Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.

@article{Brocklehurst1987SubstratederivedTE,
  title={Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.},
  author={K. Brocklehurst and D. Kowlessur and M. O'driscoll and G. Patel and S. Quenby and E. Salih and W. Templeton and E. Thomas and F. Willenbrock},
  journal={The Biochemical journal},
  year={1987},
  volume={244 1},
  pages={
          173-81
        }
}
1. 2-(N'-Acetyl-L-phenylalanylamino)ethyl 2'-pyridyl disulphide [compound (III)] and 2-(acetamido)ethyl 2'-pyridyl disulphide [compound (IV)] were synthesized by acylation of the common intermediate, 2-aminoethyl 2'-pyridyl disulphide, to provide examples of chromogenic thiol-specific substrate-derived two-protonic-state electrophilic probe reagents. These two reagents, together with n-propyl 2-pyridyl disulphide [compound (II)], provide structural variation in the non-pyridyl part of the… Expand
Reversible binding of peptide aldehydes to papain. Structure-activity relationships.
Cysteinyl proteinases and their selective inactivation.
  • E. Shaw
  • Chemistry, Medicine
  • Advances in enzymology and related areas of molecular biology
  • 1990
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