Information on EC 3.4.19.3 - pyroglutamyl-peptidase I

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.4.19.3
-
RECOMMENDED NAME
GeneOntology No.
pyroglutamyl-peptidase I
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-21-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MFO
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
show the reaction diagram
5-pyrrolidone-2-carboxyl-His-Gly + H2O
?
show the reaction diagram
-
slight activity
-
-
?
5-pyrrolidone-2-carboxyl-His-Trp + H2O
?
show the reaction diagram
-
-
-
-
?
ACE inhibitor + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Trp-
-
?
acid-thyroliberin + H2O
pyroglutamate + His-Pro
show the reaction diagram
bombesin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Arg-
-
?
bombesin + H2O
pyroglutamate + Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
show the reaction diagram
bradykinin potentiator + H2O
pyroglutamate + ?
show the reaction diagram
bradykinin potentiator B + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Gly-
-
?
bradykinin-potentiating peptide B + H2O
?
show the reaction diagram
-
cleavage of the peptide bond adjacent to the pyroglutamic residue
-
-
?
ethyl L-pyroglutamate + H2O
L-pyroglutamate + ethanol
show the reaction diagram
Fibrinogen + H2O
?
show the reaction diagram
-
bovine fribrinogen
-
-
?
Glu(OMe)2-litorin + H2O
pyroglutamate + ?
show the reaction diagram
-
-
-
?
gonadotropin-releasing hormone + H2O
?
show the reaction diagram
hydrolyzed exclusively at the pyroglutamyl-/-Xaa bond
-
-
?
L-2-oxoimidazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
L-2-oxooxazolidine-4-carboxyl-aminoethylnitrate + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxooxazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
L-2-oxothiazolidine-4-carboxyl-D-2-aminopropylnitrate + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxothiazolidine-4-carboxyl-ethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxothiazolidine-4-carboxyl-L-2-aminopropylnitrate + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxothiazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
L-pyroglutamic acid 2-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-pyroglutamyl-aminoethylnitrate + H2O
?
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
show the reaction diagram
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphtylamine
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
show the reaction diagram
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphtylamine
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-His-Pro-4-methylcoumarin 7-amide + H2O
L-pyroglutamate + His-Pro-4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-L-Ala + H2O
L-pyroglutamate + L-Ala
show the reaction diagram
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
show the reaction diagram
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutaminic acid + p-nitroaniline
show the reaction diagram
-
-
-
?
L-pyrrolidonyl 2-naphthylamide + H2O
5-oxo-L-proline + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
leukopyrokinin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Thr-
-
?
litorin + H2O
pyroglutamate + Gln-Trp-Ala-Val-Gly-His-Phe-Met-NH2
show the reaction diagram
luliberin + H2O
pyroglutamate + His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
show the reaction diagram
luteinizing hormone releasing hormone + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-His-
-
?
luteinizing-hormone-releasing hormone + H2O
?
show the reaction diagram
N-(4-methyl-2-oxo-2H-chromen-7-yl)-5-oxo-L-prolinamide + H2O
5-oxo-L-proline + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Leu-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
show the reaction diagram
oxoimidazolidinyl-4-carbonyl-Gly-Ile + H2O
?
show the reaction diagram
-
-
-
-
?
