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Enzyme Nomenclature
Information on EC 3.4.19.3 - pyroglutamyl-peptidase I
for references in articles please use BRENDA:EC3.4.19.3
Word Map on EC 3.4.19.3
- 3.4.19.3
- trh
- lymphocyte
-
thyrotropin-releasing
- thymocytes
-
edman
-
endopeptidase
-
aminopeptidases
-
thyrotropin
- amyloliquefaciens
-
trh-degrading
-
deblocked
- neurotensin
- thyroliberin
-
diketopiperazine
- his-pro
-
l-pyroglutamic
- analysis
- hermes
-
adipokinetic
- medicine
-
cyclo
- luliberin
-
intrathymic
-
post-proline
- litoralis
-
pancreatitis-associated
- phytolacca
-
protein-i
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.4.19.3
-
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RECOMMENDED NAME
GeneOntology No.
pyroglutamyl-peptidase I
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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CAS REGISTRY NUMBER
COMMENTARY
9075-21-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
strain mito, strain NSI and strain tamarii; strain PCI 219, ML-208 and strain DT-39
-
-
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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
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
ACE inhibitor + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-Trp-
-
?
bombesin + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-Arg-
-
?
bradykinin potentiator B + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-Gly-
-
?
bradykinin-potentiating peptide B + H2O
?
-
cleavage of the peptide bond adjacent to the pyroglutamic residue
-
-
?
gonadotropin-releasing hormone + H2O
?
hydrolyzed exclusively at the pyroglutamyl-/-Xaa bond
-
-
?
L-pyroglutamic acid 2-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
-
-
-
-
?
L-pyroglutamyl p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamate + 7-amino-4-methylcoumarin
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphtylamine
-
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphtylamine
-
-
-
-
?
L-pyroglutamyl-His-Pro-4-methylcoumarin 7-amide + H2O
L-pyroglutamate + His-Pro-4-methylcoumarin 7-amide
-
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutaminic acid + p-nitroaniline
-
-
-
?
L-pyrrolidonyl 2-naphthylamide + H2O
5-oxo-L-proline + 2-naphthylamine
-
-
-
-
?
leukopyrokinin + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-Thr-
-
?
luteinizing hormone releasing hormone + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-His-
-
?
N-(4-methyl-2-oxo-2H-chromen-7-yl)-5-oxo-L-prolinamide + H2O
5-oxo-L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
neurotensin + H2O
pyroglutamate + ?
contains the N-terminal dipeptide pyroglutamyl-Leu-
-
?
pyroglutamic acid-7-amido-4-methylcoumarin + H2O
L-pyroglutamate + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamyl-2-naphthylamide + H2O
pyroglutamate + 2-naphthylamine
-
-
-
-
?
pyroglutamyl-4-methylcoumaryl-7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
-
-
?
pyroglutamyl-peptide + H2O
pyroglutamate + peptide
-
the enzyme is able to specifically remove the amino-terminal pyroglutamyl residue protecting proteins or peptides from aminopeptidases
-
?
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
-
-
-
-
?
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
-
-
-
-
?
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
-
-
-
-
?
acid-thyroliberin + H2O
pyroglutamate + His-Pro
-
i.e. pyroglutamyl-His-Pro
-
?
bombesin + H2O
pyroglutamate + Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
-
-
-
-
?
bombesin + H2O
pyroglutamate + Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
-
i.e. pyroglutamyl-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
-
?
ethyl L-pyroglutamate + H2O
L-pyroglutamate + ethanol
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
-
-
-
?
litorin + H2O
pyroglutamate + Gln-Trp-Ala-Val-Gly-His-Phe-Met-NH2
-
frog litorin
-
?
litorin + H2O
pyroglutamate + Gln-Trp-Ala-Val-Gly-His-Phe-Met-NH2
-
frog litorin
-
?
luliberin + H2O
pyroglutamate + His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
i.e. pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
?
