1,2:4,5-Biscyclohexylidene-DL-myo-inositol - CAS 104873-71-4
Category: Carbohydrates
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1.Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1.
Suleimanova AD1, Beinhauer A2, Valeeva LR1, Chastukhina IB1, Balaban NP1, Shakirov EV3, Greiner R2, Sharipova MR4. Appl Environ Microbiol. 2015 Oct;81(19):6790-9. doi: 10.1128/AEM.01384-15. Epub 2015 Jul 24.
Phosphorus is an important macronutrient, but its availability in soil is limited. Many soil microorganisms improve the bioavailability of phosphate by releasing it from various organic compounds, including phytate. To investigate the diversity of phytate-hydrolyzing bacteria in soil, we sampled soils of various ecological habitats, including forest, private homesteads, large agricultural complexes, and urban landscapes. Bacterial isolate Pantoea sp. strain 3.5.1 with the highest level of phytase activity was isolated from forest soil and investigated further. The Pantoea sp. 3.5.1 agpP gene encoding a novel glucose-1-phosphatase with high phytase activity was identified, and the corresponding protein was purified to apparent homogeneity, sequenced by mass spectroscopy, and biochemically characterized. The AgpP enzyme exhibits maximum activity and stability at pH 4.5 and at 37°C. The enzyme belongs to a group of histidine acid phosphatases and has the lowest Km values toward phytate, glucose-6-phosphate, and glucose-1-phosphate.
2.D-myo-inositol 1,4,5-trisphosphate analogues modified at the 3-position inhibit phosphatidylinositol 3-kinase.
Ward SG1, Mills SJ, Liu C, Westwick J, Potter BV. J Biol Chem. 1995 May 19;270(20):12075-84.
Several natural and unnatural inositol phosphates and analogues were analyzed for their ability to inhibit the in vitro phosphatidylinositol 3-kinase (PI 3-kinase) activity immunoprecipitated from a leukemic T cell line by a p85 monoclonal antibody. A 3-position ring-modified analogue of D-myo-inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), L-chiro-inositol 2,3,5-trisphosphate (L-chiro-Ins(2,3,5)P3) and its phosphorothioate analogue, L-chiro-inositol 2,3,5-trisphosphorothioate, as well as the analogue benzene 1,2,4-trisphosphate induced reversible inhibition of PI 3-kinase activity, which correlated with decreased Vmax but unchanged Km values for PI 3-kinase. Other inositol phosphates, including D- and L-Ins(1,4,5)P3, D-myo-inositol 1,3,4,5-tetrakisphosphate, the enantiomers of myo-inositol 1,3,4-trisphosphate, DL-myo-inositol 1,4,6-trisphosphate (DL-Ins(1,4,6)P3), and DL-scyllo-inositol 1,2,4-trisphosphate (DL-scyllo-Ins(1,2,4)P3), did not inhibit PI 3-kinase activity under identical conditions.
3.Functional identification of sll1383 from Synechocystis sp PCC 6803 as L-myo-inositol 1-phosphate phosphatase (EC molecular cloning, expression and characterization.
Patra B1, Ghosh Dastidar K, Maitra S, Bhattacharyya J, Majumder AL. Planta. 2007 May;225(6):1547-58. Epub 2006 Nov 23.
The genome sequence of the cyanobacterium Synechocystis sp. PCC6803 revealed four Open reading frame (ORF) encoding putative inositol monophosphatase or inositol monophosphatase-like proteins. One of the ORFs, sll1383, is approximately 870 base pair long and has been assigned as a probable myo-inositol 1 (or 4) monophosphatase (IMPase; EC IMPase is the second enzyme in the inositol biosynthesis pathway and catalyses the conversion of L-myo-inositol 1-phosphate to free myo-inositol. The present work describes the functional assignment of ORF sll1383 as myo-inositol 1-phosphate phosphatase (IMPase) through molecular cloning, bacterial overexpression, purification and biochemical characterization of the gene product. Affinity (K (m)) of the recombinant protein for the substrate DL-myo-inositol 1-phosphate was found to be much higher (0.0034 +/- 0.0003 mM) compared to IMPase(s) from other sources but in comparison V (max) ( approximately 0.
4.DL-myo-inositol 1,2,4,5-tetrakisphosphate, a potent analog of D-myo-inositol 1,4,5-trisphosphate.
Hirata M1, Narumoto N, Watanabe Y, Kanematsu T, Koga T, Ozaki S. Mol Pharmacol. 1994 Feb;45(2):271-6.
Synthetic DL-myo-inositol 1,2,4,5-tetrakisphosphate (DL-Ins-(1,2,4,5)P4) functioned as a full agonist, with only 3-fold less potency than D-Ins(1,4,5)P3 in eliciting the release of Ca2+ from nonmitochondrial pools of permeabilized rat basophilic leukemic cells. DL-Ins(1,2,4,5)P4 inhibited the binding of D-[3H]Ins(1,4,5)P3 to the purified D-Ins(1,4,5)P3 receptor with almost the same potency as seen for the Ca2+ release. This compound inhibited the hydrolysis of D-[3H]Ins(1,4,5)P3 to D-[3H]Ins(1,4)P2 catalyzed by erythrocyte ghosts, with a Ki value of as low as 1.4 microM, but it could not serve as a substrate for the same enzyme. D-Ins(1,4,5)P3 3-kinase in rat brain cytosol did not recognize the compound at concentrations up to 30 microM. Thus, it would appear that DL-Ins(1,2,4,5)P4 can serve as a potent and long lasting experimental and pharmacological tool for stimulating D-Ins(1,4,5)P3-mediating processes.
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CAS 104873-71-4 1,2:4,5-Biscyclohexylidene-DL-myo-inositol

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