physalaemin + H2O
pyroglutamate + Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2
show the reaction diagram
pyroglutamic acid-7-amido-4-methylcoumarin + H2O
L-pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pyroglutamyl-2-naphthylamide + H2O
pyroglutamate + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
pyroglutamyl-4-methylcoumaryl-7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
pyroglutamyl-4-methylumbelliferyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Ala + H2O
pyroglutamate + Ala
show the reaction diagram
pyroglutamyl-Arg + H2O
pyroglutamate + Arg
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Asp + H2O
pyroglutamate + Asp
show the reaction diagram
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
show the reaction diagram
pyroglutamyl-D-Ala + H2O
pyroglutamate + D-Ala
show the reaction diagram
pyroglutamyl-D-Leu + H2O
pyroglutamate + D-Leu
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Glu + H2O
pyroglutamate + Glu
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Gly + H2O
pyroglutamate + Gly
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Gly-Ile + H2O
pyroglutamate + Gly-Ile
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His + H2O
pyroglutamate + His
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His-Gly + H2O
pyroglutamate + His-Gly
show the reaction diagram
pyroglutamyl-His-Gly-NH2 + H2O
pyroglutamate + His-Gly-NH2
show the reaction diagram
pyroglutamyl-His-Pro-Gly + H2O
pyroglutamate + His-Pro-Gly
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His-Pro-Gly-NH2 + H2O
pyroglutamate + His-Pro-Gly-NH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Ile + H2O
pyroglutamate + Ile
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Leu + H2O
pyroglutamate + Leu
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Lys + H2O
pyroglutamate + Lys
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Met + H2O
pyroglutamate + Met
show the reaction diagram
-
-
-
-
?
pyroglutamyl-p-pitroanilide + H2O
pyroglutamate + p-pitroaniline
show the reaction diagram
pyroglutamyl-peptide + H2O
pyroglutamate + peptide
show the reaction diagram
-
the enzyme is able to specifically remove the amino-terminal pyroglutamyl residue protecting proteins or peptides from aminopeptidases
-
?
pyroglutamyl-Phe + H2O
pyroglutamate + Phe
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Phe-Pro-NH2 + H2O
pyroglutamate + Phe-Pro-NH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Ser + H2O
pyroglutamate + Ser
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Thr + H2O
pyroglutamate + Thr
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Trp + H2O
pyroglutamate + Trp
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Tyr + H2O
pyroglutamate + Tyr
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Val + H2O
pyroglutamate + Val
show the reaction diagram
-
-
-
-
?
pyroglutamyle-4-methylcoumarin 7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
thyroliberin + H2O
pyroglutamate + His-Pro-NH2
show the reaction diagram
thyroliberin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
thyrotrophin releasing hormone
?
show the reaction diagram
thyrotrophin-releasing hormone + H2O
?
show the reaction diagram
thyrotropin-releasing hormone + H2O
?
show the reaction diagram
additional information
?
-
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
pyroglutamyl-peptide + H2O
pyroglutamate + peptide
show the reaction diagram
-
the enzyme is able to specifically remove the amino-terminal pyroglutamyl residue protecting proteins or peptides from aminopeptidases
-
?
thyrotrophin releasing hormone
?
show the reaction diagram
thyrotrophin-releasing hormone + H2O
?
show the reaction diagram
Q4U338
