Now showing items 1-8 of 8

    • Chemical Modification of a Dehydratase Enzyme Involved in Bacterial Virulence by an Ammonium Derivative: Evidence of its Active Site Covalent Adduct 

      González Bello, Concepción; Tizón, Lorena; Lence Quintana, Emilio José; Otero Casas, José Manuel; Raaij, Mark J. van; Martínez Guitián, Marta; Beceiro Casas, Alejandro; Thompson, Paul; Hawkins, Alastair R. (American Chemical Society, 2015)
      The first example of an ammonium derivative that causes a specific modification of the active site of type I dehydroquinase (DHQ1), a dehydratase enzyme that is a promising target for antivirulence drug discovery, is ...
    • Exploring the Water-Binding Pocket of the Type II Dehydroquinase Enzyme in the Structure-Based Design of Inhibitors 

      Blanco Rodríguez, Beatriz; Sedes, Antía; Peón López, Antonio; Otero Casas, José Manuel; Raaij, Mark J. van; Thompson, Paul; Hawkins, Alastair R.; González Bello, Concepción (American Chemical Society, 2014)
      Structural and computational studies to explore the WAT1 binding pocket in the structure-based design of inhibitors against the type II dehydroquinase (DHQ2) enzyme are reported. The crystal structures of DHQ2 from M. ...
    • Hydroxylammonium derivatives for selective active-site lysine modification in the anti-virulence bacterial target DHQ1 enzyme 

      Maneiro Rey, María; Lence Quintana, Emilio José; Sanz Gaitero, Marta; Otero Casas, José Manuel; Raaij, Mark J. van; Thompson, Paul; Hawkins, Alastair R.; González Bello, Concepción (Royal Society of Chemistry, 2019)
      Targeted irreversible inhibitors bearing electrophiles that become activated towards covalent bond formation upon binding to a specific protein/enzyme is an emerging area in drug discovery. Targeting lysine residues is ...
    • Insights into substrate binding and catalysis in bacterial type I dehydroquinase 

      Maneiro Rey, María; Peón López, Antonio; Lence Quintana, Emilio José; Otero Casas, José Manuel; Raaij, Mark J. van; Thompson, Paul; Hawkins, Alastair R.; González Bello, Concepción (Portland Press, 2014-09-15)
      Structural, biochemical and computational studies to study substrate binding and the role of the conserved residues of the DHQ1 (type I dehydroquinase) enzyme active site are reported in the present paper. The crystal ...
    • Irreversible covalent modification of type I dehydroquinase with a stable Schiff base 

      Tizón, Lorena; Maneiro Rey, María; Peón López, Antonio; Otero Casas, José Manuel; Lence Quintana, Emilio José; Poza, Sergio; Raaij, Mark J. van; Thompson, Paul; Hawkins, Alastair R.; González Bello, Concepción (Royal Society of Chemistry, 2015)
      The irreversible inhibition of type I dehydroquinase (DHQ1), the third enzyme of the shikimic acid pathway, is investigated by structural, biochemical and computational studies. Two epoxides, which are mimetics of the ...
    • Mechanistic Basis of the Inhibition of Type II Dehydroquinase by (2S)- and (2R)-2-Benzyl-3-dehydroquinic Acids 

      Lence Quintana, Emilio José; Tizón, Lorena; Otero Casas, José Manuel; Peón López, Antonio; Prazeres, Verónica F. V.; Llamas Saiz, Antonio Luis; Fox, Gavin V.; Raaij, Mark J. van; Lamb, Heather; Hawkins, Alastair R.; González Bello, Concepción (American Chemical Society, 2013)
      The structural changes caused by the substitution of the aromatic moiety in (2S)-2-benzyl-3-dehydroquinic acids and its epimers in C2 by electron-withdrawing or electron-donating groups in type II dehydroquinase enzyme ...
    • Mycobacterium tuberculosis Shikimate Kinase Inhibitors: Design and Simulation Studies of the Catalytic Turnover 

      Blanco Rodríguez, Beatriz; Prado, Verónica; Lence Quintana, Emilio José; Otero Casas, José Manuel; García Doval, Carmela; Raaij, Mark J. van; Llamas Saiz, Antonio Luis; Lamb, Heather; Hawkins, Alastair R.; González Bello, Concepción (American Chemical Society, 2013)
      Shikimate kinase (SK) is an essential enzyme in several pathogenic bacteria and does not have any counterpart in human cells, thus making it an attractive target for the development of new antibiotics. The key interactions ...
    • Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone 

      García Doval, Carmela; Castón, José R.; Luque, Daniel; Granell, Meritxell; Otero Casas, José Manuel; Llamas Saiz, Antonio Luis; Renouard, Madalena; Boulanger, Pascale; Raaij, Mark J. van (MDPI, 2015)
      Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell ...





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