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cgd4_2910  -  aminopeptidase

Cryptosporidium parvum Iowa II

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High impact information on cgd4_2910

  • Cryptosporidium parvum oocysts were studied for the expression of aminopeptidase by using amino acids bound to the synthetic fluorescent substrate 7-amino-4-trifluoromethyl coumarin [1].
  • With arginyl-6-amino-2-styrylquinoline as a substrate, aminopeptidase activity was observed in permeabilized oocysts and freshly excysted sporozoites but not on intact oocysts or empty oocyst membranes after excystation [1].
  • 1. Reverse transcription-polymerase chain reaction indicated that the gene for AP is expressed during sporulation, but expression is absent or greatly reduced in the sporozoites and merozoites [2].
  • The AP activity was inhibited by the AP inhibitors bestatin and 1,6-phenanthroline, but not by serine protease inhibitors [2].
  • The AP had specificity for synthetic endopeptidase substrates that contain arginine, alanine, or glycine at the N terminus [2].

Anatomical context of cgd4_2910

  • After 1 h of incubation, intact oocysts showed no activity; however, homogenization and solubilization with Triton X-114 followed by phase separation yielded a 22-fold increase in aminopeptidase activity in the detergent fraction [1].


  1. Arginine aminopeptidase, an integral membrane protein of the Cryptosporidium parvum sporozoite. Okhuysen, P.C., DuPont, H.L., Sterling, C.R., Chappell, C.L. Infect. Immun. (1994) [Pubmed]
  2. Partial purification and characterization of an aminopeptidase from Eimeria tenella. Fetterer, R.H., Miska, K.B., Barfield, R.C. J. Parasitol. (2005) [Pubmed]
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