Amino acid degradation valine

The essential amino acids methionine, valine, isoleucine, and threonine are degraded to form propionyl-CoA. The conversion of propionyl CoA to succinyl CoA is common to their degradative pathways. Propionyl CoA is also generated from the oxidation of odd-chain fatty acids. 

Fatty acids with odd numbers of carbon atoms are rare in mammals, but fairly common in plants and marine organisms. Humans and animals whose diets include these food sources metabolize odd-carbon fatty acids via the /3-oxida-tion pathway. The final product of /3-oxidation in this case is the 3-carbon pro-pionyl-CoA instead of acetyl-CoA. Three specialized enzymes then carry out the reactions that convert propionyl-CoA to succinyl-CoA, a TCA cycle intermediate. (Because propionyl-CoA is a degradation product of methionine, valine, and isoleucine, this sequence of reactions is also important in amino acid catabolism, as we shall see in Chapter 26.) The pathway involves an initial carboxylation at the a-carbon of propionyl-CoA to produce D-methylmalonyl-CoA (Figure 24.19). The reaction is catalyzed by a biotin-dependent enzyme, propionyl-CoA carboxylase. The mechanism involves ATP-driven carboxylation of biotin at Nj, followed by nucleophilic attack by the a-carbanion of propi-onyl-CoA in a stereo-specific manner. 

Branched-chain amino acids are leucine, isoleucine and valine the increased concentrations are also consistent with an increased rate of degradation, as muscle protein contains a high proportion of these amino acids. The extent of the decrease in ATP concentration is even greater than in exaustive physical activity. Note the very large fall is glutamine concentration. 

Figure 9-4. Metabolism of the branched-chain amino acids. The first two reactions, transamination and oxidative decarboxylation, are catalyzed by the same enzyme in all cases. Details are provided only for isoleucine. Further metabolism of isoleucine and valine follows a common pathway to propionyl CoA. Subsequent steps in the leucine degradative pathway diverge to yield acetoacetate. An intermediate in the pathway is 3-hydroxy-3-methylglutaryl CoA (HMG-CoA), which is a precursor for cytosolic cholesterol biosynthesis.

The branched-chain amino acids (isoleucine, leucine, and valine), unlike the other amino acids, are degraded only in extrahepatic tissues. 

Degradation of amino acids most often begins with conversion, either by transamination3563 or by NAD+-dependent dehydrogenation,357 to the corresponding 2-oxoacid and oxidative decarboxylation of the latter (Fig. 15-16). Alanine, valine, leucine, and isoleucine are all treated this way in the animal body. Alanine gives pyruvate and acetyl-CoA directly, but the others yield CoA derivatives that undergo... 

Free amino acids are further catabolized into several volatile flavor compounds. However, the pathways involved are not fully known. A detailed summary of the various studies on the role of the catabolism of amino acids in cheese flavor development was published by Curtin and McSweeney (2004). Two major pathways have been suggested (1) aminotransferase or lyase activity and (2) deamination or decarboxylation. Aminotransferase activity results in the formation of a-ketoacids and glutamic acid. The a-ketoacids are further degraded to flavor compounds such as hydroxy acids, aldehydes, and carboxylic acids. a-Ketoacids from methionine, branched-chain amino acids (leucine, isoleucine, and valine), or aromatic amino acids (phenylalanine, tyrosine, and tryptophan) serve as the precursors to volatile flavor compounds (Yvon and Rijnen, 2001). Volatile sulfur compounds are primarily formed from methionine. Methanethiol, which at low concentrations, contributes to the characteristic flavor of Cheddar cheese, is formed from the catabolism of methionine (Curtin and McSweeney, 2004 Weimer et al., 1999). Furthermore, bacterial lyases also metabolize methionine to a-ketobutyrate, methanethiol, and ammonia (Tanaka et al., 1985). On catabolism by aminotransferase, aromatic amino acids yield volatile flavor compounds such as benzalde-hyde, phenylacetate, phenylethanol, phenyllactate, etc. Deamination reactions also result in a-ketoacids and ammonia, which add to the flavor of... 

The Edman degradation removes the N-terminal amino acid, which is identified as a phenylthiohy-dantoin derivative. The first Edman degradation of Val-Phe-Gly-Ala gives the phenylthiohydantoin derived from valine the second gives the phenylthiohydantoin derived from phenylalanine. 

Rohan had suggested that the operative reaction in the development of chocolate aroma might be a Strecker degradation of the amino acid fraction. Bailey et al. (8) demonstrated quantitatively that three aldehydes, which could be related to leucine, valine, and alanine, were prominent in the volatiles from a typical sample of roasted, ground cacao beans. 

Table 5.2 lists the amino acid molar ratios determined for LHCP from several plant sources, and compares these results with the mean values obtained for the main glycopeptide subfraction (peak I in Table 5.1) from microbubble surfactant. It can be seen from Table 5.2 that the amino acid composition of LHCP clearly resembles that of the main glycopeptide subfraction. Specifically, in both cases nonpolar residues represent a majority and near constant fraction (i.e., 59-62%) of the amino acid composition, with the relative amounts of such residues in practically all individual cases listed following the pattern glycine > leucine, alanine, valine, proline > isoleucine, phenylalanine > methionine, tryptophan (Table 5.2). Accordingly, the glycopeptide fraction of microbubble surfactant may represent a degradation product of the light-harvesting chlorophyll a/b-protein, which is well known (ref. 373-375) to be extremely widely distributed in terrestrial, freshwater, and salt-water environments (cf. ref. 379).

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