trypanosomal pyroglutamyl aminopeptidase I is responsible for the abnormally rapid degradation of thyrotrophin-releasing hormone in the circulation of infected rats
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
1 mM, weak activation
CoSO4
-
activates
FeCl2
-
1 mM, weak activation
FeCl3
-
1 mM, weak activation
MgCl2
-
1 mM, weak activation
MnCl2
-
1 mM, weak activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,7-phenanthroline
-
-
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
-
-
2-Iodoacetamide
2-Pyrrolidinone
-
1 mM inhibits by 44%
2-Pyrrolidone
4,7-phenanthroline
-
-
4-(2-aminoethyl)-benzenesulfonylfluoride
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
activity is restored by 2-mercaptoethanol
8-hydroxyquinoline
acetamide
-
-
Acid thyroliberin
-
competitive inhibition of thyroliberin hydrolysis
amastatin
Anorexogenic peptide
-
competitive inhibition of thyroliberin hydrolysis
-
Arphamenine B
-
-
bacitracin
-
weak
bestatin
-
inhibits soluble PAP-I in the hippocampus by 14.8% and in the hypothalamus by 14.4%. Inhibition of membrane-bound PAP-I in the hypothalamus by 8.8%
bradykinin-potentiating peptide 5a
-
competitive inhibition of thyroliberin hydrolysis
-
Chelating agents
-
strong
chymostatin
-
-
diethyl dicarbonate
-
-
Dithiobisnitrobenzoate
-
-
dithiothreitol
-
-
E64
-
0.1 mM, 15% inhibition
Elastinal
-
-
Eledoisin
-
competitive inhibition of thyroliberin hydrolysis
formic acid ethyl ester
-
-
iodoacetamide
iodoacetate
iodoacetic acid
-
0.1 mM completely inhibits
L-pyroglutamate
-
weak
L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane
-
i.e. E-64, partial
leupeptin
-
-
Luliberin
-
competitive inhibition of thyroliberin hydrolysis
luteinizing hormone releasing hormone 1-5
-
-
-
Luteinizing hormone-releasing hormone
-
inhibits hydrolysis of thyrotropin-releasing hormone
Mn2+
-
weak inhibition
N-bromosuccinimide
-
-
N-ethylmaleimide
Nalpha-benzyloxycarbonyl-L-pyroglutamyl chloromethylketone
natural oligosaccharide gum from Hakea gibbosa
-
effective non-competitive inhibitor. The natural gum may be a promising additive not only for its sustained-release and mucoadhesive properties, but also for its ability to slow the enzymatic degradation of therapeutic polypeptides incorporated in dosage forms
-
neurotensin
-
competitive inhibition of thyroliberin hydrolysis
p-chloromercuribenzoate
-
1 mM, activity is completely lost
p-hydroxymercuribenzoate
-
-
peptidic calpain inhibitor
-
i.e. EP-475, partial
-
phenylmethylsulfonyl fluoride
-
1 mM inhibits by 53.4%
puromycin
pyroglutamic acid-Ala
-
competitive inhibitor
pyroglutamic acid-His-Pro-NH2
-
thyrotropin-releasing hormone, relative highest affinity, competitive inhibitor
pyroglutamic acid-Val
-
competitive inhibitor
pyroglutaminal
-
-
pyroglutamyl-D-Ala
-
-
pyroglutamyl-His methyl ester
-
inhibits hydrolysis of thyrotropin-releasing hormone
-
pyroglutamyl-L-dopa-Pro-NH2
-
inhibits hydrolysis of thyrotropin-releasing hormone
-
pyroglutamyl-Pro
-
-
-
Sodium tetrathionate
thioglycolic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
weak activation
cyclosporin
-
increases particulate and soluble PAP activity in the renal cortex. Particulate PAP activity returns to levels similar to controls after 15 days of cyclosporin withdrawal, soluble PAP does not regress. Soluble and particulate aminopeptidases in resident and elicited macrophages are unaffected by cyclosporin
DFP
-
weak activation
dithiothreitol
DTT
-
enhances activity
glucose
-
alters the hypothalamic activity of soluble PAP-I
Insulin
-
alters the hypothalamic activity of soluble PAP-I
-
methanol
-
a methanol based deblocking solution preserves enzymatic activity, provides conditions compatible with sequencing and enhances deblocking of electroblotted samples
PMSF
-
