Effect of sulfhydryl group modification on the activities of 5-oxo-L-prolinase.

  title={Effect of sulfhydryl group modification on the activities of 5-oxo-L-prolinase.},
  author={Joanne M. Williamson and Alton Meister},
  journal={The Journal of biological chemistry},
  volume={257 15},
5-Oxo-L-prolinase was isolated from rat kidney by a new procedure; highly active and apparently homogeneous enzyme was obtained in 50% yield after 1700-fold purification. The enzyme, which couples cleavage of ATP to ADP with that of 5-oxo-L-proline to L-glutamate, is uncoupled by Ca2+, Co2+, or excess Mn2+ as well as by replacement of adenosine 5'-triphosphate or of 5-oxo-L-proline by certain analogs as previously reported. The enzyme has Mr = 325,000 and is composed of 2 apparently identical… CONTINUE READING


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