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PROSITE documentation PDOC00417 [for PROSITE entry PS00491]

Aminopeptidase P and proline dipeptidase signature





Description

Aminopeptidase P (EC 3.4.11.9) is the enzyme responsible for the release of any N-terminal amino acid adjacent to a proline residue. Proline dipeptidase (EC 3.4.13.9) (prolidase) splits dipeptides with a prolyl residue in the carboxyl terminal position.

Bacterial aminopeptidase P II (gene pepP) [1], proline dipeptidase (gene pepQ) [2], and human proline dipeptidase (gene PEPD) [3] are evolutionary related. These proteins are manganese metalloenzymes.

Yeast hypothetical proteins YER078c and YFR006w and Mycobacterium tuberculosis. hypothetical protein MtCY49.29c also belong to this family.

As a signature pattern for these enzymes we selected a conserved region that contains three histidine residues.

Note:

These proteins belong to family M24B in the classification of peptidases [4,E1].

Last update:

December 2004 / Pattern and text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PROLINE_PEPTIDASE, PS00491; Aminopeptidase P and proline dipeptidase signature  (PATTERN)


References

1AuthorsYoshimoto T. Tone H. Honda T. Osatomi K. Kobayashi R. Tsuru D.
TitleSequencing and high expression of aminopeptidase P gene from Escherichia coli HB101.
SourceJ. Biochem. 105:412-416(1989).
PubMed ID2659585

2AuthorsNakahigashi K. Inokuchi H.
TitleNucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli.
SourceNucleic Acids Res. 18:6439-6439(1990).
PubMed ID2243799

3AuthorsEndo F. Tanoue A. Nakai H. Hata A. Indo Y. Titani K. Matsuda I.
TitlePrimary structure and gene localization of human prolidase.
SourceJ. Biol. Chem. 264:4476-4481(1989).
PubMed ID2925654

4AuthorsRawlings N.D. Barrett A.J.
TitleEvolutionary families of metallopeptidases.
SourceMethods Enzymol. 248:183-228(1995).
PubMed ID7674922

E1Titlehttps://www.uniprot.org/docs/peptidas



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