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PROSITE documentation PDOC00417

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.

Technical section:

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

PROLINE_PEPTIDASE, PS00491; Aminopeptidase P and proline dipeptidase signature  (PATTERN)
Consensus pattern: [HA]-[GSYR]-[LIVMT]-[SG]-H-x-[LIV]-G-[LIVMNKS]-x-[IVEL]-[HNC]-[DEV]
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00491
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00491
• Scan Swiss-Prot/TrEMBL entries against PS00491
• view ligand binding statistics
Matching PDB structures: 1A16 1JAW 1M35 1N51 ... [ALL]

References:

1 AuthorsYoshimoto 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
2 AuthorsNakahigashi 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
3 AuthorsEndo 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
4 AuthorsRawlings N.D., Barrett A.J.
TitleEvolutionary families of metallopeptidases.
SourceMethods Enzymol. 248:183-228(1995).
PubMed ID7674922
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?peptidas.txt

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