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.

Benzer Materyaller

• Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.
  Yazar:: Reid, J D, ve diğerleri
  Baskı/Yayın Bilgisi: (2001)
• A computational analysis of SARS cysteine proteinase-octapeptide substrate interaction: implication for structure and active site binding mechanism
  Yazar:: Phakthanakanok, Krongsakda, ve diğerleri
  Baskı/Yayın Bilgisi: (2009)
• Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.
  Yazar:: Gul, Sheraz, ve diğerleri
  Baskı/Yayın Bilgisi: (2003)
• Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium smegmatis Cysteine Ligase (MshC)
  Yazar:: Fan, Fan, ve diğerleri
  Baskı/Yayın Bilgisi: (2007)
• 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.
  Yazar:: Brocklehurst, K, ve diğerleri
  Baskı/Yayın Bilgisi: (1978)