Botta et al., "Simplified analogues of immucillin-G retain potent human purine nucleoside phosphorylase
inhibitory activity," Journal of Medicinal Chemistry, vol.
Glycogen phosphorylase (GP) is the enzyme responsible for the synthesis of glucose-1-phosphate, the source of energy for muscles and the rest of the body .
Abbreviations GS: Glycogen synthase GP: Glycogen phosphorylase PEPCK1: Phosphoenolpyruvate carboxykinase 1 G-6-Pase: Glucose-6-phosphatase GLUT2: Glucose transporter type 2 PGC-1[alpha]: PPAR[gamma] coactivator 1a AMPK: AMP-activated protein kinase ACC: Acetyl-CoA carboxylase TORC: Transducer of regulated CREB mTOR: Mammalian target of rapamycin CREB: cAMP-response element-binding protein.
Part 2: synthesis and biological evaluation of maslinic acid derivatives as glycogen phosphorylase inhibitors," Bioorganic and Medicinal Chemistry Letters, vol.
Identification and comparative analysis of thymidine phosphorylase
in plasma of healthy subjects and cancer patients.
Transitory starch in the source leaf is degraded by starch degrading enzymes including amylase and starch phosphorylase. No difference was detected between the mutant and normal leaves for activity of either of these enzymes (Table 4).
Enzyme activity Ensyme C2-4 (normal) Ex139 (hls) units [g.zup.-1] protein Amylase 34.7 35.3 Starch phosphorylase 15.7 15.3 Hexokinase 0.95 1.01 Phosphoglucomutase 0.84 0.80 Phosphohexose isomerase 1.88 1.87 Phosphofruetokinase 0.84 0.83 Aldolase 6.9 6.5 Triosephosphate isomerase 125 126 Fructose-1,6-bisphosphatase 2.8 2.7 UDP glucose pyrophosphorylase 0.5 0.5 Sucrose-P phosphalase 18 17 Invertase 61.4 87.3 Significance Ensyme of t-test Amylase NS Starch phosphorylase NS Hexokinase NS Phosphoglucomutase NS Phosphohexose isomerase NS Phosphofruetokinase NS Aldolase NS Triosephosphate isomerase NS Fructose-1,6-bisphosphatase NS UDP glucose pyrophosphorylase NS Sucrose-P phosphalase NS Invertase (**) (*), (**) means significantly different at P = 0.05 and P = 0.01, respectively.
The starch degrading enzymes, amylase and starch phosphorylase, have been associated with transitory starch breakdown, but these had identical activities in his and normal-leaf plants, and identical native PAGE banding patterns.
These include: [Beta]-amylase (1,4-[Alpha]-D-glucan maltohydrolase) [EC 22.214.171.124, an exo-amylase that hydrolyzes starch from the nonreducing ends, producing maltose and [Beta]-limit dextrin; [Alpha]-amylase (1,4-[Alpha]-D-glucan glucanohydrolase) [EC 126.96.36.199], an endo-amylase that hydrolyzes starch by random hydrolysis of nonterminal glucosidic linkages to produce glucose, maltose, maltotriose, and branched oligosaccharides; [Alpha]-glucosidase ([Alpha]-D-glucoside glucohydrolase) [EC 188.8.131.52], which hydrolyzes maltose and other oligosaccharides to glucose, and starch phosphorylase (1,4-[Alpha]-D-glucan: orthophosphate [Alpha]-D-glucosyltransferase) [EC 184.108.40.206], which catalyzes in a reversible manner the formation of glucose-1-phosphate from starch and inorganic phosphate.
Starch phosphorylase activity was detected in the synthesis direction as described by Steup (1990).
Furosemide, at a final concentration of 0.1 mmol/L in serum-anti-[T.sub.3] antibody-furosemide solution, provided maximum [T.sub.3] displacement without interfering with the phosphorylase assay.
Effect of sodium cholate on the catalytic and structural properties of phosphorylase b.