The Experts below are selected from a list of 240 Experts worldwide ranked by ideXlab platform

Michael Hodges - One of the best experts on this subject based on the ideXlab platform.

  • experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Edouard Boexfontvieille, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Michael Hodges
    Abstract:

    Abstract In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes, and compared isotope effects using natural and deuterated glycolate, in either natural or deuterated solvent. The 12C/13C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the 13C natural abundance in glycolate, using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an H/D isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

  • Experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Edouard Boex-fontvieille, Michael Hodges
    Abstract:

    In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The (12)C/(13)C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the (13)C natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

John W. Kozarich - One of the best experts on this subject based on the ideXlab platform.

  • Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
    Annual review of biochemistry, 2008
    Co-Authors: Benjamin F. Cravatt, Aaron T. Wright, John W. Kozarich
    Abstract:

    Genome sequencing projects have provided researchers with a complete inventory of the predicted proteins produced by eukaryotic and prokaryotic organisms. Assignment of functions to these proteins represents one of the principal challenges for the field of proteomics. Activity-based protein profiling (ABPP) has emerged as a powerful chemical proteomic strategy to characterize Enzyme function directly in native biological systems on a global scale. Here, we review the basic technology of ABPP, the Enzyme classes addressable by this method, and the biological discoveries attributable to its application.

  • Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
    2008
    Co-Authors: Benjamin F. Cravatt, Aaron T. Wright, John W. Kozarich
    Abstract:

    Genome sequencing projects have provided researchers with a complete inventory of the predicted proteins produced by eukaryotic and prokaryotic organisms. Assignment of functions to these proteins represents one of the principal challenges for the field of proteomics. Activity-based protein profiling (ABPP) has emerged as a powerful chemical proteomic strategy to characterize Enzyme function directly in native biological systems on a global scale. Here, we review the basic technology of ABPP, the Enzyme classes addressable by this method, and the biological discoveries attributable to its application.

  • Activity-based proteomics: Enzyme Chemistry redux.
    Current opinion in chemical biology, 2003
    Co-Authors: John W. Kozarich
    Abstract:

    The principles of Enzyme Chemistry, mechanism of action and inhibitor design are being applied to proteomics by the development of activity-based probes. This approach suggests a potentially broad method for interrogating Enzyme family members, both known and unknown, in cells and proteomic fractions without the need for individual assay development and isolation. The serine hydrolases and cysteine proteases have provided the proofs of concept for activity-based proteomics, and other studies are rapidly following. The result will be a proteomics technology of great value to drug discovery and development.

Guillaume Tcherkez - One of the best experts on this subject based on the ideXlab platform.

  • experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Edouard Boexfontvieille, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Michael Hodges
    Abstract:

    Abstract In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes, and compared isotope effects using natural and deuterated glycolate, in either natural or deuterated solvent. The 12C/13C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the 13C natural abundance in glycolate, using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an H/D isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

  • Experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Edouard Boex-fontvieille, Michael Hodges
    Abstract:

    In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The (12)C/(13)C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the (13)C natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

Younes Dellero - One of the best experts on this subject based on the ideXlab platform.

  • experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Edouard Boexfontvieille, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Michael Hodges
    Abstract:

    Abstract In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes, and compared isotope effects using natural and deuterated glycolate, in either natural or deuterated solvent. The 12C/13C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the 13C natural abundance in glycolate, using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an H/D isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

  • Experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Edouard Boex-fontvieille, Michael Hodges
    Abstract:

    In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The (12)C/(13)C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the (13)C natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

Mathieu Jossier - One of the best experts on this subject based on the ideXlab platform.

  • experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Edouard Boexfontvieille, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Michael Hodges
    Abstract:

    Abstract In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes, and compared isotope effects using natural and deuterated glycolate, in either natural or deuterated solvent. The 12C/13C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the 13C natural abundance in glycolate, using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an H/D isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.

  • Experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis
    Journal of Biological Chemistry, 2015
    Co-Authors: Younes Dellero, Valerie Flesch, Mathieu Jossier, Caroline Mauve, Guillaume Tcherkez, Edouard Boex-fontvieille, Michael Hodges
    Abstract:

    In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase Enzyme Chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant Enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The (12)C/(13)C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the (13)C natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 Enzymes.