phosphorolytic

In archaea, the Rrp41 subunit of the complex is a phosphorolytic exoribonuclease.

Enzymes that have phosphorolytic 3' to 5' exoribonuclease activity (break phosphodiester bond)

Thus additional residues in the APEs control specificity while still allowing a reasonable rate of phosphorolytic cleavage.

The phosphorolytic enzymes use inorganic phosphate to cleave the phosphodiester bonds - releasing nucleotide diphosphates.

This analysis indicated that residues binding 3' to the site of phosphorolytic cleavage control the substrate specificity of APE1.

The energy is obtained through the phosphorolytic cleavage of glycosidic bonds as well as the anaerobic glycolysis of the glucose monomers.

The plant alpha-glucan phosphorylase, commonly called starch phosphorylase (EC 2.4.1.1), is largely known for the phosphorolytic degradation of starch.

Exoribonucleases can use either water to cleave the nucleotide-nucleotide bond (which is called hydrolytic activity) or inorganic phosphate (which is called phosphorolytic activity).

Hydrolytic exoribonucleases are classified under EC number 3.1 and phosphorolytic exoribonucleases under EC number 2.7.7.

After glycogen phosphorylase catalyzes the phosphorolytic cleavage of a glucosyl residue from the glycogen polymer, the freed glucose has a phosphate group on its 1-carbon.

Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a cofactor to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides.

It is proposed that alpha-glucosidase in the glucosidic path plays an important part in complementing the phosphorolytic pathway in the liver's metabolic response to energy demands of exercise.

Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity.

As the phosphorolytic enzymes use inorganic phosphate to cleave bonds they release nucleotide disphosphates), whereas the hydrolytic enzymes (which use water) release nucleotide monosphosphates).

In eukaryotes, the absence of the phosphorolytic activity is compensated by the presence of the hydrolytic enzymes, which are responsible for the ribonuclease activity of the exosome in such organisms.

Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.

If the glycogen chain has n glucose units, the products of a single phosphorolytic event are one molecule of glucose 1-phosphate and a glycogen chain of n-1 remaining glucose units.

Exoribonucleases contained in exosome complexes are either phosphorolytic (the RNase PH-like proteins) or, in eukaryotes, hydrolytic (the RNase R and RNase D domain proteins).