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pig-ppce

Pig prolyl endopeptidase

Comment

Relationship

Family : S9N_PPCE_Peptidase_S9

Block : X

Position in NCBI Life Tree : Sus scrofa

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)

> cellular organisms N E > Eukaryota N E > Opisthokonta N E > Metazoa N E > Eumetazoa N E > Bilateria N E > Deuterostomia N E > Chordata N E > Craniata N E > Vertebrata N E > Gnathostomata N E > Teleostomi N E > Euteleostomi N E > Sarcopterygii N E > Dipnotetrapodomorpha N E > Tetrapoda N E > Amniota N E > Mammalia N E > Theria N E > Eutheria N E > Boreoeutheria N E > Laurasiatheria N E > Cetartiodactyla N E > Suina N E > Suidae N E > Sus N E > Sus scrofa N E

Molecular evidence

1E5T - Prolyl oligopeptidase from C255T\/Q397C\/K684M pig mutant 1E8M - Prolyl oligopeptidase from pig brain mutant covalently bound Z pro prolinal 1E8N - Prolyl oligopeptidase from pig brain mutant covalently bound octapeptide 1H2W - Prolyl Oligopeptidase From Porcine Brain 1H2X - Prolyl Oligopeptidase From Porcine Brain, Y473F Mutant 1H2Y - Prolyl Oligopeptidase From Porcine Brain, Y473F Mutant With Covalently Bound Inhibitor Z-Pro-Prolinal 1H2Z - Prolyl Oligopeptidase From Porcine Brain, S554A Mutant With Bound Peptide Ligand Suc-Gly-Pro 1O6F - Prolyl Oligopeptidase From Porcine Brain, D641A Mutant With Bound Peptide Ligand Suc-Gly-Pro 1O6G - Prolyl Oligopeptidase From Porcine Brain, D641N Mutant With Bound Peptide Ligand Suc-Gly-Pro 1QFM - Prolyl oligopeptidase from pig 1QFS - Prolyl oligopeptidase with covalently bound inhibitor Z-pro-prolinal from pig 1UOO - Prolyl Oligopeptidase From Porcine Brain, S554A Mutant With Bound Peptide Ligand Gly-Phe-Arg-Pro 1UOP - Prolyl Oligopeptidase From Porcine Brain, S554A Mutant With Bound Peptide Ligand Gly-Phe-Glu-Pro 1UOQ - Prolyl Oligopeptidase From Porcine Brain, S554A Mutant With Bound Peptide Ligand Glu-Phe-Ser-Pro 1VZ2 - Prolyl oligopeptidase from porcine brain Y73C\/V427C\/C255T mutant 1VZ3 - Prolyl oligopeptidase from porcine brain T597C mutant 2XDW - Inhibition of Prolyl Oligopeptidase with a Synthetic Unnatural Dipeptide 3EQ7 - Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors 1 3EQ8 - Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors 2 3EQ9 - Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors 3 4AMY - Prolyl Oligopeptidase from porcine brain with a covalently bound inhibitor IC-1 4AMZ - Prolyl Oligopeptidase from porcine brain with a covalently bound inhibitor IC-2 4AN0 - Prolyl Oligopeptidase from porcine brain with a covalently bound inhibitor IC-3 4AN1 - Prolyl Oligopeptidase from porcine brain with a covalently bound inhibitor IC-4 4AX4 - Prolyl Oligopeptidase from porcine brain, H680A mutant 4BCB - Prolyl Oligopeptidase from porcine brain with a covalently bound P2- substituted N-acyl-prolylpyrrolidine inhibitor 1 4BCC - Prolyl Oligopeptidase from porcine brain with a covalently bound P2-substituted N-acyl-prolylpyrrolidine inhibitor 2 4BCD - Prolyl Oligopeptidase from porcine brain with a non-covalently bound P2- substituted N-acyl-prolylpyrrolidine inhibitor 3

No kinetic

No disease

Database

Sequence

Peptide

MLSFQYPDVY RDETAIQDYH GHKVCDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNILS DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFSCMAWTH DGKGMFYNAY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS IREGCDPVNR LWYCDLQQES NGITGILKWV KLIDNFEGEY DYVTNEGTVF TFKTNRHSPN YRLINIDFTD PEESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNT LQLHDLATGA LLKIFPLEVG SVVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI NGGSNGGLLV ATCANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG CSDSKQHFEW LIKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIDWIP

References (13)

Title : Substrate-like novel inhibitors of prolyl specific oligo peptidase for neurodegenerative disorders - Khan_2023_J.Biomol.Struct.Dyn__1
Author(s) : Khan M , Halim SA , Waqas M , Golmohammadi F , Balalaie S , Csuk R , Uddin J , Khan A , Al-Harrasi A
Ref : J Biomol Struct Dyn , :1 , 2023
Abstract :
PubMedSearch : Khan_2023_J.Biomol.Struct.Dyn__1
PubMedID: 37608559
Gene_locus related to this paper: pig-ppce

