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Information on EC 3.4.14.12 - Xaa-Xaa-Pro tripeptidyl-peptidase and Organism(s) Porphyromonas gingivalis and UniProt Accession Q7MUW6

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Porphyromonas gingivalis
UNIPROT: Q7MUW6 not found.
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The taxonomic range for the selected organisms is: Porphyromonas gingivalis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Hydrolysis of Xaa-Xaa-Pro-/-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline
Synonyms
prolyl tripeptidyl peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
prolyl tripeptidyl aminopeptidase
-
prolyl tripeptidyl peptidase
-
-
-
-
prolyltripeptidyl aminopeptidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
227604-68-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Phe-Pro-2-naphthylamide + H2O
Ala-Phe-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
Ala-Phe-Pro-beta-naphthylamide + H2O
Ala-Phe-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
Gly-Ala-Pro-2-naphthylamide + H2O
Gly-Ala-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
Gly-Ala-Pro-beta-naphthylamide + H2O
Gly-Ala-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
L-Asp-L-Ala-L-Pro-4-nitroanilide + H2O
L-Asp-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Z-Gly-Ala-Pro-2-naphthylamide + H2O
Z-Gly-Ala-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
Ala-Arg-Pro-Ala-D-Lys-amide + H2O
Ala-Arg-Pro + Ala-D-Lys-amide
show the reaction diagram
-
-
-
-
?
Ala-Phe-Pro-p-nitroanilide + H2O
Ala-Phe-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
Arg-Gly-Pro + Phe-Pro-Ile
show the reaction diagram
-
-
-
-
?
Arg-His-Pro-Lys-Tyr-Lys-Thr-Glu-Leu + H2O
Arg-His-Pro + Lys-Tyr-Lys-Thr-Glu-Leu
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
Arg-Pro-Pro + Gly-Phe
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
show the reaction diagram
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
show the reaction diagram
-
no activity
-
-
?
Gly-Val-Pro-Lys-Thr-His-Leu-Glu-Leu + H2O
Gly-Val-Pro + Lys-Thr-His-Leu-Glu-Leu
show the reaction diagram
-
-
-
-
?
Human cystatin C + H2O
?
show the reaction diagram
-
cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
interleukin 6 + H2O
?
show the reaction diagram
-
cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
Pro-Asn-Pro-Asn-Gln-Gly-Asn-Phe-Ile + H2O
Pro-Asn-Pro + Asn-Gln-Gly-Asn-Phe-Ile
show the reaction diagram
-
-
-
-
?
Val-Glu-Pro-Ile-Pro-Tyr + H2O
Val-Glu-Pro + Ile-Pro-Tyr
show the reaction diagram
-
-
-
-
?
Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys + H2O
Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys
show the reaction diagram
-
-
-
-
?
Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys-Glu-Val-Ala-Ala-Pro-His-Arg-Gln + H2O
Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys-Glu-Val-Ala-Ala-Pro-His-Arg-Gln
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ala-Ile-pyrrolidin-2-yl boronic acid
-
Ala-Ile-pyrrolidine-2-yl boronic acid
-
3,4-dichloroisocoumarin
diisopropyl fluorophosphate
-
10 mM, complete inhibition
Pefabloc SC
-
80% inhibition at 1 mg/ml and complete inhibition at 10 mg/ml
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
5 mM, 2fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 0.85
Ala-Phe-Pro-beta-naphthylamide
0.17 - 0.85
Gly-Ala-Pro-2-naphthylamide
0.38 - 0.42
Gly-Ala-Pro-beta-naphthylamide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8 - 511
Ala-Phe-Pro-beta-naphthylamide
2.65 - 511
Gly-Ala-Pro-2-naphthylamide
2.65 - 354
Gly-Ala-Pro-beta-naphthylamide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000881 - 0.0488
Ala-Ile-pyrrolidin-2-yl boronic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
118
purification step, chromatography on a Toyopearl HW65C column
160
purification step, chromatography on a DEAE-Toyopearl column
2.12
cell free extract
32.1
purification step, after protamine sulfate treatment
74.7
purification step, ammonium sulfate precipitation, 35-70% pellet
