Pleiotropic enzyme activities of genetically engineered human prolidase

Qing Ding Wang, Mu Gen Chi, Qian Li, Man Ji Sun

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


AIM: To investigate whether the human prolidase possesses the G-type organophosphate hydrolyzing enzyme(Gase) activity besides its ability to catalyze the hydrolysis of the dipeptides bearing a proline residue at the C-terminus. METHODS: Genetic engineering techniques were used in the cloning and expression of the recombinant human prolidase. Prolidase and Gase activities were assayed in the conventional ways. RESULTS: The recombinant human prolidase expressed in COS-7 cells catalyzed the hydrolysis of organophosphorous compound soman as well as the hydrolysis of dipeptide Gly-Pro. Both activities were two-folds higher than that in the non-transformed COS-7 counterpart. Comparison between the two activities in COS-7 cells transfected with the recombinant vector containing the prolidase gene and the control cells showed parallel elevation with a constant ratio. CONCLUSION: It is infered that the Gase and the prolidase are of the same enzyme, or at least belong to isozyme.

Original languageEnglish
Pages (from-to)380-383
Number of pages4
JournalChinese Journal of Pharmacology and Toxicology
Issue number5
StatePublished - Oct 2003


  • Dipeptides
  • Human
  • Hydrolases, organophosphorous compounds
  • Liver
  • Prolidase
  • Soman

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology


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