Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation.

Lignende værker

• Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.
  af: Gul, Sheraz, et al.
  Udgivet: (2003)
• Evidence for ‘lock and key’ character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes
  af: Sonkaria, Sanjiv, et al.
  Udgivet: (2004)
• Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.
  af: Hussain, Syeed, et al.
  Udgivet: (2003)
• Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features
  af: Gul, Sheraz, et al.
  Udgivet: (2006)
• Conformational Isomerism Can Limit Antibody Catalysis
  af: Debler, Erik W., et al.
  Udgivet: (2008)