A re-appraisal of the structural basis of stereochemical recognition in papain. Insensitivity of binding-site-catalytic-site signalling to P2-chirality in a time-dependent inhibition.

Lignende værker

• Dependence of the P2-S2 stereochemical selectivity of papain on the nature of the catalytic-site chemistry. Quantification of selectivity in the catalysed hydrolysis of the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides.
  af: Kowlessur, D, et al.
  Udgivet: (1990)
• The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.
  af: Kowlessur, D, et al.
  Udgivet: (1989)
• The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.
  af: Brocklehurst, K, et al.
  Udgivet: (1989)
• Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.
  af: Brocklehurst, K, et al.
  Udgivet: (1988)
• Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.
  af: Salih, E, et al.
  Udgivet: (1987)