Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.

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)
• Differences in the chemical and catalytic characteristics of two crystallographically `identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment
  Publicado em: (1988)
• Differences between the electric fields of the catalytic sites of papain and actinidin detected by using the thiol-located nitrobenzofurazan label as a spectroscopic reporter group.
  Por: Brocklehurst, K, et al.
  Publicado em: (1984)
• 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)
• Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.
  Por: Brocklehurst, K, et al.
  Publicado em: (1981)