- Protecting group directed stereoselective reduction of an epi-inosose: Efficient synthesis of epi-inositol
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A facile and high yielding synthesis of epi-inositol via stereoselective reduction of a pentaprotected epi-inosose is reported. Extent of stereoselectivity during the hydride reduction appears to depend on the ability of the substrate to complex with metal ions in the reducing agent.
- Patil, Madhuri T.,Krishnaswamy, Shobhana,Sarmah, Manash P.,Shashidhar, Mysore S.
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supporting information; experimental part
p. 3756 - 3758
(2011/08/06)
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- Kinetics of the reaction catalyzed by inositol dehydrogenase from Bacillus subtilis and inhibition by fluorinated substrate analogs
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Inositol dehydrogenase (EC 1.1.1.18) from Bacillus subtilis catalyzes the oxidation of myo-inositol to scyllo-inosose by transfer of the equatorial hydride of the substrate to NAD+. This is a key enzyme in the metabolism of myo-inositol, a primary carbon source for soil bacteria. In light of our recent discovery that the enzyme has a broad substrate spectrum while maintaining high stereoselectivity, we seek a more thorough understanding of the enzyme and its active site. We have examined the kinetics of the recombinant enzyme, and synthesized fluorinated substrate analogues as competitive inhibitors. We have evaluated all rate constants in the ordered, sequential Bi Bi mechanism. No steady-state kinetic isotope effect is observed using myo-[2-2H]-inositol, indicating that the chemical step of the reaction is not rate-limiting. We have synthesized the substrate analogs 2-deoxy-2-fluoro-myo-inositol, its equatorial analog 1-deoxy-1-fluoro-scyllo- inositol, the gem-difluorinated analog 1-deoxy-1,1-difluoro-scyllo-inositol, and the sugar analog α-D-glucosyl fluoride. Of these, 1-deoxy-1-fluoro- scyllo-inositol showed no inhibition, while all others tested had Ki values comparable to the Km values of the analogous substrates myo-inositol and α-D-glucose.
- Daniellou, Richard,Zheng, Hongyan,Palmer, David R.J.
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p. 522 - 527
(2007/10/03)
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- Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis
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The doubly functional aminotransferase BtrS in the 2-deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruptio
- Yokoyama, Kenichi,Kudo, Fumitaka,Kuwahara, Mieko,Inomata, Kousuke,Tamegai, Hideyuki,Eguchi, Tadashi,Kakinuma, Katsumi
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p. 5869 - 5874
(2007/10/03)
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- Stereoselective oxidation of protected inositol derivatives catalyzed by inositol dehydrogenase from Bacillus subtilis
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Inositol dehydrogenase (EC 1.1.1.18) from Bacillus subtilis is shown to have a nonpolar cavity adjacent to the active site, allowing racemic protected inositol derivatives such as 4-O-benzyl-myo-inositol to be recognized with very high apparent stereoselectivity.
- Daniellou, Richard,Phenix, Christopher P.,Tam, Pui Hang,Laliberte, Michael C.,Palmer, David R. J.
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p. 401 - 403
(2007/10/03)
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- The oxidation of partially acylated myoinositols
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1,3,4,6-Tetrakis-and 1,3,4,5,6-pentakis-acylmyoinositols are obtained by the controlled catalyzed acylation of myoinositol. The extent of the substitution depends both on the reaction conditions and the structure of the acylating agent, including steric f
- Kurzer, Frederick,Chapman, Dennis
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- The Selectivity of Attack by the Hydroxyl Radical on Myoinositol, and the Importance of Stereoelectronic Factors upon Radical Rearrangement: an Electron Spin Resonance Conformational-analysis Study
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E.s.r. spectroscopy has been employed to show that the reaction of .OH with the model substrate myoinositol is unselective; at pH 4, e.s.r. signals of all possible radicals produced by C-H abstraction are detected.A conformational analysis based on the hy
- Gilbert, Bruce C.,King, David M.,Thomas, C. Barry
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p. 1821 - 1827
(2007/10/02)
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