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Information on EC 3.4.21.26 - prolyl oligopeptidase and Organism(s) Novosphingobium capsulatum and UniProt Accession Q9ZNM8
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3.4.21.26 prolyl oligopeptidaseSpecify your search results
Word Map
- 3.4.21.26
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dipeptidyl
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stroma
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cancer-associated
- aminopeptidase
- neuropeptides
- endopeptidases
- neurotensin
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proline-containing
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fapis
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biodistribution
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myofibroblasts
- flavobacterium
- celiac
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beta-propeller
- bradykinin
- trh
- dppiv
- meningosepticum
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3.4.14.5
-
18f-fdg
-
theranostic
-
exopeptidase
-
pyroglutamyl
- phosphoramidon
- amanita
- amnesia
-
carcinoma-associated
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peptidase-iv
- pharmacology
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ac-sdkp
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seven-bladed
-
gluten-free
-
suvmean
- gliadin
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n-acetyl-seryl-aspartyl-lysyl-proline
-
bispecific
-
acylpeptide
- medicine
- nutrition
- food industry
- drug development
The taxonomic range for the selected organisms is: Novosphingobium capsulatum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
prolyl oligopeptidase, fibroblast activation protein, proline endopeptidase, post-proline cleaving enzyme, prolylendopeptidase, proline-specific endopeptidase, post-proline endopeptidase, glutenase, prolyl endoprotease, pepo2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endoprolylpeptidase
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-
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peptidase, postproline endo-
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post-proline cleaving enzyme
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post-proline endopeptidase
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postproline endopeptidase
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postproline-cleaving enzyme
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-
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proline endopeptidase
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proline-specific endopeptidase
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-
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prolyl endopeptidase
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-
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additional information
the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the substrate induces an opening at the interface pf the peptidase and the beta-propeller domains while entering into the active site, concerted movements of the domains are required for enzyme activity
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Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
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CAS REGISTRY NUMBER
COMMENTARY
72162-84-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
-
-
-
?
additional information
?
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the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, the loops connecting the peptidase and propeller domains act like a hinge, holding the structure together as the domains move apart, creating a large opening, overview
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-
?
additional information
?
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ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten
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?
additional information
?
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substrate specificity with exclusion of peptides with more than 30 amino acids, overview
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-
?
additional information
?
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the enzyme cleaves at the C-terminal side of proline residues, the bacterial enzyme is also capable of cleaving Ala-Xaa and Val-Xaa bonds, no activity with large proteins with over 30 amino acids
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-
?
additional information
?
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the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Z-Pro-prolinal
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a transition state analog inhibitor, binding structure
additional information
-
no effect by SH-reagents and metal chelators
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additional information
-
structure-function relationship of inhibitors, specificity at the P2 and S3 position, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics mechanism
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
tertiary structure, overview, the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I406V
one of the mutations that shows the most significant correlation to improved activity and/or stability under simulated gastric conditions
I514V
one of the mutations that shows the most significant correlation to improved activity and/or stability under simulated gastric conditions
K103T
one of the mutations that shows the most significant correlation to improved activity and/or stability under simulated gastric conditions
M511L
one of the mutations that shows the most significant correlation to improved activity and/or stability under simulated gastric conditions
V474I
one of the mutations that shows the most significant correlation to improved activity and/or stability under simulated gastric conditions
additional information
mutants of SC PEP, variants with as much as 20% enhanced specific activity at pH 4.5 and 200fold greater resistance to pepsin are identified
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
variants with as much as 20% enhanced specific activity at pH 4.5 and 200fold greater resistance to pepsin identified
694952
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Enhancing the activity and stability of PEPs under gastric conditions (low pH, high pepsin concentration) is a challenge for protein engineers
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
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microbial PEPs are studied as potential therapeutics for celiac sprue, an inflammatory disease of the small intestine triggered by proline-rich gluten
additional information
oral therapeutic candidate for protecting celiac sprue patients from the toxic effects of dietary gluten
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kabashima, T.; Fujii, M.; Meng, Y.; Ito, K.; Yoshimoto, T.
Prolyl endopeptidase from Sphingomonas capsulata: isolation and characterization of the enzyme and nucleotide sequence of the gene
Arch. Biochem. Biophys.
358
141-148
1998
Novosphingobium capsulatum (Q9ZNM8), Novosphingobium capsulatum
Besedin, D.V.; Rudenskaya, G.N.
Proline-specific endopeptidases
Russ. J. Bioorg. Chem.
29
1-17
2003
Agaricus bisporus, Bos taurus, Cavia porcellus, Gallus gallus, Elizabethkingia meningoseptica, Oryctolagus cuniculus, Novosphingobium capsulatum, Ovis aries, Homo sapiens, Lyophyllum cinerascens, Mus musculus, Rattus norvegicus, Sus scrofa, Xanthomonas sp., Ascidia sp., Clupea pallasii, Lactifluus hygrophoroides, Russula lepida
-
Rea, D.; Fueloep, V.
Structure-function properties of prolyl oligopeptidase family enzymes
Cell Biochem. Biophys.
44
349-365
2006
Homo sapiens, Myxococcus xanthus, Pyrococcus furiosus, Trypanosoma cruzi, Novosphingobium capsulatum (Q9ZNM8)
Gass, J.; Khosla, C.
Prolyl endopeptidases
Cell. Mol. Life Sci.
64
345-355
2007
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Szeltner, Z.; Polgar, L.
Structure, function and biological relevance of prolyl oligopeptidase
Curr. Protein Pept. Sci.
9
96-107
2008
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Platyrrhini, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Garcia-Horsman, J.A.; Maennistoe, P.T.; Venaelaeinen, J.I.
On the role of prolyl oligopeptidase in health and disease
Neuropeptides
41
1-24
2007
Dictyostelium discoideum, Novosphingobium capsulatum, Flavobacterium sp., Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa (P23687)
Ehren, J.; Govindarajan, S.; Moron, B.; Minshull, J.; Khosla, C.
Protein engineering of improved prolyl endopeptidases for celiac sprue therapy
Protein Eng. Des. Sel.
21
699-707
2008
Novosphingobium capsulatum (Q9ZNM8)
Kaushik, S.; Etchebest, C.; Sowdhamini, R.
Decoding the structural events in substrate-gating mechanism of eukaryotic prolyl oligopeptidase using normal mode analysis and molecular dynamics simulations
Proteins
82
1428-1443
2014
Aeromonas caviae, Myxococcus xanthus, Sus scrofa (P23687), Sus scrofa, Novosphingobium capsulatum (Q9ZNM8)
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