The prolyl oligopeptidase family

@article{Polgar2002ThePO,
  title={The prolyl oligopeptidase family},
  author={L. Polgár},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2002},
  volume={59},
  pages={349-362}
}
  • L. Polgár
  • Published 2002
  • Chemistry, Medicine
  • Cellular and Molecular Life Sciences CMLS
Abstract. A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze peptides containing more than about 30 residues. This group is unrelated to the classical trypsin and subtilisin families, and includes dipeptidyl peptidase IV, acylaminoacyl peptidase and oligopeptidase B, in addition to the prototype prolyl oligopeptidase. The recent crystal structure determination of prolyl oligopeptidase (80 kDa) has shown that the enzyme contains a peptidase domain with an… Expand
Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanisms
TLDR
This work has identified a new type within POP enzymes that exhibits not only unique activity but also a novel substrate-screening mechanism. Expand
Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanisms.
Serine peptidases of the prolyl oligopeptidase (POP) family are of substantial therapeutic importance because of their involvement in diseases such as diabetes, cancer, neurological diseases, andExpand
Evolutionary relationships of the prolyl oligopeptidase family enzymes.
TLDR
The phylogenetic trees indicate that the four POP family enzymes were present in the last common ancestor of all life forms and that the beta-propeller domain has been part of the family for billions of years. Expand
The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity
TLDR
Unexpectedly, the PREPL A protein did not cleave peptide substrates containing a P1 basic residue, but did slowly hydrolyse an activated ester substrate, and reacted with diisopropyl fluorophosphate, suggesting that the catalytic serine is a reactive residue. Expand
Truncated prolyl oligopeptidase from Pyrococcus furiosus
TLDR
It was concluded that the N‐terminal segment did not facilitate the substrate binding, independent of the size of the substrate, but contributed principally to the protein stability required for the formation of the proper active site. Expand
Prolyl endopeptidases
TLDR
The structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as drug targets and therapeutic agents are described. Expand
Substrate-dependent Competency of the Catalytic Triad of Prolyl Oligopeptidase*
TLDR
The catalytic competence of the Asp641 residue of the catalytic triad was studied using the D641N and D641A variants of the enzyme, and Crystal structure determination of these mutants revealed subtle perturbations related to the catalyst activity. Expand
The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed β-propeller fold
TLDR
The structure of human DPPIV is reported, especially focusing on a unique eight-bladed beta-propeller domain, and the way for the access of the substrate to this domain is discussed. Expand
Understanding the cellular role of prolyl oligopeptidase
TLDR
It has been determined that DpoA is highly similar to the mammalian enzyme and it has been demonstrated that while some variation was observed at the sequence level there is clear homology around the active site and the catalytic triad is conserved. Expand
Involvement and unusual substrate specificity of a prolyl oligopeptidase in class III lanthipeptide maturation.
TLDR
In vitro investigations of the gene cluster from Kribbella flavida, involving reconstitution of the biosynthesis of the new lanthipeptide flavipeptin, proved that a POP-type FlaP protease is responsible for leader removal and revealed that FlaP is specific to the post-translationally modified peptide and can discriminate between N- and C-terminal rings. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 144 REFERENCES
Oligopeptidase B: a new type of serine peptidase with a unique substrate-dependent temperature sensitivity.
TLDR
The kinetic analysis of the reactions of oligopeptidase B, which preferentially cleaves peptides at two adjacent basic residues, has revealed significant differences from the trypsin-like serine peptidases. Expand
Prolyl Oligopeptidase An Unusual β-Propeller Domain Regulates Proteolysis
TLDR
A resolution crystal structure of prolyl oligopeptidase, a large cytosolic enzyme that belongs to a new class of serine peptidases, is presented, which may facilitate drug design to treat memory disorders. Expand
Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
TLDR
A comparison of the relative positions of the three catalytic residues in peptidases and microbial lipases indicated structural and possibly evolutionary relationship between the two families and identified the catalytic Asp residue in the prolyl oligopeptidase family. Expand
Structures of Prolyl Oligopeptidase Substrate/Inhibitor Complexes
Structure determination of the inactive S554A variant of prolyl oligopeptidase complexed with an octapeptide has shown that substrate binding is restricted to the P4-P2′ region. In addition, it hasExpand
A potential processing enzyme in prokaryotes: Oligopeptidase B, a new type of serine peptidase
Basic amino acid pairs in polypeptides represent important markers for processing enzymes to produce biologically active products. Such enzymes related to the serine peptidase subtilisin haveExpand
Prolyl oligopeptidase from Pyrococcus furiosus.
TLDR
This chapter focuses on the POPase from the hyperthermophilic archaeon, Pyrococcus furiosus, which possesses properties unique in this class of serine proteases, including its thermal stability and its autoproteolytic activity. Expand
[15] Oligopeptidase B: Protease II from Escherichia coli
Publisher Summary This chapter highlights oligopeptidase B from Escherichia coli (E. coli protease II), with special emphasis to the structure–activity relationships, in comparison with other relatedExpand
[2] Families of serine peptidases
TLDR
This chapter examines families of serine peptidases, found in viruses, bacteria, and eukaryotes, which can be grouped together into about six clans that may have common ancestors. Expand
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
  • L. Polgár
  • Chemistry, Medicine
  • The Biochemical journal
  • 1992
TLDR
This result, combined with kinetic isotope studies, offers strong evidence that a physical step, presumably a conformational change associated with substrate binding, is the rate-determining step in the prolyl endopeptidase catalysis. Expand
Aminoacylpyrrolidine-2-nitriles: potent and stable inhibitors of dipeptidyl-peptidase IV (CD 26).
TLDR
A series of aminoacylpyrrolidine-2-nitriles, in which the carboxyl group of proline is replaced by a nitrile group, was synthesized as inhibitors of dipeptidyl- peptidase IV, demonstrating that the generally held concept that nitriles are poor inhibitors of serine proteinases needs to be reconsidered. Expand
...
1
2
3
4
5
...