Enzyme translocation effects

The mutation of ThrlSl, Glyl82, or Glul83 to alanine, or of Glul83 to glutamine also completely inhibited the ATP or acetylphosphate-dependent Ca transport, without effect on the phosphorylation of the enzyme by ATP in the presence of Ca or by Pi in the absence of Ca [127]. The phosphoenzyme formed from ATP retained its ADP-sensitivity at low concentration and alkaline pH, but its rate of decomposition was much slower than that of the wild-type enzyme in the presence of EGTA. These observations implicate the 181-183 region in the conformational changes related to Ca translocation. 

Farkade VD, Harrison STL, Pandit AB (2005) Heat induced translocation of proteins and enzymes within the cells an effective way to optimize the microbial cell disruption process. Biochem Eng J 23 247-257... 

All isoforms of PKC are predominantly localized to the cytosol and, upon activation, undergo translocation to either plasma or nuclear membranes. However, newly synthesized PKCs are localized to the plasmalemma and are in an open conformation in which the auto inhibitory pseudosubstrate sequence is removed from the substrate binding domain. The maturation of PKC isoforms is effected by phosphoinositide-dependentkinase-I (PDK-I), which phosphorylates a conserved threonine residue in the activation loop of the catalytic (C4) domain [24]. This in turn permits the autophosphorylation of C-terminus threonine and serine residues in PKC, a step which is a prerequisite for catalytic activity (see also Chs 22 and 23). The phosphorylated enzyme is then released into the cytosol, where it is maintained in an inactive conformation by the bound pseudosubstrate. It was originally thought that 3-phosphoinositides such as PI(3,4)P2 and PI(3,4,5)P3 could directly activate PKCs. However, it now seems more likely that these lipids serve to activate PDK-1 (a frequent contaminant of PKC preparations). 

To date, there have only been a limited number of studies directly examining PKC in bipolar disorders [77], Although undoubtedly an oversimplification, particulate (membrane) PKC is sometimes viewed as the more active form of PKC, and thus an examination of the subcellular partitioning of this enzyme can be used as an index of the degree of activation. Friedman etal. [78] investigated PKC activity and PKC translocation in response to serotonin in platelets obtained from bipolar-disorder patients before and during lithium treatment. They reported that the ratios of platelet-membrane-bound to cytosolic PKC activities were elevated in the manic patients. In addition, serotonin-elicited platelet PKC translocation was found to be enhanced in those patients. With respect to brain tissue, Wang and Friedman [74] measured PKC isozyme levels, activity and translocation in postmortem brain tissue from patients with bipolar disorder, and reported increased PKC activity and translocation in the brains of bipolar patients compared with controls, effects which were accompanied by elevated levels of selected PKC isozymes in cortices of bipolar disorder patients. 

Yarbrough, J. M., Rake, J. B., and Eagon, R. G. (1980). Bacterial inhibitory effects of nitrite Inhibition of active transport, but not of group translocation, and of intracellular enzymes. Appl. Environ. Microbiol. 39, 831-834. 

Many of the same conclusions may be drawn from results with synthetic auxins as from indole-3-acetic acid water intake increased, there was a lessening of the downward translocation of photosynthate with temporary increases of soluble carbohydrates in the leaves, and alterations appeared in the metabolic ratq and direction and in enzyme activity. However, the direct site of action is not known, and many of the effects are puzzling. n-Fructose oligosaccharides in artichoke and chicory storage-tissue were diminished by 70% (calculated on the content of dry matter) in 6 days... 

Alexander"2 has tried to assess the effect of indole-3-acetic acid, (2,4-dichlorophenoxy) acetic acid, and maleic hydrazide on the soluble carbohydrates and enzyme systems in sugarcane leaves. All of the chemical treatments increased sucrose, total reducing value, D-fructose, and D-glucose in leaves (compared with the controls), with a maximum at nine days after applying about two g. per plant. The indole auxin increased sucrose most, followed by the phenoxy compound and the hydrazide D-glucose increased in the reverse order. Poor translocation from the leaves may have caused the temporary increase in leaf photosynthate. Alterations in the enzyme activities as a result of the chemical treatment are difficult to interpret, partly since so little is known about their relative importance, and partly because the activity in the controls varied by as much as 100% from one sampling period to the next. 

Extensive studies have been carried out on the proton-translocating ATPase of mitochondrial, bacterial and chloroplast membranes. This enzyme can also function in reverse to exploit the electrochemical potential of protons built up by respiration for the synthesis of ATP from ADP and P .298 The synthesis of ATP can be effected by the application of external electrical pulses to the ATPase vesicles in suspension with submitochondrial particles, showing that the diffusion potential of the protons (ApH) is not used. The yield of ATP was linearly dependent on the number of pulses.299... 

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