Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain.

Registos relacionados

• 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.
  Por: Kowlessur, D, et al.
  Publicado em: (1989)
• The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.
  Por: Brocklehurst, K, et al.
  Publicado em: (1989)
• 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.
  Por: Templeton, W, et al.
  Publicado em: (1990)
• Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.
  Por: Brocklehurst, K, et al.
  Publicado em: (1988)
• 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.
  Por: Kowlessur, D, et al.
  Publicado em: (1990)