Protein physiological role

Physiological Role of Citric Acid. Citric acid occurs ia the terminal oxidative metabolic system of virtually all organisms. This oxidative metabohc system (Fig. 2), variously called the Krebs cycle (for its discoverer, H. A. Krebs), the tricarboxyUc acid cycle, or the citric acid cycle, is a metaboHc cycle involving the conversion of carbohydrates, fats, or proteins to carbon dioxide and water. This cycle releases energy necessary for an organism s growth, movement, luminescence, chemosynthesis, and reproduction. The cycle also provides the carbon-containing materials from which cells synthesize amino acids and fats. Many yeasts, molds, and bacteria conduct the citric acid cycle, and can be selected for thek abiUty to maximize citric acid production in the process. This is the basis for the efficient commercial fermentation processes used today to produce citric acid. 

The tissue-specific patterns of expression of the PPAR. isotypes suggested that these proteins have distinct physiological roles, and this was further supported when each was specifically disrupted in mouse gene knockout models. 

The most important physiological role of CODH in the metabolism of acetogenic bacteria was unknown until 1985, when it was shown that the enzyme is bifunctional and has acetyl-CoA synthase activity (121). It was previously thought that acetyl-CoA was synthesized at the cobalt center of a vitamin-Bi2-containing protein. In the same paper, it was proposed that nickel is the active site of CO oxidation and acetyl-CoA synthesis. 

For future research in this field, in addition to physiological and biochemical approaches, genetic analysis will be essential in the establishment of causal relationships between the induction of a stress protein and the establishment of tolerance to the stress condition. In most cases it is not difficult to detect the induction of new proteins during stress. However, the induction of new proteins does not necessarily establish stress tolerance it may well be the consequence of damage caused by stress conditions. Thus, genetic mutants will be necessary to test the physiological role of a stress protein. 

The functions of a large proportion of the proteins encoded by the human genome are presently unknown. Recent advances in bioinformatics permit researchers to compare amino acid sequences to discover clues to potential properties, physiologic roles, and mechanisms of action of proteins. Algorithms exploit the tendency of nature to employ variations of a structural theme to perform similar functions in several proteins (eg, the Rossmarm nucleotide binding fold to bind NAD(P)H,... 

Premont RT, Gainetdinov RR (2007) Physiological roles of G protein-coupled receptor kinases and arrestins. Annu Rev Physiol 69 511-534... 

LOXs are normally present in the seeds of plants, although LOXs do not have a clear physiological role in seed development, because no negative effects on crop performance were observed in LOX-deficient seeds as compared with a normal line. For this reason, the possible function of seed LOXs as storage proteins is considered. 

The 5-HT4, 5-hts and 5-HT7 receptors are coupled to the stimulation of adenylyl cyclase. 5-HT4, 5-htg and 5-HT7 receptors preferentially couple to the stimulation of adenylyl cyclase, increasing cAMP formation, via the Gs family of G proteins (see Chs 19 and 21). These receptors, however, share only >35% overall sequence homology. For this reason, they are classified as distinct receptor groups or classes and not subtypes of a family. The grouping of these receptors together is considered to be somewhat arbitrary and may be modified in the future. A lower-case appellation is used for the 5-ht6 receptor because a physiological role for these receptors in intact tissue has not been found [28]. 

Multiple physiological roles for IP6 and the diphosphoinositol polyphosphates have been proposed, including effects on endocytosis and mRNA transport [3] however, definitive evidence for many of these functions is lacking. Such studies are complicated by possible nonspecific effects of this highly negatively charged molecule. Of note is the report of an IP6/IP7-dependent protein kinase activity that phosphorylates pacsin/syndapin I, a protein involved in synaptic vesicle recycling [21]. 

---