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Alanine accumulation

If alanine accumulates in muscle, it acts as an allosteric inhibitor of pyruvate kinase, so reducing the rate at which pyruvate is formed. This end-product inhibition of pyruvate kinase by alanine is over-ridden by high concentrations of fructose bisphosphate, which acts as a feed-forward activator of pyruvate kinase. ATP is an inhibitor of pyruvate kinase, and at high concentrations acts to inhibit the enzyme. More importantly, ATP acts as an allosteric inhibitor of phosphofructokinase (section 10.2.2.1). This means that, under conditions in which the supply of ATP (which can be regarded as the end-product of all energy-yielding metabolic pathways) is more than adequate to meet requirements, the metabolism of glucose is inhibited. [Pg.309]

Evidence accumulating from various laboratories has clearly demonstrated that lithium, at therapeutically relevant concentrations, exerts significant effects on the PKC signaling cascade. Current data suggest that chronic lithium attenuates PKC activity, and down-regulates the expression of PKC isozymes V in the frontal cortex and hippocampus [79, 80], Chronic lithium has also been demonstrated to dramatically reduce the hippocampal levels of a major PKC substrate, myristoylated-alanine-rich C kinase substrate (MARCKS), which has been implicated in regulating long-term neuroplastic events. [Pg.897]

N-Carbobenzoxy-L-alanine-/>-nitrophenyl ester is a specific substrate for elastase in which the rate-limiting step is deacylation, that is, hydrolysis of the acyl-enzyme intermediate. In 70% methanol over a reasonable temperature range the energy of activation of the turnover reaction, that is, deacylation, is 15.4 kcal mol. In the pH 6-7 region in this cryoprotective solvent, the turnover reacdon can be made negligibly slow at temperatures of -50 C or below. Under such conditions/i-nitro-phenol is released concurrent to acyl enzyme formation in a 1 1 stoichiometry with active enzyme in the presence of excess substrate. In other words, even at low temperatures, the acylation rate is much faster than deacylation and the acyl enzyme will accumulate on the enzyme. The rate of acyl-enzyme formation can be monitored by following the rate of p-nitrophenol release, and thus the concentration of trapped acyl enzyme may be determined. This calculadon has been carried out and... [Pg.256]

Between meals when fatty acids are oxidized in the liver for energy, accumulating acetyl CoA activates pyruvate carboxylase and gluconeogenesis and inhibits PDH, thus preventing conversion of lactate and alanine to acetyl CoA. [Pg.198]

Storage conditions and preservation treatments also can affect the free amino acid content. Some authors [242] reported changes in the concentration of free amino acids of broccoli florets stored in air or in controlled atmospheres. Arginine concentration varied greatly during air storage, while y-amino butyric acid, alanine and an unidentified amino acid accumulated in response to low O2 and/or high CO2 treatment. [Pg.589]

Most of the amino acids are consumed by insect cells, with the exception of alanine which is produced however, it has been reported that alanine overflow metabolism is energetically wasteful as it is with mammalian cells [63]. The alanine production by insect cells has been interpreted as a strategy to avoid the accumulation of toxic ammonia produced from amino acid catabolism [64]. [Pg.194]

Absorption bands at 500 nm. With many PLP enzymes certain substrates and inhibitors cause the appearance of intense and unusually narrow bands at 500 nm. Such a band is observed with aspartate aminotransferases acting on eryf/zro-3-hydroxyaspartate (Fig. 14-9). This substrate undergoes transamination very slowly, and the 500-nm absorbing form which accumulates is probably an intermediate in the normal reaction sequence. A similar spectrum is produced by tryptophan indole-lyase acting on the competitive inhibitor L-alanine. Under the same conditions the... [Pg.750]

Halorhodopsiti. In addition to bacteriorhodopsin there are three other retinal-containing proteins in membranes of halobacteria. From mutant strains lacking bacteriorhodopsin the second protein, halorhodopsin, has been isolated. It acts as a light-driven chloride ion pump, transporting Cl from outside to inside. Potassium ions follow, and the pump provides a means for these bacteria to accumulate KC1 to balance the high external osmotic pressure of the environment in which they live.578 The amino acid sequences of halorhodopsins from several species are very similar to those of bacteriorhodopsin as is the three-dimensional structure.589 However, the important proton-carrying residues D85 and D96 of bacteriorhodopsin are replaced by threonine and alanine, respectively, in halorhodopsin.590 Halorhodopsin (hR)... [Pg.1335]

Genetic techniques have been used to improve the ability of microorganisms to accumulate amino acids. Several amino acids are manufactured from their direct precursors by the use of microhially produced enzymes. For example, bacterial L-asparlale -carboxylase is used for the production of L-alanine from L-aspartic add. [Pg.80]


See other pages where Alanine accumulation is mentioned: [Pg.125]    [Pg.131]    [Pg.102]    [Pg.108]    [Pg.37]    [Pg.125]    [Pg.131]    [Pg.102]    [Pg.108]    [Pg.37]    [Pg.180]    [Pg.45]    [Pg.234]    [Pg.199]    [Pg.75]    [Pg.366]    [Pg.188]    [Pg.357]    [Pg.268]    [Pg.206]    [Pg.227]    [Pg.163]    [Pg.22]    [Pg.82]    [Pg.5]    [Pg.182]    [Pg.173]    [Pg.41]    [Pg.274]    [Pg.32]    [Pg.62]    [Pg.68]    [Pg.281]    [Pg.580]    [Pg.191]    [Pg.295]    [Pg.1370]    [Pg.1398]    [Pg.1808]    [Pg.1814]    [Pg.87]    [Pg.571]    [Pg.869]    [Pg.16]   


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