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Threonine essentiality

An attractive and useful method for the preparation of aziridine-2-carboxylic esters makes use of the readily available amino acids serine and threonine. Essentially, this synthesis involves the ring closure of 1,2-amino alcohols. [Pg.97]

See also - Table 5.1, Genetic Code, Glutathione, Metabolism of Serine, Glycine, and Threonine, Essential Amino Acids, Titration Curve of Glycine... [Pg.55]

See also Metabolism of Serine, Glycine, and Threonine, Essential Amino Acids... [Pg.525]

Because of the simplicity of swiae and poultry feeds, most feed manufacturers add vitamins (qv) and trace minerals to ensure an adequate supply of essential nutrients. Amino acids (qv) such as methionine [7005-18-7] lysiae [56-87-17, threonine [36676-50-3] and tryptophan [6912-86-3], produced by chemical synthesis or by fermentation (qv), are used to fortify swiae and poultry diets. The use of these supplements to provide the essential amino acids permits diets with lower total cmde proteia coateat. [Pg.141]

The nutritional value of a proteia can be improved by the addition of amino acids of low abundance ia that proteia. Thus the fortification of plant proteias such as wheat, com, and soybean with L-lysiae, DL-methionine, or other essential amino acids (L-tryptophan and L-threonine) is expected to alleviate some food problems (11). Such fortification has been widespread ia the feedstuff of domestic animals. [Pg.271]

Cottonseed. When compared with FAO/WHO/UNU essential amino acid requirements (see Table 3), cottonseed proteins are low in lysine, threonine, and leucine for 2 to 5-year-old children, yet meet all requirements for adults. [Pg.301]

Sundower Seed. Compared to the FAO/WHO/UNU recommendations for essential amino acids, sunflower proteins are low in lysine, leucine, and threonine for 2 to 5-year-olds but meet all the requirements for adults (see Table 3). There are no principal antinutritional factors known to exist in raw sunflower seed (35). However, moist heat treatment increases the growth rate of rats, thereby suggesting the presence of heat-sensitive material responsible for growth inhibitions in raw meal (72). Oxidation of chlorogenic acid may involve reaction with the S-amino group of lysine, thus further reducing the amount of available lysine. [Pg.301]

PHOSPHOPROTEINS. These proteins have phosphate groups esterified to the hydroxyls of serine, threonine, or tyrosine residues. Casein, the major protein of milk, contains many phosphates and serves to bring essential phosphorus to the growing infant. Many key steps in metabolism are regulated between states of activity or inactivity, depending on the presence or absence of phosphate groups on proteins, as we shall see in Chapter 15. Glycogen phospho-rylase a is one well-studied example. [Pg.126]

Note carefully the difference between enantiomers and diastereomers. Enantiomers have opposite configurations at all chirality centers, whereas diastereomers have opposite configurations at some (one or more) chirality centers but the same configuration at others. A full description of the four stereoisomers of threonine is given in Table 9.2. Of the four, only the 2S,3R isomer, [o]D= -28.3, occurs naturally in plants and animals and is an essential human nutrient. This result is typical most biological molecules are chiral, and usually only one stereoisomer is found in nature. [Pg.303]

Not all proteins are nutritionally equivalent. Mote of some than of others is needed to maintain nittogen balance because different proteins contain different amounts of the various amino acids. The body s requirement is for specific amino acids in the correct proportions to replace the body proteins. The amino acids can be divided into two groups essential and nonessential. There are nine essential or indispensable amino acids, which cannot be synthesized in the body histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. If one of these is lacking or inadequate, then—regardless of the total intake of protein—it will not be possible to maintain nitrogen balance since there will not be enough of that amino acid for protein synthesis. [Pg.480]

The carboxy terminus of the ft receptor was essential for agonist-induced desensitization [83, 132] since truncation of the receptor prevented desensitization. Like those findings with the k receptor, the enzyme G protein receptor kinase (GRK) appears to be involved in the desensitization process, since blockade of GRK prevented the desensitization process. Wang [132] has proposed that GRK catalyzes the phosphorylation of a series of serine/threonine residues in the C-terminus of the fi receptor to desensitize the receptor. [Pg.479]

The mitogen-activated protein kinase cascade is second-messenger-independent. Although the second-messenger-dependent protein kinases were identified first as playing an important role in neuronal function, we now know that many other types of protein serine-threonine kinase are also essential (Table 23-1). Indeed, one of the most critical discoveries of the 1990s was the delineation of the mitogen-activated protein kinase (MAP kinase or MAPK) cascades. [Pg.396]

Characteristically, legume seeds are rich in protein and contain intermediate to high levels of lysine and threonine which are important in balancing the deficiencies of these essential amino acids in cereal diets. Certain legume proteins, such as soybean, also exhibit strong functional properties, especially water solubility, water and fat binding and emulsification. Thus soybean flours, protein concentrates and isolates have been used widely as nutritional supplements and functional ingredients in foods. [Pg.179]

The complete identification of the amino acids which are essential in the diet is due to W.C. Rose (1938). His first attempts to replace casein with its constituents were unsuccessful because an essential amino acid component in the protein hydrolysate had been missed. After threonine had been isolated by him from casein and fibrin, and shown to be essential, Rose identified val, met, his, lys, phe, leu, ile, thr, and arg as... [Pg.24]

In Saccharomyces cerevisiae, multiple histone H2A phosphorylation sites have been characterized (Serine 122, Serine 129, Threonine 126) (Wyatt et al, 2003 Harvey et al, 2005 Redon et al, 2006). Histone H2A (S129) is essential for DNA double-strand-break responses (see Section 4) and histone H2A (SI22) is important for survival in the presence of DNA damage (Harvey et al, 2005) (Fig. 2). [Pg.323]


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See also in sourсe #XX -- [ Pg.285 ]




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