luliberin + H2O
pyroglutamate + His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
-
-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
-
-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
-
-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
i.e. pyroglutamyl-Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
-
-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
-
-
-
-
?
physalaemin + H2O
pyroglutamate + Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2
-
-
-
?
physalaemin + H2O
pyroglutamate + Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2
-
-
-
?
pyroglutamyl-4-methylcoumarin 7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamyl-4-methylcoumarin 7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamyl-4-methylcoumarin 7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-His-Gly + H2O
pyroglutamate + His-Gly
-
i.e. anorexogenic peptide
-
?
pyroglutamyl-p-pitroanilide + H2O
pyroglutamate + p-pitroaniline
-
-
-
-
?
thyroliberin + H2O
pyroglutamate + His-Pro-NH2
-
removes the N-terminal pyroglutamic acid
-
-
?
thyroliberin + H2O
pyroglutamate + His-Pro-NH2
-
i.e. pyroglutamyl-His-Pro-NH2, i.e. thyrotrophin releasing hormone
-
?
thyrotrophin releasing hormone
?
-
the enzyme is proposed to inactivate thyrotrophin releasing hormone in brain extracellular space
-
-
-
thyrotrophin-releasing hormone + H2O
?
trypanosomal pyroglutamyl aminopeptidase I is responsible for the abnormally rapid degradation of thyrotrophin-releasing hormone in the circulation of infected rats
-
-
?
thyrotrophin-releasing hormone + H2O
?
hydrolyzed exclusively at the pyroglutamyl-/-Xaa bond
-
-
?
additional information
?
-
-
slight activity toward L-pyroglutamyl-D-amino acids, inert toward L-pyroglutamyl-L-Pro
-
-
-
additional information
?
-
-
the molecular recognition of pyroglutamic acid is achieved through two hydrogen bonds and an insertion in the hydrophobic pocket. In the pocket Phe10 is more important to the hydrophobic interaction than is Phe142 and furthermore Phe13 serves as an induced fit mechanism
-
?
additional information
?
-
-
the enzyme does not catalyze the hydrolysis of peptides with six-membered ureido rings at the amino terminus, but it tolerates well a five-membered ureido ring at this position
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
no hydrolysis of dipeptides containing N-terminal pyroglutamic acid or with pyroglutamyl peptides containing more than three amino acids
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme is inactive towards uperolein and piperidone carbonyl His-Pro-NH2
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
enzyme may participate in regulating the levels of seminal thyrotropin-relasing hormone analogues and in mediating sperm death associated with necrozoospermia
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
pyroglutamate and iron regulate the expression of the enzyme
-
-
-
additional information
?
-
-
pyroglutamate and iron regulate the expression of the enzyme
-
-
-
additional information
?
-
-
PGAP performs enzymatic deblocking of pyroglutamylated immunoglobulins. Unfolding of immunoglobulins is required for excision of the pyroglutamate. The enzyme requires the substrate in an extended conformation, which is not fullfiled in the native form of immunoglobulins
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
diurnal variation and left-right distribution of pyroglutamyl peptidase I activity in the rat brain and retina
-
-
-
additional information
?
-
-
pyroglutamyl peptidase I levels and their left-right distribution in the rat retina and hypothalamus are influenced by light-dark conditions
-
-
-
additional information
?
-
the enzyme might not be dominantly involved in the degradation of thyrotropin-releasing hormone in rats
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
pyroglutamyl-peptide + H2O
pyroglutamate + peptide
-
the enzyme is able to specifically remove the amino-terminal pyroglutamyl residue protecting proteins or peptides from aminopeptidases
-
?
thyrotrophin-releasing hormone + H2O
?
Q4U338
trypanosomal pyroglutamyl aminopeptidase I is responsible for the abnormally rapid degradation of thyrotrophin-releasing hormone in the circulation of infected rats
-
-
?
thyrotrophin releasing hormone
?
