1. Selective photoregulation of the activity of glycogen synthase and glycogen phosphorylase, two key enzymes in glycogen metabolism.

    Organic & Biomolecular Chemistry 13(26):7282 (2015) PMID 26055498

    Glycogen is a polymer of α-1,4- and α-1,6-linked glucose units that provides a readily available source of energy in living organisms. Glycogen synthase (GS) and glycogen phosphorylase (GP) are the two enzymes that control, respectively, the synthesis and degradation of this polysaccharide and c...
  2. A Major Determinant for Gliding Motility in Mycoplasma genitalium: THE INTERACTION BETWEEN THE TERMINAL ORGANELLE PROTEINS MG200 AND MG491.

    Journal of Biological Chemistry 290(3):1699 (2015) PMID 25471372 PMCID PMC4340413

    Several mycoplasmas, such as the emergent human pathogen Mycoplasma genitalium, developed a complex polar structure, known as the terminal organelle (TO), responsible for a new type of cellular motility, which is involved in a variety of cell functions: cell division, adherence to host cells, an...
  3. A Major Determinant for Gliding Motility in Mycoplasma genitalium: THE INTERACTION BETWEEN THE TERMINAL ORGANELLE PROTEINS MG200 AND MG491.

    Journal of Biological Chemistry 290(3):1699 (2015) PMID 25471372

    Several mycoplasmas, such as the emergent human pathogen Mycoplasma genitalium, developed a complex polar structure, known as the terminal organelle (TO), responsible for a new type of cellular motility, which is involved in a variety of cell functions: cell division, adherence to host cells, an...
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  4. A major determinant for gliding motility in Mycoplasma genitalium: the interaction between the terminal organelle proteins MG200 and MG491.

    Journal of Biological Chemistry 290(3):1699 (2015) PMID 25471372 PMCID PMC4340413

    Several mycoplasmas, such as the emergent human pathogen Mycoplasma genitalium, developed a complex polar structure, known as the terminal organelle (TO), responsible for a new type of cellular motility, which is involved in a variety of cell functions: cell division, adherence to host cells, an...
  5. An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.

    Journal of the American Chemical Society 136(20):7249 (2014) PMID 24785434

    Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of Ka...
  6. An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.

    Journal of the American Chemical Society 136(20):7249 (2014) PMID 24785434

    Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of Ka...
  7. Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation.

    Journal of Physical Chemistry B 118(11):2924 (2014) PMID 24568093

    Isonicotinic acid hydrazide (isoniazid or INH) is a front line antitubercular pro-drug that is converted to its active form, isonicotinyl-NAD, by the bacterial catalase-peroxidase KatG. Understanding the role of KatG in the INH activation process has been hampered by a lack of knowledge of the a...
  8. Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation.

    Journal of Physical Chemistry B 118(11):2924 (2014) PMID 24568093

    Isonicotinic acid hydrazide (isoniazid or INH) is a front line antitubercular pro-drug that is converted to its active form, isonicotinyl-NAD, by the bacterial catalase-peroxidase KatG. Understanding the role of KatG in the INH activation process has been hampered by a lack of knowledge of the a...
  9. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

    FASEB Journal 27(12):4811 (2013) PMID 23985801 PMCID PMC3834787

    Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with ...
  10. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

    FASEB Journal 27(12):4811 (2013) PMID 23985801 PMCID PMC3834787

    Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with ...
  11. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

    FASEB Journal 27(12):4811 (2013) PMID 23985801 PMCID PMC3834787

    Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with ...
  12. Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei catalase-peroxidase, KatG.

    Biochemistry (Washington) 52(41):7271 (2013) PMID 24044787

    Catalase-peroxidases or KatGs can utilize organic peroxyacids and peroxides instead of hydrogen peroxide to generate the high-valent ferryl-oxo intermediates involved in the catalase and peroxidase reactions. In the absence of peroxidatic one-electron donors, the ferryl intermediates generated w...
  13. Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei catalase-peroxidase, KatG.

    Biochemistry (Washington) 52(41):7271 (2013) PMID 24044787

    Catalase-peroxidases or KatGs can utilize organic peroxyacids and peroxides instead of hydrogen peroxide to generate the high-valent ferryl-oxo intermediates involved in the catalase and peroxidase reactions. In the absence of peroxidatic one-electron donors, the ferryl intermediates generated w...
  14. Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.

    Journal of Biological Chemistry 288(17):11907 (2013) PMID 23482565 PMCID PMC3636878

    Decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase (MCD; EC 4.1.1.9) is an essential facet in the regulation of fatty acid metabolism. The structure of human peroxisomal MCD reveals a molecular tetramer that is best described as a dimer of structural heterodimers, in which...
  15. Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.

    Journal of Biological Chemistry 288(17):11907 (2013) PMID 23482565 PMCID PMC3636878

    Decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase (MCD; EC 4.1.1.9) is an essential facet in the regulation of fatty acid metabolism. The structure of human peroxisomal MCD reveals a molecular tetramer that is best described as a dimer of structural heterodimers, in which...
  16. Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.

    Acta Crystallographica Section F 69(Pt 1):10 (2013) PMID 23295478 PMCID PMC3539695

    The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bis...
  17. Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.

    Acta Crystallographica Section F 69(Pt 1):10 (2013) PMID 23295478 PMCID PMC3539695

    The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bis...
  18. X-ray crystallography of viruses.

    Sub-Cellular Biochemistry 68:117 (2013) PMID 23737050

    For about 30 years X-ray crystallography has been by far the most powerful approach for determining virus structures at close to atomic resolutions. Information provided by these studies has deeply and extensively enriched and shaped our vision of the virus world. In turn, the ever increasing co...
  19. X-ray crystallography of viruses.

    Sub-Cellular Biochemistry 68:117 (2013) PMID 23737050

    For about 30 years X-ray crystallography has been by far the most powerful approach for determining virus structures at close to atomic resolutions. Information provided by these studies has deeply and extensively enriched and shaped our vision of the virus world. In turn, the ever increasing co...
  20. Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.

    Acta Crystallographica Section F 69(Pt 1):10 (2013) PMID 23295478 PMCID PMC3539695

    The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bis...