Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.

Lignende værker

• 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)
• 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.
  af: Topham, C M, et al.
  Udgivet: (1991)
• Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the papain catalytic mechanism.
  af: Brocklehurst, K, et al.
  Udgivet: (1978)
• Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.
  af: Pol, E, et al.
  Udgivet: (1995)
• Dithioesters: simple, tunable, cysteine-selective H(2)S donors
  af: Cerda, Matthew M., et al.
  Udgivet: (2018)