Glyceraldehyde-3-phosphate dehydrogenase, activity

Mazzola, J. L., Sirover, M. A. Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer s disease and in Huntington s disease fibroblasts./. Neurochem. 2001, 76 442 149. 

Rogalski-Wilk, A. A., Cohen, R. S. Glyceraldehyde-3 -phosphate dehydrogenase activity and F-actin associations in synaptosomes and postsynaptic densities of porcine cerebral cortex. Cell Mol. Neurobiol. 1997,17 51-70. 

Kim, Y.B., Lee, Y.S., Choi, D.S., Cha, S.H., Sok, D.E. (1996h). Change in glutathione S-transferase and glyceraldehyde-3-phosphate dehydrogenase activities in the organs of mice treated with 2-chloroethyl ethyl sulfide or its oxidation products. Food Chem. Toxicol. 34 259-65. 

Two new immunophilins have recently been discovered which contain both FKBP and cyclophilin domains. A 37 kDa protein isolated from the Jurkat T-cell line was found to bind FK506, rapamycin, and cyclosporin A, all with high affinity.50 FKBP37 contains two FKBP domains and one cyclophilin domain, and also possesses glyceraldehyde 3-phosphate dehydrogenase activity. The 52 kDa protein, isolated from human lymphoid cells, also binds all three immunosuppressant drugs but shows no detectable rotamase activity towards a variety of peptidic substrates.95... 

Figure 1. The rate of incorporation of carbon from Glc6P and pyruvate (ImM) into fatty acids and the rate of pyruvate (ImM) uptake by plastids isolated from embryos at three stages in development (A 1.5 mgFW, B 2.5 mgFW and C 3.5 mgFW). A unit of GAPDH (NAPH-dependent glyceraldehyde 3-phosphate dehydrogenase) activity is one />tmol min Each value is the mean SE of measurements from three separate preparations.

Since alloxan reacts with GSH to form compound 305 (26), and since GSH is a tightly bound coehzyme necessary for glyceraldehyde phosphate dehydrogenase activity (57), alloxan might well affect this enzyme step in the utilization of carbohydrate. In vitro studies using various sulfhydryl-enzyme systems have shown that alloxan, at a concentration of 0.002 M,... 

Brune and Lapetina (1989) reported that NO could activate a platelet ADP-ribosyltransferase that resulted in the ribosylation of a 39 kDa protein. Subsequent work revealed that the protein was glyceraldehyde phosphate dehydrogenase (GAP-DH), and that ribosylation was associated with reduced GAP-DH activity (Dimmeler et al., 1992). In our collaboration with Molina et al., (1992), we have shown that GAP-DH activity is dramatically inhibited in C. parvum treated rats and that this action is associated with both a ribosylation and nitro-sylation of the enzyme. Such a marked inhibition of a glycolytic enzyme could explain some of the metabolic changes observed in the liver in sepsis. 

Aside from PEPCase, a number of other CAM-related genes have been partially characterised (Table 1). These include cDNA clones for pyruvate, orthophosphate dikinase (PPDK), a specific NADP malate dehydrogenase (MDH), glyceraldehyde phosphate dehydrogenase (GaPDH) and NADP-dependent malic enzyme (MOD). Previous studies indicated that the enzymatic activities of these gene products increased upon salt stress in the ice plant (Holtum Winter, 1982). As in the case... 

Glyceraldehyde phosphate dehydrogenase probably holds the distinction of being the classic thiol enzyme in the minds of most biochemists . The thiol is believed to be involved in the initial attachment of the aldehyde substrate as a thiohemiacetal. The em me-bound thiohemiacetal is then oxidized by NAD generating an enzyme-bound thioester. In more sophisticated proposals for this mechanism the nicotinamide cofactor interacts with the active centre thiol as a charge transfer type of complex. This facilitates the reaction of the thiol with the carbonyl of the substrate. The thiol addition and the electron transfer to nicotinamide occur... 

Phosphofructokinase, the enzyme that phosphory-lates fructose-1-phosphate to yield the diphosphate, the precursor of the triose phosphates, has a fate similar to that of hexokinase, except that its prenatal activity is only three times greater than that of adult liver, and the prenatal activity drops to adult values within 9 days after birth. Fructose-1,6-diphosphate, triose-P-isomerase, and glyceraldehyde phosphate dehydrogenase all have high fetal activities that slightly increase at the adult levels in the newborn. Thus, in the fetal liver the activity of these enzymes seems to favor the formation rather than the use of lactic acid. 

The availability of thiol esters of glutathione and the possibility of their participation in the activity of enzymes such as glyceraldehyde phosphate dehydrogenase led us into an inquiry into the biological activity of the... 

The inhibitory effects of heavy metals, and of cyanide on cytochrome oxidase and of arsenate on glyceraldehyde phosphate dehydrogenase, are examples of non-competitive inhibition. This type of inhibitor acts by combining with the enzyme in such a way that for some reason the active site is rendered inoperative. The inhibition may or may not be reversible but it is not affected by the addition of extra substrate. 

As discussed in Section 22.7, illumination of chloroplasts leads to light-driven pumping of protons into the thylakoid lumen, which causes pH changes in both the stroma and the thylakoid lumen (Figure 22.27). The stromal pH rises, typically to pH 8. Because rubisco and rubisco activase are more active at pH 8, COg fixation is activated as stromal pH rises. Fructose-1,6-bisphosphatase, ribulose-5-phosphate kinase, and glyceraldehyde-3-phosphate dehydrogenase all have alkaline pH optima. Thus, their activities increase as a result of the light-induced pH increase in the stroma. 

Bloxham, D.P., and Sharma, R.P. (1979) The development of 5,5 -polymethylenebis(methanethiosulfona tes) as reversible cross-linking reagent for thiol groups and their use to form stable catalytically active cross-linked dimers with glyceraldehyde-3-phosphate dehydrogenase. Biochem. J. 181, 355. 

Figure 6.3 Multienzymatic activity test for FSA. G3P D-glyceraldehyde-3-phosphate F6P fructose-6-phosphate PGI phosphoglucose Isomerase G6P glucose-6-phosphate GPD glu-cose-6-phosphate dehydrogenase.

Among the specific enzymes whose activity has been reported to be decreased after in vitro ozone exposure are papain, glyceraldehyde-3-phosphate dehydrogenase, lysozyme, ribonuclease, and acetylcholinesterase. The latter enzyme appears to be particulady susceptible to free-radical and oxidative states. A loss in acetylcholinesterase activity has been reported in the red cells of humans and mice that inhaled ozone. However, there are only minimal amounts of this enzyme in lupg tissue, and, although it has been suggested that acetylcholinesterase is important in bronchial tract ciliary activity, there is no direct evidence to support this conjecture. 

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