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Phosphorolysis, glycogen

I. Glycogen phosphorylase catalyzes glycogen phosphorolysis (bond cleavage of the a-(I 4) bonds by the substitution of a phosphate group) to yield glucose-1-phosphate ... [Pg.30]

The glycogen phosphorolysis of phosphorylase can be reverted, which makes it possible to enzymatically polymerize amylose as well as hybrid structures with amylose as outlined in the following section. [Pg.31]

Simplified mecharusms of peptide hydrolysis and glycogen phosphorolysis arc outlined as follows ... [Pg.122]

This results in activation of cAMP-dependent protein kinase (protein kinase A), with consequent phosphorylation of target proteins, such as phosphorylase b kinase in cells that activate glycogen phosphorolysis. [Pg.295]

Fig. 3.8. The role of cAMP as an intermediate to environmental stimulus (hormone secretion) and the onset of physiological response. Adrenaline and GTP bind to a specific membrane bound regulatory subunit of adenyl cyclase. This elicits a conformational change such as to activate the catalytic subunit and stimulate cAMP synthesis. cAMP activates a protein kinase by causing its dissociation into an active catalytic subunit (R = regulatory subunit C = catalytic subunit). This in turn catalyzes the phosphorylation of two serine residues of an inactive phosphorylase b enzyme. Two dimers combine to form an active tetramer phosphorylase a. Phosphorylase catalyzes the breakdown of the sugar storage form glycogen (phosphorolysis) to glucose 1-... Fig. 3.8. The role of cAMP as an intermediate to environmental stimulus (hormone secretion) and the onset of physiological response. Adrenaline and GTP bind to a specific membrane bound regulatory subunit of adenyl cyclase. This elicits a conformational change such as to activate the catalytic subunit and stimulate cAMP synthesis. cAMP activates a protein kinase by causing its dissociation into an active catalytic subunit (R = regulatory subunit C = catalytic subunit). This in turn catalyzes the phosphorylation of two serine residues of an inactive phosphorylase b enzyme. Two dimers combine to form an active tetramer phosphorylase a. Phosphorylase catalyzes the breakdown of the sugar storage form glycogen (phosphorolysis) to glucose 1-...
Fig. 5 Catalytic mechanism of glycogen phosphorylases. The reaction scheme accounts for the reversibility of phosphorolysis of oligosaccharides (R) in the presence of orthophosphate (upper half) and primer-dependent synthesis in the presence of glucose-l-phosphate (lower half). PL enzyme-bound pyridoxal BH-f a general base contributed by the enzyme protein. Reprinted with permission from [109]. Copyright 1990 American Chemical Society... Fig. 5 Catalytic mechanism of glycogen phosphorylases. The reaction scheme accounts for the reversibility of phosphorolysis of oligosaccharides (R) in the presence of orthophosphate (upper half) and primer-dependent synthesis in the presence of glucose-l-phosphate (lower half). PL enzyme-bound pyridoxal BH-f a general base contributed by the enzyme protein. Reprinted with permission from [109]. Copyright 1990 American Chemical Society...
Glycogen phosphorylase sequentially cleaves the cx(1 -h>4) glycosidic bonds between the glucosyl residues at the nonreducing ends of the glycogen chains by simple phosphorolysis until four glucosyl units remain on each chain before a branch point (Figure 11.7). [Note ... [Pg.127]

Some phosphoric acid derivatives of 2-desoxy-D-ribose have been obtained by enzymic methods of preparation. A reaction analogous to the phosphorolysis of glycogen to D-glucose 1-phosphate241 has been effected with either hypoxanthine- or guanine-D-riboside, both of which could be split by enzymic phosphorolysis with the formation of D-ribose 1-phosphate.242 The successful conclusion of these experiments prompted similar investigations with desoxyribonucleosides. [Pg.103]

IMP is cleaved by phosphorolysis of the nucleoside to yield hypoxanthine and ribose-1-phosphate. (This reaction is similar to the phosphorolysis of glycogen by glycogen phosphorylase.)... [Pg.106]

Figure 12-1 Phosphorylase-catalyzed phosphorolysis of glycogen or starch to glucose-1-phosphate. Figure 12-1 Phosphorylase-catalyzed phosphorolysis of glycogen or starch to glucose-1-phosphate.
Glycogen phosphorylase catalyzes the sequential phosphorolysis of glycogen to release glucose 1-phosphate it is thus the key enzyme in the utilization of tissue glycogen reserves. [Pg.244]


See other pages where Phosphorolysis, glycogen is mentioned: [Pg.58]    [Pg.422]    [Pg.425]    [Pg.58]    [Pg.422]    [Pg.425]    [Pg.473]    [Pg.755]    [Pg.206]    [Pg.8]    [Pg.167]    [Pg.47]    [Pg.534]    [Pg.534]    [Pg.562]    [Pg.566]    [Pg.613]    [Pg.898]    [Pg.508]    [Pg.494]    [Pg.251]    [Pg.34]    [Pg.303]    [Pg.107]    [Pg.364]    [Pg.482]    [Pg.205]    [Pg.205]    [Pg.243]    [Pg.245]    [Pg.245]   
See also in sourсe #XX -- [ Pg.34 ]

See also in sourсe #XX -- [ Pg.34 ]




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