weak activation
thio-reducing agent
-
absolute requirement
-
tris(2-carboxyethyl)phosphine
-
at least 0.5 mM required for full activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 0.58
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
0.079 - 0.089
gonadotropin-releasing hormone
0.33 - 0.42
L-2-oxoimidazolidine-4-carboxyl-L-Ala
1.53
L-2-oxooxazolidine-4-carboxyl-aminoethylnitrate
-
37°C, pH 7.4
0.55 - 0.71
L-2-oxooxazolidine-4-carboxyl-L-Ala
1.43
L-2-oxothiazolidine-4-carboxyl-D-2-aminopropylnitrate
-
37°C, pH 7.4
0.62
L-2-oxothiazolidine-4-carboxyl-ethanolamine
-
37°C, pH 7.4
0.57
L-2-oxothiazolidine-4-carboxyl-L-2-aminopropylnitrate
-
37°C, pH 7.4
0.3 - 0.43
L-2-oxothiazolidine-4-carboxyl-L-Ala
0.0335
L-pyroglutamyl p-nitroanilide
-
-
0.018 - 0.028
L-pyroglutamyl-7-amido-4-methylcoumarin
0.25
L-pyroglutamyl-Ala
-
-
0.14
L-pyroglutamyl-aminoethylnitrate
-
37°C, pH 7.4
0.29
L-pyroglutamyl-Arg
-
-
0.29
L-pyroglutamyl-Asp
-
-
0.17 - 1.46
L-pyroglutamyl-beta-naphthylamide
0.23
L-pyroglutamyl-Glu
-
-
0.2
L-pyroglutamyl-Gly
-
-
0.23
L-pyroglutamyl-His
-
-
0.14
L-pyroglutamyl-Ile
-
-
0.045 - 0.057
L-pyroglutamyl-L-Ala
0.14
L-pyroglutamyl-Leu
-
-
0.2
L-pyroglutamyl-Lys
-
-
0.13
L-pyroglutamyl-Met
-
-
0.028 - 0.054
L-pyroglutamyl-p-nitroanilide
0.1
L-pyroglutamyl-Phe
-
-
0.15
L-pyroglutamyl-Ser
-
-
0.24
L-pyroglutamyl-Thr
-
-
0.11
L-pyroglutamyl-Trp
-
-
0.2
L-pyroglutamyl-Tyr
-
-
0.09
L-pyroglutamyl-Val
-
-
0.49
luteinizing-hormone-releasing hormone
-
-
1.91
neurotensin
-
-
0.04 - 0.15
pyroglutamate-4-methylcoumarin 7-amide
-
0.059
pyroglutamic acid-7-amido-4-methylcoumarin
-
-
0.7
pyroglutamyl-2-naphthylamide
-
-
-
0.01536
pyroglutamyl-4-methylcoumarin 7-amide
-
-
-
0.05
pyroglutamyl-4-methylcoumaryl-7-amide
-
pH 7.8, 37°C
0.89
pyroglutamyl-Ala
-
-
0.02076 - 1.79
Pyroglutamyl-beta-naphthylamide
0.00253 - 0.4198
pyroglutamyl-His-Pro-4-methylcoumarin 7-amide
-
0.0449
pyroglutamyl-His-Pro-NH2
-
-
0.73 - 20
pyroglutamyl-p-nitroanilide
0.04 - 0.727
Thyroliberin
0.59
thyroliberin-releasing hormone
-
-
-
0.05
thyrotrophic hormone releasing hormone
-
-
0.032 - 0.041
thyrotrophin-releasing hormone
0.041 - 0.056
thyrotropin-releasing hormone
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 2.3
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
9 - 12
gonadotropin-releasing hormone
2.4 - 3.6
L-2-oxoimidazolidine-4-carboxyl-L-Ala
7.6
L-2-oxooxazolidine-4-carboxyl-aminoethylnitrate
Rattus norvegicus
-
37°C, pH 7.4
6.4 - 8.1
L-2-oxooxazolidine-4-carboxyl-L-Ala
1.5
L-2-oxothiazolidine-4-carboxyl-D-2-aminopropylnitrate
Rattus norvegicus
-
37°C, pH 7.4
0.9
L-2-oxothiazolidine-4-carboxyl-ethanolamine
Rattus norvegicus
-
37°C, pH 7.4
3.2
L-2-oxothiazolidine-4-carboxyl-L-2-aminopropylnitrate
Rattus norvegicus
-
37°C, pH 7.4
2.3 - 3.4
L-2-oxothiazolidine-4-carboxyl-L-Ala
47 - 58
L-pyroglutamyl-7-amido-4-methylcoumarin
3.5
L-pyroglutamyl-aminoethylnitrate
Rattus norvegicus
-
37°C, pH 7.4
0.5 - 785
L-pyroglutamyl-beta-naphthylamide
2.4 - 3.7
L-pyroglutamyl-L-Ala
52 - 64
L-pyroglutamyl-p-nitroanilide
7.2
luteinizing-hormone-releasing hormone
Bacillus amyloliquefaciens
-
-
26.3
neurotensin
Bacillus amyloliquefaciens
-
-
3.5
pyroglutamic acid-7-amido-4-methylcoumarin
Bos taurus
-
-
7.4 - 35.1
Pyroglutamyl-beta-naphthylamide
21
thyroliberin-releasing hormone
Bacillus amyloliquefaciens
-
-
-
20 - 22
thyrotrophin-releasing hormone
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.062
2-Pyrrolidone
0.03
NEM
-
pH 7.8, 37°C
0.141
pyroglutamic acid-Ala
-
-
0.0441
pyroglutamic acid-His-Pro-NH2
-
-
0.6522
pyroglutamic acid-Val
-
-
additional information
additional information
-
Ki for the natural oligosaccharide gum from Hakea gibbosa is 0.31% w/v
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0208
