Chemical modification of octopine dehydrogenase by thiol-specific reagents: evidence for the presence of an essential cysteine at the catalytic site.

@article{Sheikh1993ChemicalMO,
  title={Chemical modification of octopine dehydrogenase by thiol-specific reagents: evidence for the presence of an essential cysteine at the catalytic site.},
  author={Samia O. Sheikh and Sarvagya S. Katiyar},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1202 2},
  pages={
          251-7
        }
}
Thiol-specific reagents, p-chloromercuricphenyl sulfonic acid (PCMS), 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and N-ethyl-maleimide (NEM), incubated with octopine dehydrogenase resulted in the loss of catalytic activity. The kinetic profile of PCMS inactivated enzyme showed that the reaction followed pseudo-first-order kinetics during the initial phase of inactivation. The reversal of enzyme activity was obtained by thiol-containing reagents. The loss of enzyme activity was prevented only… CONTINUE READING
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