phosphorylase

Glycogen phosphorylase-IN-1 is a selective and potent inhibitor of human hepatic glycogen phosphorylase (hlGPa) with inhibitory effects on hlGPa activity and on hepatocyte glycogen-derived glucose production, and can be used in the study of type 2 diabetes mellitus and canine lupus.

Glycogen phosphorylase-IN-2 (compound 9C) is an inhibitor of glycogen phosphorylase, with a Ki value of 1.9 nM and an IC50 value of 4 nM.

Peldesine (BCX 34) is an effective, competitive, reversible, and orally active inhibitor of purine nucleoside phosphorylase. Peldesine inhibits T-cell proliferation with an IC50 of 800 nM. Peldesine can be used in research on cutaneous T-cell lymphoma, psoriasis and HIV infection.

Maltoheptaose (aka amyloheptaose) is a activater of phosphorylase B specifically to prepare (neurosin)heptulose-2-phosphate.

Urease/thymidine phosphorylase-IN-1 (compound 8) is an inhibitor of urease and thymidine phosphorylase, with an IC50 of 8.20 μM for urease and 9.29 μM for thymidine phosphorylase. It is applicable in research related to Helicobacter pylori infections, Proteus mirabilis infections, and cancer.

D-galactosyl-β1-3-N-acetyl-D-hexosamine phosphorylase (BiGalHexNAcP), a member of the CAZy glycoside hydrolase family GH112, plays a pivotal role in biochemical research by catalyzing the phosphorolysis of lacto-n-biose and galacto-n-biose, yielding Gal-1-P and the corresponding N-acetyl-D-hexosamine [1].

Purine Nucleoside Phosphorylase, an essential enzyme in purine metabolism, plays a critical role in the purine salvage pathway. Its deficiency impairs T cell function. With inorganic orthophosphate as a co-substrate, this enzyme catalyzes the cleavage of the glycosidic bond linking ribose and deoxyribonucleoside, resulting in the production of a purine base and ribose (deoxyribose)-1-phosphate [1].

Sucrose phosphorylase, a bacterial transglucosidase, catalyzes the conversion of sucrose and phosphate into α-D-glucose-1-phosphate and D-fructose. This enzyme can also hydrolyze glucosylated sucrose into α-D-glucose or transfer the glucosyl group to a receptor's hydroxyl group, resulting in new α-D-glucoside products. Its enzymatic activity towards the base, substrate, and product is weak [1].

Phosphorylase Kinase β-Subunit Fragment (420-436) is a peptide fragment (430-436) derived from the β-Subunit of phosphorylase kinase. Phosphorylase kinase, a serine/threonine-specific protein kinase, plays a crucial role in activating glycogen phosphorylase for the release of glucose-1-phosphate from glycogen [1].

Uridine phosphorylase, E. coli (EC 2.4.2.3), catalyzes the reversible phosphorolysis of uridine, resulting in the production of ribose-1-phosphate and uracil.

NucleosidePhosphorylase, bacterial (EC 2.4.2.1), is a pentosyltransferase. It plays a role in three metabolic pathways: purine metabolism, pyrimidine metabolism, and the metabolism of nicotinate and nicotinamide. The enzyme's substrates are purine nucleoside and phosphate, while its products are purine and α-D-ribose-1-phosphate.

Maltosephosphorylase, Bacteria (EC 2.4.1.8), is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose.

1,3-β-D-Glucanphosphorylase (EC 2.4.1.97) acts on diverse β-1,3-oligoglucans and laminari-type glucans.

1,2-α-Glucosylglycerolphosphorylase (EC 2.4.1.332) can convert β-D-glucose 1-phosphate into α-D-glucopyranose and phosphate in the absence of glycerol. During this reaction, the glucose residue is transferred to a water molecule, accompanied by inversion of anomeric configuration.

1,2-β-Oligoglucanphosphorylase (EC 2.4.1.333) catalyzes the reversible phosphorolysis of β-(1→2)-D-glucan. The substrate for this phosphorolysis reaction must be at least 3 D-glucose units long.

1,4-β-Mannosyl-N-acetylglucosaminephosphorylase (EC 2.4.1.320) is involved in the degradation of host-derived N-glycans.

1,2-β-Oligomannanphosphorylase (EC 2.4.1.340) catalyzes a reversible reaction. In the synthesis direction, it produces oligosaccharides with degrees of polymerization (DP) of 3, 4, and 5. The phosphorolysis reaction can proceed fully; however, enzyme activity peaks when the substrate contains a minimum of three residues.

1,3-α-Oligoglucanphosphorylase (EC 2.4.1.334) catalyzes a reversible reaction. The substrate for the phosphorolytic reaction consists of α-1,3-linked oligoglucans with a degree of polymerization of 3 or more.

1,3-β-Oligoglucanphosphorylase (EC 2.4.1.30) is a member of the glycosyltransferase family, specifically classified as a hexosyltransferase. This enzyme utilizes two substrates, (1,3-β-D-glucosyl) n and phosphate, to produce (1,3-β-D-glucosyl) n-1 and α-D-glucose-1-phosphate as its two products.

β-1,2-Mannobiosephosphorylase (EC 2.4.1.339) catalyzes a reversible reaction.

β-D-Galactosyl-(1-4)-L-rhamnosephosphorylase (EC 2.4.1.247) exhibits activity with β-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose. The order of activity is as follows: L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose.

α,α-Trehalosephosphorylase (EC 2.4.1.64) is a member of the glycosyltransferase family, specifically classified as a hexosyltransferase.

β-1,4-Mannooligosaccharidephosphorylase (EC 2.4.1.319) catalyzes the reversible phosphorolysis of β-1,4-mannooligosaccharides composed of at least three monomer units.

1,3-β-Galactosyl-N-acetylhexosaminephosphorylase (EC 2.4.1.211) catalyzes the reaction that uses β-D-pyranogalactosyl-(1→3)-N-acetyl-D-galactosamine as its substrate to produce N-acetyl-D-galactosamine.