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
pH 7.6, 0.2 M HEPES, stable for at least 12 h
37
-
pH 7.6, 0.2 M HEPES, stable for at least 12 h
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.17
-
calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
72500
2 * 72500, gel filtration
77000
determined by SDS-PAGE
79390
160000
-
gel filtration
82266
-
2 * 83000, SDS-PAGE, 2 * 82266, calculated
83000
-
2 * 83000, SDS-PAGE, 2 * 82266, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
dimer
-
2 * 83000, SDS-PAGE, 2 * 82266, calculated
additional information
-
two protein bands which represent different forms of the enzyme are detected by SDS-PAGE: 75800 Da and 81800 Da
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, with 1.1 M potassium/sodium tartrate, 100 mM Ches buffer (pH 9.0), and 200 mM lithium sulfate
hanging drop vapour diffusion method, with 100 mM Ches (pH 9.0), 1.1 M potassium/sodium tartrate, 200 mM lithium sulfate
the structure of the ligand-free enzyme is solved at 2.1 A resolution, the structure of the S603A mutant-substrate complex is solved at 2.9 A resolution
the structure of the prolyl tripeptidyl aminopeptidase complexed with the inhibitor is determined at 2.2 A resolution, the structure of the mutant E636A at 2.0 A, and in complex with the inhibitor at 1.95 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E205A
mutant for examination of the function of the glutamate residue in substrate recognition, mutant expressed in inclusion bodies
E205Q
mutant for examination of the function of the glutamate residue in substrate recognition, mutant expressed in soluble form, no activity detected
E636A
S603A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Toyopearl HW65C column chromatography and DEAE-Toyopearl column chromatography
Toyoperal HW650C chromatography and DEAE-Toyopearl column chromatography
using a Toyopearl HW650C and a DEAE-Toyopearl column
using a Toyopearl HW65C and a DEAE-Toyopearl column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
expressed in Escherichia coli strain JM83
into the pQE30 vector for transformation of Escherichia coli M15 cells
into the pQE30 vector, lacking the region corresponding to residues 1-38, for transformation of Escherichia coli M15 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
continuous assay for endoprotease activity of meprin alpha and beta using prolyl tripeptidyl aminopeptidase and the chromogenic substrate KKGYVADAP-p-nitroanilide
synthesis
strategy for expression and onestep-purification of the prolyl tripeptidyl peptidase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banbula, A.; Mak, P.; Bugno, M.; Silberring, J.; Dubin, A.; Nelson, D.; Travis, J.; Potempa, J.
Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of peridontitis
J. Biol. Chem.
274
9246-9252
1999
Porphyromonas gingivalis
Manually annotated by BRENDA team
Nakajima, Y.; Ito, K.; Xu, Y.; Yamada, N.; Onohara, Y.; Ito, T.; Yoshimoto, T.
Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis
Acta Crystallogr. Sect. F
F61
1046-1048
2005
Porphyromonas gingivalis
Manually annotated by BRENDA team
Ito, K.; Nakajima, Y.; Xu, Y.; Yamada, N.; Onohara, Y.; Ito, T.; Matsubara, F.; Kabashima, T.; Nakayama, K.; Yoshimoto, T.
Crystal structure and mechanism of tripeptidyl activity of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis
J. Mol. Biol.
362
228-240
2006
Porphyromonas gingivalis (Q7MUW6)
Manually annotated by BRENDA team
Xu, Y.; Nakajima, Y.; Ito, K.; Zheng, H.; Oyama, H.; Heiser, U.; Hoffmann, T.; Gaertner, U.T.; Demuth, H.U.; Yoshimoto, T.
Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism
J. Mol. Biol.
375
708-719
2008
Porphyromonas gingivalis (Q7MUW6)
Manually annotated by BRENDA team
Schulze, A.; Wermann, M.; Demuth, H.U.; Yoshimoto, T.; Ramsbeck, D.; Schlenzig, D.; Schilling, S.
Continuous assays for meprin alpha and beta using prolyl tripeptidyl aminopeptidase (PtP) from Porphyromonas gingivalis
Anal. Biochem.
559
11-16
2018
Porphyromonas gingivalis, Porphyromonas gingivalis (Q7MUW6)
Manually annotated by BRENDA team