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Tryptophan regulation

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]

Certain amino acids and their derivatives, although not found in proteins, nonetheless are biochemically important. A few of the more notable examples are shown in Figure 4.5. y-Aminobutyric acid, or GABA, is produced by the decarboxylation of glutamic acid and is a potent neurotransmitter. Histamine, which is synthesized by decarboxylation of histidine, and serotonin, which is derived from tryptophan, similarly function as neurotransmitters and regulators. /3-Alanine is found in nature in the peptides carnosine and anserine and is a component of pantothenic acid (a vitamin), which is a part of coenzyme A. Epinephrine (also known as adrenaline), derived from tyrosine, is an important hormone. Penicillamine is a constituent of the penicillin antibiotics. Ornithine, betaine, homocysteine, and homoserine are important metabolic intermediates. Citrulline is the immediate precursor of arginine. [Pg.87]

TABLE 23-3 Examples of proteins regulated by phosphorylation Enzymes involved in neurotransmitter biosynthesis Tyrosine hydroxylase Tryptophan hydroxylase Neurotransmitter receptors Adrenergic receptors Dopamine receptors Opioid receptors Glutamate receptors Many others... [Pg.401]

B. and Willson, T.M. (2003) X-ray crystal structure of the liver X receptor (> ligand binding domain regulation by a histidine-tryptophan switch. The Journal of Biological Chemistry, 278, 27138-27143. [Pg.337]

The Lac operon is but one example of the genetic adaptations which allow bacteria to respond to their environment. Other examples are to be found in amino acid metabolism, for example the TRP operon which regulates tryptophan metabolism. [Pg.71]

In summary, regulation through tryptophan catabolism appears to be an essential component of host responses to fungi such that its manipulation may allow fungi to either evade or promote immune activation. [Pg.135]


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