Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.

Míreanna Comhchosúla

• 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.
  le: Kowlessur, D, et al.
  Foilsithe: (1989)
• Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase omega.
  le: Brocklehurst, K, et al.
  Foilsithe: (1985)
• Comparative resonance Raman spectroscopic and kinetic studies of acyl-enzymes involving papain, actinidin and papaya peptidase II.
  le: Brocklehurst, K, et al.
  Foilsithe: (1984)
• The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain.
  le: Brocklehurst, K, et al.
  Foilsithe: (1989)
• Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin.
  le: Lindahl, P, et al.
  Foilsithe: (1992)