Evidence that binding to the S(2)-subsite of papain may be coupled with catalytically relevant structural change involving the cysteine-25–histidine-159 diad. Kinetics of the reaction of papain with a two-protonic-state reactivity probe containing a hydrophobic side chain

Ítems similars

• Challenging a Paradigm: Theoretical Calculations of the Protonation State of the Cys25-His159 Catalytic Diad in Free Papain
  per: Shokhen, Michael, et al.
  Publicat: (2009)
• Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.
  per: Shipton, M, et al.
  Publicat: (1978)
• 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.
  per: Brocklehurst, K, et al.
  Publicat: (1978)
• Reactivities of the various protonic states in the reactions of papain and of L-cysteine with 2,2'- and with 4,4'- dipyridyl disulphide: evidence for nucleophilic reactivity in the un-ionized thiol group of the cysteine-25 residue of papain occasioned by its interaction with the histidine-159-asparagine-175 hydrogen-bonded system.
  per: Brocklehurst, K, et al.
  Publicat: (1972)
• The specificity of the S(1) subsite of papain
  per: Alecio, M. Robert, et al.
  Publicat: (1974)