moist heat treatment (48). As for cottonseed, peanuts are prone to contamination by aflatoxin. FDA regulations limit aflatoxin levels of peanuts and meals to 100 ppb for breeding beef catde, breeding swine, or poultry 200 ppb for finishing swine 300 ppb for finishing beef catde 20 ppb for immature animals and dairy animals and 20 ppb for humans. [Pg.301]

Lysine plus threonine severely inhibits growth of maize in a synergistic manner. Growth inhibition could result from combined effects of lysine on aspartate kinase and threonine on homoserine dehydrogenase, resulting in starvation for methionine. Growth inhibition by lysine -i- threonine can be overcome by supplying methionine. Bryan [1980) Miflin [1977). [Pg.442]


See other pages where Methionine threonine plus lysine is mentioned: [Pg.122]    [Pg.957]    [Pg.348]    [Pg.236]    [Pg.622]    [Pg.442]    [Pg.444]    [Pg.44]    [Pg.358]   
See also in sourсe #XX -- [ Pg.485 , Pg.486 ]




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