-
-
1.093
-
-
3.45
-
-
3.5
pH 7.5, temperature not specified in the publication
340
-
crude enzyme
3633
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
6.5 - 8
-
-
6.8 - 7.6
-
-
7 - 8.5
-
hydrolysis of pyroglutamyl-4-methylcoumaryl-7-amide
7.3
-
pituitary enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
about 40% of maximal activity at pH 5.0 and at pH 8.0
5.5 - 10
-
pH 5.5: about 50% of maximal activity, pH 10.0: about 65% of maximal activity
6 - 8.5
-
pH 6.5: about 45% of maximal activity, pH 8.5: about 25% of maximal activity
7 - 9.5
-
50% of maximal activity at pH 7 and at pH 9.5
7.5 - 10
-
activity dropping off sharply outside this pH range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
-
80 - 85
-
wild-type enzyme in absence of dithiothreitol
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 80
60 - 100
-
60°C: about 40% of maximal activity, 100°C: about 90% of maximal activity, wild-type enzyme, in presence of dithiothreitol
75 - 105
-
75°C: about 60% of maximal activity, 105°C: about 90% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
orchidectomy increases activity of pyrrolidone carboxypeptidase type I, testosterone replacement returns it to control levels
Manually annotated by BRENDA team
-
mucosa
Manually annotated by BRENDA team
-
high levels of of soluble PGP I activity during the initial moments of development, in the fourth postnatal day activity starts to decrease until adulthood. Activity of the particulate form shows lowest values, during the first 20 days of life a significant decrease takes place, from this moment activity remains constant. No significant changes in activity of the particulate form
Manually annotated by BRENDA team
-
high activity of soluble PGP I during the first days of development, between 20-30 postnatal days activity decreases significantly
Manually annotated by BRENDA team
-
from colon
Manually annotated by BRENDA team
-
pyroglutamyl-peptidase I is not involved in the aetilohy and pathology of coeliac disease
Manually annotated by BRENDA team
additional information
-
activity dysregulation at different local and systemic levels may participate in the initiation, promotion and progression of breast cancer induced in rat by N-methyl nitrosourea through the increase of gonadotropin-releasing hormone
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
particulate form shows lower activity levels than the soluble form
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Staphylococcus aureus (strain COL)
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xenorhabdus bovienii (strain SS-2004)
Xenorhabdus bovienii (strain SS-2004)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22441
-
2 * 22441, calculation from nucleotide sequence
22936
-
x * 22936, ionspray triple quadrupole mass spectrometry, carboxymethylated enzyme
22940
-
ionspray triple quadrupole mass spectrometry, carboxymethylated enzyme
23135
-
x * 23135, calculation from nucleotide sequence
23188
-
1 * 23188, calculation from nucleotide sequence
23500
-
4 * 23500, SDS-PAGE
23700
-
gel filtration
23777
-
x * 23777, calculation from nucleotide sequence
24020
-
sequence analysis
24472
-
4 * 24472, denaturing PAGE
24747
4 * 24747, calculated from sequence
25000
-
-
25200
-
4 * 25200, SDS-PAGE
30000
-
x * 30000, wild-type enzyme, 3 bands of 30000 Da and of 60000 Da are detected in mutant enzymes S185C and C68S/S185C, SDS-PAGE in presence and in absence of 2-mercaptoethanol
30270
-
sequence analysis
36000
-
gel filtration
45640
-
ionspray triple quadrupole mass spectrometry, native enzyme
45643
-
x * 45643, ionspray triple quadrupole mass spectrometry, native enzyme
55000 - 65000
-
enzyme from brain
72000
-
gel filtration
80000 - 108000
gel filtration
