Information on EC 3.4.14.12 - Xaa-Xaa-Pro tripeptidyl-peptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.14.12
-
RECOMMENDED NAME
GeneOntology No.
Xaa-Xaa-Pro tripeptidyl-peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
227604-68-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Pro-p-nitroanilide + H2O
Ala-Ala-Pro + p-nitroaniline
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-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
Ala-Phe-Pro-p-nitroanilide + H2O
Ala-Phe-Pro + p-nitroaniline
show the reaction diagram
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
show the reaction diagram
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13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
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-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
show the reaction diagram
-
22% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
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-Ala-Pro-2-naphthylamide + H2O
Gly-Ala-Pro + 2-naphthylamide
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
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide + H2O
Gly-L-Ala-Gly-L-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-L-Ala-L-Pro-4-nitroanilide + H2O
Gly-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
-
32% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
Gly-L-Ala-L-Pro-beta-naphthylamide + H2O
Gly-L-Ala-L-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
show the reaction diagram
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
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cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
interleukin 6 + H2O
?
show the reaction diagram
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cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Ala-L-Phe-L-Pro-4-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + 4-nitroaniline
show the reaction diagram
-
24% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
L-Pro-L-Pro-L-Pro + 4-nitroaniline
show the reaction diagram
-
26% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
show the reaction diagram
-
24% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Phe-Pro-p-nitroanilide + H2O
Phe-Pro + p-nitroaniline
show the reaction diagram
-
13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Pro-Asn-Pro-Asn-Gln-Gly-Asn-Phe-Ile + H2O
Pro-Asn-Pro + Asn-Gln-Gly-Asn-Phe-Ile
show the reaction diagram
-
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser-Pro + p-nitroaniline
show the reaction diagram
-
13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
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
-
-
-
-
?
Z-Gly-Ala-Pro-2-naphthylamide + H2O
Z-Gly-Ala-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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the production of prolyl tripeptidyl peptidase may contribute to the pathogenesis of periodontal tissue destruction though the mutual interaction of this enzyme, host and bacterial collagenases, and dipeptidyl peptidases in the degradation of collagen during the course of infection
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-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5 mM, 67% residual activity
3,4-dichloroisocoumarin
Ala-Ile-pyrrolidin-2-yl boronic acid
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-
Ala-Ile-pyrrolidine-2-yl boronic acid
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-
diisopropyl fluorophosphate
Pefabloc SC
Phenylmethylsulfonylfluoride
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1 mM, no residual activity
tosyl-L-lysine chloromethyl ketone
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1.0 mM, 47% inhibition
additional information
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1 mM NEM, 5 mM 1,10-phenanthroline, 1 mM EDTA, 0.2 mM E64, 0.4 mM antipain, 0.2 mM leupeptin, 1 mg/ml aprotinin, 0.2 mM bestatin or 1 mM mercaptoethanol; no inhibition by
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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5 mM, 2fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.069
Ala-Ala-Pro-p-nitroanilide
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pH 7.5, 37°C
0.17 - 0.85
Ala-Phe-Pro-beta-naphthylamide
0.129
Ala-Phe-Pro-p-nitroanilide
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pH 7.5, 37°C
0.114
Arg-Pro-p-nitroanilide
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pH 7.5, 37°C
0.17 - 0.85
Gly-Ala-Pro-2-naphthylamide
0.38 - 0.42
Gly-Ala-Pro-beta-naphthylamide
0.26
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide
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pH 6.5, 30°C
0.072
Gly-L-Ala-L-Pro-beta-naphthylamide
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pH 6.5, 30°C
0.084
Lys-Pro-p-nitroanilide
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pH 7.5, 37°C
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
43
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide
Streptomyces mobaraensis
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pH 6.5, 30°C
115
Gly-L-Ala-L-Pro-beta-naphthylamide
Streptomyces mobaraensis
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pH 6.5, 30°C
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
2.12
-
cell free extract
32.1
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purification step, after protamine sulfate treatment
74.7
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purification step, ammonium sulfate precipitation, 35-70% pellet
118
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purification step, chromatography on a Toyopearl HW65C column
160
-
purification step, chromatography on a DEAE-Toyopearl column
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
activity assay
7.2
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; activity assay, Ala-Phe-Pro-beta-naphthylamide is used as a substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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no significant activity is observed below pH 6.0 and above pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
pH 7.6, 0.2 M HEPES, stable for at least 12 h
42
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; activity assay, Ala-Phe-Pro-beta-naphthylamide is used as a substrate
50
-
significant decrease in activity above
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.17
-
calculated
10.2
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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connnected to wall through ionic interactions
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
x * 50000, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
72500
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2 * 72500, gel filtration
77000
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determined by SDS-PAGE
79390
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; calculated from amino acid sequence
82266
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2 * 83000, SDS-PAGE, 2 * 82266, calculated
83000
-
2 * 83000, SDS-PAGE, 2 * 82266, calculated
145000
-
determined by gel filtration; gel filtration
154000
-
SDS-PAGE
160000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 83000, SDS-PAGE, 2 * 82266, calculated
homodimer
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; 2 * 72500, gel filtration; 2 * 77000, SDS-PAGE
additional information
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two protein bands which represent different forms of the enzyme are detected by SDS-PAGE: 75800 Da and 81800 Da
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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sequence contains an N-terminal signal peptide of 33 amino acids followed by mature protein of 444 amino acids
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; 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
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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 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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
significant loss of stability above
60
-
5 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40°C, stable for several weeks
-
4°C, stable for 24 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Toyopearl HW65C column chromatography and DEAE-Toyopearl column chromatography; using a Toyopearl HW65C and a DEAE-Toyopearl column
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Toyoperal HW650C chromatography and DEAE-Toyopearl column chromatography; using a Toyopearl HW650C and a DEAE-Toyopearl column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells; into the pQE30 vector for transformation of Escherichia coli M15 cells
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expressed in Escherichia coli strain JM83; into the pQE30 vector, lacking the region corresponding to residues 1-38, for transformation of Escherichia coli M15 cells
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ENGINEERING
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
-
mutant for examination of the function of the glutamate residue in substrate recognition; reduced activity
S603A
-
inactive; inactive mutant
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