-
the enzyme is proposed to inactivate thyrotrophin releasing hormone in brain extracellular space
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
enzyme may participate in regulating the levels of seminal thyrotropin-relasing hormone analogues and in mediating sperm death associated with necrozoospermia
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
pyroglutamate and iron regulate the expression of the enzyme
-
-
-
additional information
?
-
-
pyroglutamate and iron regulate the expression of the enzyme
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
diurnal variation and left-right distribution of pyroglutamyl peptidase I activity in the rat brain and retina
-
-
-
additional information
?
-
-
pyroglutamyl peptidase I levels and their left-right distribution in the rat retina and hypothalamus are influenced by light-dark conditions
-
-
-
additional information
?
-
Q76IC5
the enzyme might not be dominantly involved in the degradation of thyrotropin-releasing hormone in rats
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
additional information
?
-
-
the enzyme appears to play an important role in the activation and inactivation of many N-terminal pyroglutamyl-terminating peptides
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
activity is restored by 2-mercaptoethanol
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
-
Luteinizing hormone-releasing hormone
-
inhibits hydrolysis of thyrotropin-releasing hormone
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
-
pyroglutamic acid-His-Pro-NH2
-
thyrotropin-releasing hormone, relative highest affinity, competitive inhibitor
pyroglutamyl-His methyl ester
-
inhibits hydrolysis of thyrotropin-releasing hormone
pyroglutamyl-L-dopa-Pro-NH2
-
inhibits hydrolysis of thyrotropin-releasing hormone
amastatin
-
inhibits soluble PAP-I in the hippocampus by 12.5% and in the hypothalamus by 13.8%. Does not inhibit membrane-bound PAP-I
Nalpha-benzyloxycarbonyl-L-pyroglutamyl chloromethylketone
-
-
Nalpha-benzyloxycarbonyl-L-pyroglutamyl chloromethylketone
-
inactive towards the D-isomer
puromycin
-
inhibits soluble PAP-I in the hippocampus by 15.5% and in the hypothalamus by 42.5%. Inhibition of membrane-bound PAP-I in the hippcampus by 11.5%
Zn2+
-
inhibits soluble PAP-1 in the hippocampus and hypothalamus, does not inhibit membrane-bound PAP-I
additional information
-
postive linear correlation between pKi and the carbon chain length for a homologous series of n-alkanols up to C5
-
additional information
-
Ca2+, Mg2+, Na+, Li+, pepstatin A, 1,10-phenanthroline, benzamidine, bestatin and trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane have no or little inhibitory effect
-
additional information
-
not inhibited by phenyl methyl sulphonyl fluoride. 28% reduced activity of soluble PAP-I and 40-45% reduced activity of membrane-bound PAP-I in both the hippocampus and hypothalamus of streptozotocin-diabetic rats. Changes can be mitigated by concomitant treatment with insulin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
methanol
-
a methanol based deblocking solution preserves enzymatic activity, provides conditions compatible with sequencing and enhances deblocking of electroblotted samples
dithiothreitol
-
rapid increase in activity from 2 to 6 mM, above this concentration plateau effect
dithiothreitol
-
presence of disulfide-reducing agent such as dithiothreitol required
dithiothreitol
-
strongly stimulates activity of wild-type enzyme and mutant enzyme C188S and shifts the pH-optimum to higher temperatures by about 10°C
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
-
37°C, pH 7.4
0.079
gonadotropin-releasing hormone
37°C, pH 7.4, native enzyme
0.089
gonadotropin-releasing hormone
37°C, pH 7.4, recombinant enzyme
0.018
L-pyroglutamyl-7-amido-4-methylcoumarin
37°C, pH 7.4, native enzyme
0.028
L-pyroglutamyl-7-amido-4-methylcoumarin
37°C, pH 7.4, recombinant enzyme
0.17
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142Y
0.18
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme C68S/S185C; pH 7.0, 37°C, mutant enzyme S185C
0.2
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F13Y
0.21
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, wild-type enzyme
0.25
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, wild-type enzyme
0.55
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142A
0.76
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F10Y
1.46
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142Y