86000
-
gel filtration
91000
-
non-denaturing PAGE
96000
-
gel filtration
214000
-
gel filtration
230000
240000
-
enzyme from liver
260000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
trimer
-
3 * 24000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallographic analysis of enzyme-inhibitor complex with pyroglutaminal and of the mutant enzyme F142, hanging drop vapour diffusion method
-
crystal structure of wild-type and mutant enzyme C142S/C188S determined at 2.2 and 2.7 A resolution
-
PCP-0SH polar mutants C142S/C188S/E192D andC142S/C188S/E192Q crystallize at a 6.5% PEG4000, while the apolar mutants C142S/C188S/E192A, C142S/C188S/E192I and C142S/C188S/E192V crystallize at a 5.7-6.0% PEG4000. The protein molecules crystallize in two different space groups. E192Q and E192V form isomorphic monoclinic crystals in the space group P2(1), which agree with those of the wild-type PCP and cysteine-free PCP-0SH (C142S/C188S), while E192A, E192D, and E192I form orthorhombic crystals in the space group P2(1)2(1)2(1). In both crystal systems, four subunit (monomer) molecules are contained in the asymmetric unit. A systematic analysis of individual structures indicates that the mutation does not have any significant effect on the overall structure
-
hanging drop vapor diffusion method at 4°C, 1.6 A resolution
crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4
-
at acidic pH the mutant enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V, C142S/C188S/E192D and C142S/C188S/E192Q are less stable than cysteine-free mutant C142S/C188S
667733
4 - 9.2
-
rapid inactivation below pH 4.0 and above pH 9.2
95299
7 - 8.2
-
stable
95283
10.5
-
at alkaline pH the mutant enzyme enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V and C142S/C188S/E192Q are more stable than cysteine-free mutant C142S/C188S
667733
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
room temperature, 40% loss of activity after 15 days, 57% loss of activity after 1 month
24
-
50 mM phosphate buffer, pH 7, 10 mM 2-mercaptoethanol, 28% loss of activity after 1 month
30
-
pH 7.0, 30 min, about 5% loss of activity of wild-type enzyme and of mutant enzyme S185C
37
-
1 h, rapid inactivation
45
-
stable for at least 1 h
47
-
thermodynamics of heat denaturation of the monomeric enzyme form of mutant enzyme C142S/C188S at pH 2.3. The mechanism of refolding is a two-state process. The equilibrium establishes with a relaxation time of 5080 s at Tm = 46.5°C
55
-
partial inactivation
59
-
peak temperature on the differential scanning calorimetry is 59.3°C, pH 2.15, cysteine-free mutant enzyme C142S/C188S
79
-
peak temperature on the differential scanning calorimetry is 78.9°C, pH 3.04 cysteine-free mutant enzyme C142S/C188S
80
-
pH 7.0, 30 min, complete loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C
89
-
peak temperature on the differential scanning calorimetry is 77.6°C, pH 7.3, cysteine-free mutant enzyme C142S/C188S; peak temperature on the differential scanning calorimetry is 88.8°C, pH 8,7, cysteine-free mutant enzyme C142S/C188S
102
-
peak temperature on the differential scanning calorimetry is 101.7°C, pH 9,6, cysteine-free mutant enzyme C142S/C188S
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol and EDTA stabilize
addition of 1% bovine serum albumin to the purified enzyme improves stability with 88% of the activity remaining after 4 days at 4°C and 93% of the activity remaining after 21 days at -80°C
-
enzyme solubilized by sodium deoxycholate and Triton X-100, -20°C or 4°C, 24 h, more than 50% loss of activity
-
freezing and thawing, 67% of the activity is recovered after one cycle, 70% loss of activity after 5 cycles
-
subunit interactions play an important role in stabilizing the enzyme in addition to the intrinsic enhanced stability of its monomer
