Phosphorylase formation

A Phosphorylases Formation of a P - O bond under phosphorolytic cleavage of a C-Hetero-atom bond. 2.4.1. 2.4.2. Hexosyltransferases Pentosyltransferases... 

Maltose phosphorylase proceeds via a single-displacement reaction that necessarily requires the formation of a ternary maltose E Pi (or glucose E glucose-l-phosphate) complex for any reaction to occur. Exchange reactions are a characteristic of enzymes that obey double-displacement mechanisms at some point in their catalysis. 

MP, approximately 30 phosphorylase kinase molecules are activated these in turn activate some 800 molecules of phosphorylase. Each of these catalyzes the formation of many molecules of glucose-l-P. 

Both phosphorylase a and phosphorylase kinase a are dephosphorylated and inactivated by protein phos-phatase-1. Protein phosphatase-1 is inhibited by a protein, inhibitor-1, which is active only after it has been phosphorylated by cAMP-dependent protein kinase. Thus, cAMP controls both the activation and inactivation of phosphorylase (Figure 18-6). Insulin reinforces this effect by inhibiting the activation of phosphorylase b. It does this indirectly by increasing uptake of glucose, leading to increased formation of glucose 6-phosphate, which is an inhibitor of phosphorylase kinase. 

After intravenous administration, about 80-90% of the dose is catabolized in the liver by dihydropyrimidine dehydrogenase (DPD) [38] (Figure 14.3). The formation of the inactive 5-fluoro-5,6-dihydrouracil (5-FUH2) by DPD is the rate-limiting step of 5-FU catabolism [39]. DPD is widely distributed among tissues, with the highest levels found in the liver. Once 5-FU entered tumor cells, its antitumor effect is mainly dependent on the extent of 5-FU anabolism. After two sequential anabolic steps involving thymidine phosphorylase (TP) and thymidine kinase... 

That the same enzyme,28 sucrose phosphorylase, is involved in the reaction of L-arabinose is indicated by the following observation. When L-arabinose is added to a mixture containing the enzyme, D-glucose-1-phosphate and D-fructose, of which the last is present in insufficient concentration to give the maximum rate of sucrose formation, an increase... 

We may conclude from this discussion that in the formation of the phosphorylase-sucrose complex the glucosidic oxygen, the OH groups at C6, C4 and C2 of the glucopyranose moiety and the OH group at C3 of the fructofuranose moiety of the substrate are involved. 

Murakami and Kondo (1975) reported that the cationic micelle is quite effective for the pyridoxal-catalyzed elimination of S-phenylcysteine. The significant rate acceleration was explained by the binding of the Schiff s base to the micelle phase, followed by the efficient proton abstraction by hydroxide ion at the micelle surface. According to Gani et al. (1978), mixed micelles of CTAB and dodecylamine hydrochloride are good models for the site accommodating pyridoxal 5 -phosphate in glycogen phosphorylase, since the micelles can imitate well the formation of SchifT s bases in hydrophobic environments. 

The next key point is to realize that each enzyme in the pathway exists in both active and inactive forms. cAMP initiates a cascade of reactions by activating protein kinase A (PK-A)," the active form of which activates the next enzyme in the sequence, and so on. At the end of the day, glycogen phosphorylase is activated and glucose or ATP is produced. This signaling pathway is a marvelous amplification system. A few molecules of glucagon or adrenaline may induce formation of many molecules of cAMP, which may activate many of PK-A, and so on. The catalytic power of enzymes is magnified in cascades of this sort. 

The large and negative value for hexokinase indicates that this enzyme catalyses the reaction only in the direction of glucose 6-phosphate formation, i.e. it is a non-equilibrium reaction in vivo. In contrast, the low value for phosphoglucoisomerase indicates that it is a reaction that is close to equilibrium in vivo, that is, it can proceed in either direction. AG valnes for all the reactions of glycolysis indicate that those catalysed by hexokinase, phosphorylase, phos-phofractokinase and pyrnvate kinase are non-eqnilibrinm the others are near eqnilibrinm (Fignre 2.6). 

Malonate complexes, osmium, 37 286 Maltose phosphorylase, arsenate and, 44 194 compound I formation, 43 99 exogenous reduction of intermediates, 43 116-119... 

Pfannemtiller et al. showed that it is possible to obtain carbohydrate-containing amphiphiles with various alkyl chains via amide bond formation. For this, mal-tooligosaccharides were oxidized to the corresponding aldonic acid lactones, which could subsequently be coupled to alkylamines [128-136]. Such sugar-based surfactants are important industrial products with applications in cosmetics, medical applications etc. [137-139]. The authors were also able to extend the attached mal-tooligosaccharides by enzymatic polymerization using potato phosphorylase, which resulted in products with very interesting solution properties [140, 141]. 

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