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 R 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… 

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  • 2007
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Characterization of Aminopeptidase in the Free-living Nematode Panagrellus redivivus: Subcellular Distribution and Possible Role in Neuropeptide Metabolism

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References

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It is proposed that human cytosolic AP-P is a single metal ion-dependent enzyme and that manganese is most likely the metal ion used in vivo.

Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.

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.

Purification and properties of membrane-bound aminopeptidase P from rat lung.

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.

Structural studies of aminopeptidase P. A novel cellular peptidase.

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 these

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  • Chemistry, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1998
The structure of the proline-specific aminopeptidase from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions.

Aminopeptidase P from human leukocytes.

The observed resistance of Gly-Pro,pro-Gly, Pro-Phe and Pro-Ile to hydrolysis by the purified enzyme strongly indicates absence of known proline-specific dipeptidases in the aminopeptidase-P preparation.

Aminopeptidase P from rat brain. Purification and action on bioactive peptides.

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.

Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme.

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.