inositol-3-phosphate has been researched along with inositol-1-phosphate* in 4 studies
4 other study(ies) available for inositol-3-phosphate and inositol-1-phosphate
Article | Year |
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Altering the Phosphorylation Position of Pyrophosphate-Dependent
Most kinases utilize ATP as a phosphate donor and phosphorylate a wide range of phosphate acceptors. An alternative phosphate donor is inorganic pyrophosphate (PPi), which costs only 1/1000 of ATP. To develop a method to engineer PPi-dependent kinases, we herein aimed to alter the product of PPi-dependent Topics: Catalytic Domain; Crystallization; Diphosphates; Inositol Phosphates; Kinetics; Magnetic Resonance Spectroscopy; Mutant Proteins; Mutation; Phosphoric Monoester Hydrolases; Phosphorylation; Protein Conformation; Tandem Mass Spectrometry; Thermotoga maritima | 2021 |
Nonenzymatic peptide-based catalytic asymmetric phosphorylation of inositol derivatives.
The ability to use small peptides as catalysts for asymmetric phosphorylation provides opportunities for rapid syntheses of phosphate-containing compounds and natural products. This short review outlines the genesis of this concept and its reduction to practice in the context of concise syntheses of the enantiomeric D-I-1P and D-I-3P targets. The implications for the development of additional site-selective catalysts are discussed. Topics: Catalysis; Inositol Phosphates; Kinetics; Models, Chemical; Oxidation-Reduction; Peptides; Phosphorylation; Stereoisomerism; Structure-Activity Relationship | 2003 |
Enantiodivergence in small-molecule catalysis of asymmetric phosphorylation: concise total syntheses of the enantiomeric D-myo-inositol-1-phosphate and D-myo-inositol-3-phosphate.
Peptide-based catalysts have been found that catalyze the enantiodivergent phosphorylation of a meso myo-inositol-derived triol (1). The sequential screening of random peptide libraries, followed by the evaluation of a focused library, led to the identification of two peptides (2 and 24) that are complementary in producing enantiomeric D-myo-inositol-1-phosphate and D-myo-inositol-3-phosphate derivatives. The catalysts were then used to complete efficient total syntheses of both D-I-1P and D-I-3P in optically pure form. Additional information is gleaned from relative rate experiments that unambiguously show the catalysts to afford enantioselection through rate accelerative pathways with respect to simple achiral alkylimidazole catalysts. Furthermore, solvent effect studies show that the two enantiodivergent catalysts exhibit different tolerances of polar media. The systematic discovery of site-selective catalysts establishes a basis for future studies of chiral catalysts that differentiate unique functional groups in polyfunctional molecules. Topics: Catalysis; Inositol Phosphates; Kinetics; Oligopeptides; Phosphorylation; Stereoisomerism | 2002 |
Effect of lithium on muscarinic cholinoceptor-stimulated phosphoinositide-specific phospholipase C substrate selectivity in CHO-m1 cells.
Topics: Animals; CHO Cells; Cricetinae; Humans; Inositol Phosphates; Kinetics; Lithium; Phosphatidylinositol Diacylglycerol-Lyase; Phosphatidylinositols; Phosphoric Diester Hydrolases; Receptors, Muscarinic; Recombinant Proteins; Substrate Specificity | 1995 |