-
trypsin solubilized enzyme, no loss of activity after 14 days at 4°C, 20% loss of activity after 14 days at -20°C
-
wild-type and mutant enzyme C142S/C188S, the anomalous high stability of the hyperthermophilic enzyme originates from the unusually slow rate of unfolding reaction during treatment with guanidine-hydrochloride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetonitrile
Ethanol
guanidine-HCl
-
approximately 70% of the original activity is retained after preincubation with 10 mM DTT, 50 mM Na-phosphate buffer (pH 7.0) containing less than either 0.01% SDS, 1 M urea, or 1 M guanidine-HCl at 37°C for 15 min
isopropanol
Methanol
SDS
-
approximately 70% of the original activity is retained after preincubation with 10 mM DTT, 50 mM Na-phosphate buffer (pH 7.0) containing less than either 0.01% SDS, 1 M urea, or 1 M guanidine-HCl at 37°C for 15 min
urea
-
approximately 70% of the original activity is retained after preincubation with 10 mM DTT, 50 mM Na-phosphate buffer (pH 7.0) containing less than either 0.01% SDS, 1 M urea, or 1 M guanidine-HCl at 37°C for 15 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, 24 h, more than 50% loss of activity of the enzyme solubilized by sodium deoxycholate and Triton X-100
-
-20°C, 50 mM phosphate buffer, pH 7, 10 mM 2-mercaptoethanol, 70% loss of activity after 1 month
-
-20°C, pH 7, in presence of 5 mM EDTA and 5 mM 2-mercaptoethanol, stable for 3 months
-
-20°C, rapid inactivation in presence of EDTA and 2-mercaptoethanol
-
-20°C, retains more than 90% of its activity for 1 month in the presence of a thiol-reducing agent
-
-80°C, 17% loss of activity after 4 weeks
-
4°C, -20°C or -70°C, 1 month, 90% loss of activity
-
4°C, 50 mM phosphate buffer, pH 7, 10 mM 2-mercaptoethanol, 13% loss of activity after 1 month
-
4°C, 72 h, 10% loss of activity of the enzyme solubilized in CHAPS
-
4°C, 72 h, 60% loss of activity of the enzyme solubilized in CHAPS
-
4°C, almost 60% of the initial activity is recovered after 1 month
-
4°C, pH 7, in presence of 5 mM EDTA and 5 mM 2-mercaptoethanol, less than 50% loss of activity
-
4°C, pH 7.8, stable for at least 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by cation exchange chromatography
-
by immobilised nickel ion affinity chromatography
-
by Ni-affinity chromatography and gel filtration
-
from Trypanosoma brucei-infected rat plasma
purification of mutant enzmyes F10Y, F10A, F13Y, F13A, F142Y and F142A
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed by use of a baculovirus vector in Spodoptera frugiperda
-
expressed in Escherichia coli under the control of an inducible tac promoter
expression in Escherichia coli
expression in Escherichia coli, wild-type and mutant enzymes
-
expression of mutant enzmyes F10Y, F10A, F13Y, F13A, F142Y and F142A
-
mutant enzymes S185C and C68S/S185C expressed in Escherichia coli
-
N-terminal His-tagged native or mutant PPI expressed in Escherichia coli BL21(DE3)
-
overexpression in Escherichia coli
PAP1 gene cloned into vector pCR2.1, subcloned into vector pQE60, subcloned into expression vector pPC225, having the ORF for recombinant PAP1 in fusion with a His 6 tag on the C-terminal, expressed in Escherichia coli XL10-Gold cells
-
PCP-0SH and its mutant expressed in Escherichia coli strain JM109
-
PGAP expressed from a pET3a-series vector in Escherichia coli BL21(DE) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C68S/S185C
-
the ratio of turnover number to Km-value for the substrate L-pyroglutamyl-beta-naphthylamide is 1.3fold higher than the value of the wild-type enzyme. The disulfide bridge between the substituted C185 bonds two subunits, additional 60000 Da band detected by SDS-PAGE. Thermal stability is increased by about 30°C compared to wild-type enzyme
