Jensen, Pernille Rose, and Sebastian Meier. “Catalytic Cycle of Carbohydrate Dehydration by Lewis Acids: Structures and Rates from Synergism of Conventional and DNP NMR.” Chemical Communications 56, no. 46 (June 9, 2020): 6245–48.
Lewis acids play key roles in many chemical reactions. Structural and functional (kinetic) detail in Lewis acid catalysed fructose conversion are derived herein by the combined use of conventional and dissolution dynamic nuclear polarization (D-DNP) NMR. Structural information obtained with D-DNP NMR was used to identify conditions that stabilize an elusive initial intermediate and to determine its chemical structure. Carbohydrate dehydration through this intermediate had been predicted computationally. Complementary kinetic NMR assays yielded rate constants spanning three orders of magnitude for the three biggest energy barriers in the catalytic cycle.
[ASAP] Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography
Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00517/20191003/images/medium/bi9b00517_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00517
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02-29-2020 09:52 PM
Selenoglutathione Diselenide: Unique Redox Reactionsin the GPx-Like Catalytic Cycle and Repairing of Disulfide Bonds inScrambled Protein
Selenoglutathione Diselenide: Unique Redox Reactionsin the GPx-Like Catalytic Cycle and Repairing of Disulfide Bonds inScrambled Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00751/20171012/images/medium/bi-2017-00751x_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00751
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UncoveringNonconventional and Conventional HydrogenBonds in Oligosaccharides through NMR Experiments and Molecular Modeling:Application to Sialyl Lewis-X
UncoveringNonconventional and Conventional HydrogenBonds in Oligosaccharides through NMR Experiments and Molecular Modeling:Application to Sialyl Lewis-X
Marcos D. Battistel, Hugo F. Azurmendi, Martin Frank and Daro?n I. Freedberg
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03824/20151015/images/medium/ja-2015-038244_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03824
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Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Abstract The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation, rigorous enzymatic assays of isomerization are required. However, most measures of isomerase activity require significant constraints on substrate sequence and only yield rate constants for the cis isomer,
kcatcis and apparent Michaelis constants,
...
nmrlearner
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09-30-2011 08:01 PM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...
nmrlearner
Journal club
0
09-30-2011 06:00 AM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...