Title : P2-substituted N-acylprolylpyrrolidine inhibitors of prolyl oligopeptidase: biochemical evaluation, binding mode determination, and assessment in a cellular model of synucleinopathy - Van der Veken_2012_J.Med.Chem_55_9856
Author(s) : Van der Veken P , Fulop V , Rea D , Gerard M , Van Elzen R , Joossens J , Cheng JD , Baekelandt V , De Meester I , Lambeir AM , Augustyns K
Ref : Journal of Medicinal Chemistry , 55 :9856 , 2012
Abstract :
PubMedSearch : Van der Veken_2012_J.Med.Chem_55_9856
PubMedID: 23121075
Gene_locus related to this paper: pig-ppce

Title : The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity - Szeltner_2012_Biochim.Biophys.Acta_1834_98
Author(s) : Szeltner Z , Juhasz T , Szamosi I , Rea D , Fulop V , Modos K , Juliano L , Polgar L
Ref : Biochimica & Biophysica Acta , 1834 :98 , 2012
Abstract :
PubMedSearch : Szeltner_2012_Biochim.Biophys.Acta_1834_98
PubMedID: 22940581
Gene_locus related to this paper: pig-ppce

Title : Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase. - Kaszuba_2012_Biochimie_94_1398
Author(s) : Kaszuba K , Rog T , Danne R , Canning P , Fulop V , Juhasz T , Szeltner Z , St Pierre JF , Garcia-Horsman A , Mannisto PT , Karttunen M , Hokkanen J , Bunker A
Ref : Biochimie , 94 :1398 , 2012
Abstract :
PubMedSearch : Kaszuba_2012_Biochimie_94_1398
PubMedID: 22484394
Gene_locus related to this paper: pig-ppce

Title : Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide - Racys_2010_Bioorg.Med.Chem_18_4775
Author(s) : Racys DT , Rea D , Fulop V , Wills M
Ref : Bioorganic & Medicinal Chemistry , 18 :4775 , 2010
Abstract :
PubMedSearch : Racys_2010_Bioorg.Med.Chem_18_4775
PubMedID: 20627594
Gene_locus related to this paper: pig-ppce

Title : Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding - Szeltner_2003_J.Biol.Chem_278_48786
Author(s) : Szeltner Z , Rea D , Renner V , Juliano L , Fulop V , Polgar L
Ref : Journal of Biological Chemistry , 278 :48786 , 2003
Abstract :
PubMedSearch : Szeltner_2003_J.Biol.Chem_278_48786
PubMedID: 14514675
Gene_locus related to this paper: pig-ppce

Title : Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site - Szeltner_2002_J.Biol.Chem_277_42613
Author(s) : Szeltner Z , Rea D , Renner V , Fulop V , Polgar L
Ref : Journal of Biological Chemistry , 277 :42613 , 2002
Abstract :
PubMedSearch : Szeltner_2002_J.Biol.Chem_277_42613
PubMedID: 12202494
Gene_locus related to this paper: pig-ppce

Title : Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase - Szeltner_2002_J.Biol.Chem_277_44597
Author(s) : Szeltner Z , Rea D , Juhasz T , Renner V , Mucsi Z , Orosz G , Fulop V , Polgar L
Ref : Journal of Biological Chemistry , 277 :44597 , 2002
Abstract :
PubMedSearch : Szeltner_2002_J.Biol.Chem_277_44597
PubMedID: 12228249
Gene_locus related to this paper: pig-ppce

Title : Structures of prolyl oligopeptidase substrate\/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue - Fulop_2001_J.Biol.Chem_276_1262
Author(s) : Fulop V , Szeltner Z , Renner V , Polgar L
Ref : Journal of Biological Chemistry , 276 :1262 , 2001
Abstract :
PubMedSearch : Fulop_2001_J.Biol.Chem_276_1262
PubMedID: 11031266
Gene_locus related to this paper: pig-ppce

Title : Catalysis of serine oligopeptidases is controlled by a gating filter mechanism - Fulop_2000_EMBO.Rep_1_277
Author(s) : Fulop V , Szeltner Z , Polgar L
Ref : EMBO Rep , 1 :277 , 2000
Abstract :
PubMedSearch : Fulop_2000_EMBO.Rep_1_277
PubMedID: 11256612
Gene_locus related to this paper: pig-ppce

Title : Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis - Fulop_1998_Cell_94_161
Author(s) : Fulop V , Bocskei Z , Polgar L
Ref : Cell , 94 :161 , 1998
Abstract :
PubMedSearch : Fulop_1998_Cell_94_161
PubMedID: 9695945
Gene_locus related to this paper: pig-ppce

Title : cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue - Rennex_1991_Biochemistry_30_2195
Author(s) : Rennex D , Hemmings BA , Hofsteenge J , Stone SR
Ref : Biochemistry , 30 :2195 , 1991
Abstract :
PubMedSearch : Rennex_1991_Biochemistry_30_2195
PubMedID: 1900195
Gene_locus related to this paper: pig-ppce

Title : Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification - Stone_1991_Biochem.J_276 ( Pt 3)_837
Author(s) : Stone SR , Rennex D , Wikstrom P , Shaw E , Hofsteenge J
Ref : Biochemical Journal , 276 ( Pt 3) :837 , 1991
Abstract :
PubMedSearch : Stone_1991_Biochem.J_276 ( Pt 3)_837
PubMedID: 2064618
Gene_locus related to this paper: pig-ppce