F10Y
-
the ratio of turnover number to Km-value is 4.6% of the wild-type value
F13A
-
the ratio of turnover number to Km-value is 0.04% of the wild-type value
F13Y
-
the ratio of turnover number to Km-value is 51.5% of the wild-type value
F142A
-
the ratio of turnover number to Km-value is 0.06% of the wild-type value
F142Y
-
the ratio of turnover number to Km-value is 81.3% of the wild-type value
S185C
-
the ratio of turnover number to Km-value for the substrate L-pyroglutamyl-beta-naphthylamide is 1.4fold higher than the value of the wild-type enzyme. The disulfide bridge between the substituted C185 bonds two subunits, additional 60000 Da band detected by SDS-PAGE. The mutant enzyme is more stable than the wild-type enzyme at pH 4.0 and at pH 12.0. Thermal stability is increased by about 30°C compared to wild-type enzyme
C210A
-
no detectable activity
E101Q
-
ca. 2% activity of the native enzyme
E107Q
-
ca. 50% activity of the native enzyme
H234S
-
no detectable activity
C144A
-
inactive enzyme
D89A
-
no activity
D89N
-
35% of activity of the wild-type enzyme
E10Q
-
enzyme displays catalytic properties and sensitivities to 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide similar to those of wild-type enzyme
E22Q
-
enzyme displays catalytic properties and sensitivities to 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide similar to wild-type enzyme
H166S
-
inactive enzyme
A199P
-
alpha6-helix region of A199P in the D1 state (initial denatured state) is partially unprotected, while some hydrophobic residues are protected against H/D exchange, although these hydrophobic residues are unprotected in the wild-type protein. Structure of A199P in the D1 state forms a temporary stable denatured structure with a non-native hydrophobic cluster and the unstructured alpha6-helix
C142S
-
complete loss of the activity
C142S/C188S
C142S/C188S/E192A
-
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S
C142S/C188S/E192D
-
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04, pH 7.3, pH 8.7 and pH 9.6 is less than that of the cysteine-free mutant enzyme C142S/C188S
C142S/C188S/E192I
-
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S
C142S/C188S/E192Q
-
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S
C142S/C188S/E192V
-
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S
C188S
-
activity is reduced by one-fourth relative to the activity of the wild-type enzyme
Cys144Ser/Cys188Ser
-
cysteine-free variant. The 114-208 segment of the mutant folds into a stable compact structure with non-native helix-helix association in the D1 state. In the folding process from the D1 state to the native state, the alpha4- and alpha6-helices become separated and the central beta-sheet is folded between these helices. The non-native interaction between the alpha4- and alpha6-helices may be responsible for the unusually slow folding of the mutant
additional information
-
PPI-deficient mutants show no detectable phenotype, retain infectivity to macrophages in vitro and in mice
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the heat denaturation of wild-type enzyme and mutant enzymes C188S and C142S/C188S is highly reversible in the dimeric forms, but completely irreversible in the tetrameric form
-
the heat-denaturation of the mutant enzyme C142S/C188S is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
additional information
-
C-terminal alpha-helix in the D1 state plays an important role in retaining the D1 state under the stable conditions and in correctly folding into the native structure of PCP-0SH
Show AA Sequence (3319 entries)
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