{PDOC00417}
{PS00491; PROLINE_PEPTIDASE}
{BEGIN}
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* Aminopeptidase P and proline dipeptidase signature *
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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.

-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.

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

-Last update: December 2004 / Pattern and text revised.

[ 1] Yoshimoto T., Tone H., Honda T., Osatomi K., Kobayashi R., Tsuru D.
     "Sequencing and high expression of aminopeptidase P gene from
     Escherichia coli HB101."
     J. Biochem. 105:412-416(1989).
     PubMed=2659585
[ 2] Nakahigashi K., Inokuchi H.
     "Nucleotide sequence between the fadB gene and the rrnA operon from
     Escherichia coli."
     Nucleic Acids Res. 18:6439-6439(1990).
     PubMed=2243799
[ 3] Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I.
     "Primary structure and gene localization of human prolidase."
     J. Biol. Chem. 264:4476-4481(1989).
     PubMed=2925654
[ 4] Rawlings N.D., Barrett A.J.
     "Evolutionary families of metallopeptidases."
     Methods Enzymol. 248:183-228(1995).
     PubMed=7674922
[E1] https://www.uniprot.org/docs/peptidas

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