{PDOC00587}
{PS00708; PRO_ENDOPEP_SER}
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* Prolyl oligopeptidase family serine active site *
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The prolyl oligopeptidase family [1,2,3] consist  of  a number of evolutionary
related peptidases whose catalytic  activity seems  to be provided by a charge
relay system similar to  that of the trypsin family of  serine  proteases, but
which evolved by independent convergent evolution.   The known members of this
family are listed below.

 - Prolyl endopeptidase (EC 3.4.21.26) (PE) (also called post-proline cleaving
   enzyme). PE is an enzyme that cleaves peptide bonds on  the C-terminal side
   of prolyl residues. The sequence of PE has been obtained  from  a mammalian
   species (pig)   and   from  bacteria  (Flavobacterium  meningosepticum  and
   Aeromonas hydrophila);  there  is  a  high  degree of sequence conservation
   between these sequences.
 - Escherichia  coli protease II (EC 3.4.21.83) (oligopeptidase B) (gene prtB)
   which cleaves  peptide  bonds on the C-terminal side of lysyl and argininyl
   residues.
 - Dipeptidyl peptidase IV (EC 3.4.14.5) (DPP IV).   DPP IV is  an enzyme that
   removes  N-terminal   dipeptides  sequentially   from  polypeptides  having
   unsubstituted N-termini provided that the penultimate residue is proline.
 - Yeast vacuolar dipeptidyl aminopeptidase A (DPAP A) (gene: STE13)  which is
   responsible for the proteolytic maturation of the alpha-factor precursor.
 - Yeast vacuolar dipeptidyl aminopeptidase B (DPAP B) (gene: DAP2).
 - Acylamino-acid-releasing  enzyme  (EC 3.4.19.1)  (acyl-peptide  hydrolase).
   This enzyme catalyzes the hydrolysis of  the amino-terminal peptide bond of
   an N-acetylated protein to generate a N-acetylated amino acid and a protein
   with a free amino-terminus.

A conserved serine residue has experimentally  been  shown (in E.coli protease
II as well  as  in  pig  and bacterial PE)  to  be necessary for the catalytic
mechanism. This serine, which is part of the catalytic  triad (Ser, His, Asp),
is generally located  about 150 residues away from the C-terminal extremity of
these enzymes  (which  are  all proteins  that contains about 700 to 800 amino
acids).

-Consensus pattern: D-x(3)-A-x(3)-[LIVMFYW]-x(14)-G-x-S-x-G-G-[LIVMFYW](2)
                    [S is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for yeast DPAP A.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These  proteins belong to families S9A/S9B/S9C in the classification of
 peptidases [4,E1].

-Last update: November 1997 / Text revised.

[ 1] Rawlings N.D., Polgar L., Barrett A.J.
     "A new family of serine-type peptidases related to prolyl
     oligopeptidase."
     Biochem. J. 279:907-908(1991).
     PubMed=1953688
[ 2] Barrett A.J., Rawlings N.D.
     "Oligopeptidases, and the emergence of the prolyl oligopeptidase
     family."
     Biol. Chem. Hoppe-Seyler 373:353-360(1992).
     PubMed=1515061
[ 3] Polgar L., Szabo E.
     "Prolyl endopeptidase and dipeptidyl peptidase IV are distantly
     related members of the same family of serine proteases."
     Biol. Chem. Hoppe-Seyler 373:361-366(1992).
     PubMed=1355343
[ 4] Rawlings N.D., Barrett A.J.
     "Families of serine peptidases."
     Methods Enzymol. 244:19-61(1994).
     PubMed=7845208
[E1] https://www.uniprot.org/docs/peptidas

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