Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans.

@article{Laurent2001FunctionalEA,
  title={Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans.},
  author={V{\'e}ronique Laurent and Darren Brooks and David Coates and R Elwyn Isaac},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 20},
  pages={
          5430-8
        }
}
Aminopeptidase P (AP-P; X-Pro aminopeptidase; EC 3.4.11.9) cleaves the N-terminal X-Pro bond of peptides and occurs in mammals as both cytosolic and plasma membrane forms, encoded by separate genes. In mammals, the plasma membrane AP-P can function as a kininase, but little is known about the physiological role of the cytosolic enzyme. The C. elegans genome contains a single gene encoding AP-P (W03G9.4), analysis of which predicts regions displaying high levels of amino-acid sequence homology… Expand
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References

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TLDR
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TLDR
It is indicated that mammalian membrane-bound AP-P has an active-site configuration similar to that of other members of the peptidase clan MG, which is compatible with either a dual metal ion model or a single metal ion in the active site. Expand
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Western blot analysis, using an antibody generated against the recombinant protein, and Northern blot hybridization showed ubiquitous expression of the protein in different tissues with the highest expression level in the testis. Expand
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TLDR
The membrane-bound form of aminopeptidase P (aminoacylprolyl-peptide hydrolase) was purified 670-fold to apparent homogeneity from rat lung microsomes and was shown to have four binding subsites, the first three of which must be occupied for hydrolysis to occur. Expand
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The plasma membrane of many cell types contains a cohort of peptidases that serve to modulate the activity of circulating regulatory peptides. Many of these are zinc metallopeptidases and theseExpand
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TLDR
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TLDR
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TLDR
Several bioactive peptides with Xaa-Pro sequences, especially bradykinin, substance P, corticortropin-like intermediate lobe peptide, casomorphin and [Tyr]melanostatin were shortened by the N-terminal amino acid by aminopeptidase P action. Expand
Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme.
TLDR
The activity of aminopeptidase P was inhibited by chelating agents and was stimulated by Mn2+ or Co2+ ions, confirming the metallo-enzyme nature of this peptidase. Expand
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