phosphorylase


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phosphorylase

 [fos-for´ĭ-lās]
an enzyme that, in the presence of inorganic phosphate, catalyzes the conversion of glycogen into glucose-1-phosphate.

phos·phor·y·lase

(fos-fōr'i-lās),
An enzyme cleaving poly(1,4-α-d-glucosyl)n with orthophosphate to form poly(1,4-α-d-glucosyl)n-1 and α-d-glucose 1-phosphate. The active form of the enzyme is a phosphorylated protein.

phosphorylase

/phos·phor·y·lase/ (fos-for´ĭ-lās)
1. any of a group of enzymes that catalyze the phosphorolysis of glycosides, transferring the cleaved glycosyl group to inorganic phosphate. When not qualified with the substrate name, the term usually denotes glycogen phosphorylase (animals) or starch phosphorylase (plants).
2. any of a group of enzymes that catalyze the transfer of a phosphate group to an organic acceptor.

phosphorylase

(fŏs′fər-ə-lās′, -lāz′)
n.
Any of a class of enzymes that catalyze the attachment of a phosphate group to another molecule.

phosphorylase

[fosfôr′ilās]
Etymology: Gk, phosphoros, bringer of light + ase, enzyme suffix
any of a group of physiologically important enzymes that catalyze reactions between phosphates and glycogen or other starch components, yielding glucose-1-phosphate.

phos·phor·y·lase

(fos-fōr'i-lās)
A phosphorylated enzyme cleaving poly(1,4-α-d-glucosyl)n with inorganic phosphate to form poly(1,4-α- d-glucosyl)n-1 and α-d-glucose 1-phosphate.

phosphorylase

a key regulatory enzyme that, in the presence of inorganic phosphate, catalyzes the removal of one glucose unit from glycogen to glucose-1-phosphate.

citrulline phosphorylase
see ornithine carbamoyl transferase.
phosphorylase kinase
an enzyme that activates phosphorylase by catalyzing the phosphorylation of serine. See also kinase.
References in periodicals archive ?
Glycogen phosphorylase isoenzyme BB in diagnosis of myocardial ischaemic injury and infarction.
Interestingly, cones express glycogen phosphorylase (Brennenstuhl et al.
Leklem and Shultz (18) indicate that exercise stimulates the release and activation of the enzyme glycogen phosphorylase pyridoxal phosphate.
Phase II study of Capecitabine with concomitant radiotherapy for patients with locallyadvanced pancreatic cancer: up-regulation of thymidine phosphorylase.
The final product is ATP, which is a form of energy storage needed for cellular metabolism [10-15] This hypothesis would have two consequences on the one hand, degradation of glycogen phosphorylase activation or induction of glycogen as it is explained above, this reaction remained upstream of the cascade of biochemical reactions that lead to a complete glycolysis with the results in the formation of ATP, the other possible entry of glucose into hepatocytes through activation of glycogen synthase.
Fructose-1,6-bisphosphatase activity was measured by the method of Gancedo and Gancedo (1971), pyruvate kinase activity was estimated by the method of Pogson and Denton (1967), lactate dehydrogenase activity was estimated by the method of King (1965), glycogen synthase activity was estimated by the method of Leloir and Goldemberg (1962), glycogen phosphorylase activity was estimated by the method of Cornblath et al.
Furthermore, studies have assessed the seasonality of the glycogen phosphorylase and glycogen synthase enzymes in the green frog (Rana esculenta) liver and have found that phosphorylase is more active during wintertime, while the synthase, during the summer, suggesting a seasonal influence on the activity of these enzymes (SCAPIN; DI GIUSEPPE, 1994).
Glycogen phosphorylase is the primary enzyme involved in this breakdown and Aegle marmelos appears to inhibit glycogen phosphorylase, thereby regulating the glycogenolysis pathway and leading to a decrease in the glucose level in the blood (Narendhirakannan et al.
Expression of glycogen phosphorylase, responsible for glycogen catabolism was increased 4-fold by P4 when compared to controls (P<0.
Galactosaemia, in fact, often results in hypoglycaemia caused by hepatic accumulation of galactose-1phosphate, which inhibits enzymes of glycogenolysis; including glucose-6-phosphatase, glucose-6-phosphate dehydrogenase, phosphoglucomutase and glycogen phosphorylase.
The study in Cell outlined a new role for a protein called polynucleotide phosphorylase (PNPASE) in regulating the import of RNA into mitochondria.