0.028
L-pyroglutamyl-p-nitroanilide
37°C, pH 7.4, native enzyme
0.044
L-pyroglutamyl-p-nitroanilide
37°C, pH 7.4, recombinant enzyme
0.032
thyrotrophin-releasing hormone
37°C, pH 7.4, recombinant enzyme
0.041
thyrotrophin-releasing hormone
37°C, pH 7.4, native enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9
gonadotropin-releasing hormone
37°C, pH 7.4, native enzyme
12
gonadotropin-releasing hormone
37°C, pH 7.4, recombinant enzyme
47
L-pyroglutamyl-7-amido-4-methylcoumarin
37°C, pH 7.4, recombinant enzyme
58
L-pyroglutamyl-7-amido-4-methylcoumarin
37°C, pH 7.4, native enzyme
0.5
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142A
0.8
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142Y
54.7
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F10Y
163
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F13Y
210
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme F142Y
319
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, wild-type enzyme
641
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme C68S/S185C
770
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, mutant enzyme S185C
785
L-pyroglutamyl-beta-naphthylamide
-
pH 7.0, 37°C, wild-type enzyme
52
L-pyroglutamyl-p-nitroanilide
37°C, pH 7.4, native enzyme
64
L-pyroglutamyl-p-nitroanilide
37°C, pH 7.4, recombinant enzyme
20
thyrotrophin-releasing hormone
37°C, pH 7.4, native enzyme
22
thyrotrophin-releasing hormone
37°C, pH 7.4, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki for the natural oligosaccharide gum from Hakea gibbosa is 0.31% w/v
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
peptidase activities have seasonal and tissue-specific characteristics, which suggest a relevant role in the reproductive physiology
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
7 - 8
7.5
8.5
additional information
additional information
-
optimal activity between 8.8-10.5, activity decreases rapidly below pH 8.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
6 - 9
6 - 9
-
pH 6.0: about 75% of maximal activity, pH 9.0: about 70% of maximal activity, hydrolysis of pyroglutamyl-4-methylcoumaryl-7-amide
6 - 9
pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
70
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
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
50 - 80
-
50°C: about 50% of maximal activity, 80°C: about 40% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
orchidectomy increases activity of pyrrolidone carboxypeptidase type I, testosterone replacement returns it to control levels
-
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
-
high activity of soluble PGP I during the first days of development, between 20-30 postnatal days activity decreases significantly
-
pyroglutamyl-peptidase I is not involved in the aetilohy and pathology of coeliac disease
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
-
pyroglutamate aminopeptidase II is predominantly localized in neuronal cells
-
in the cortex, activity of soluble PGP I and particulate PGP I decreases 5fold and 4fold, respectively, from the embryo to the adult
orchidectomy increases activity of pyrrolidone carboxypeptidase type I, high dose of testosterone returns activity to control levels
-
highest levels of soluble PGP I in all developmental stages, significant increase until 4 postnatal days, afterwards activity decreases slowly until 15 postnatal days, but subsequently continues to increase until 30 postnatal days. Activity of the particulate form increases until parturition day, until adulthood it remains constant with a small increase after 30 postnatal days
-
activity of soluble PGP I does not change significantly until 20 postnatal days, significant increase between 20-30 postnatal days. Significant decrease in the activity of the particulate form from embryonic day 22 to the fourth postnatal day, until 90 postnatal days activity remains constant
no change in pyrrolidone carboxypeptidase type I after orchidectomy, activity increases after administration of testosterone
-
highest level in particulate sperm fraction. Increased activity in necrozoospermia
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
particulate form shows lower activity levels than the soluble form
-
-
activity is high from embryonic day 22 until postnatal Day 9, and afterwards decreases
-
activity is low until postnatal Day 9, with a peak at postnatal Day 2, and the activity increases at postnatal day 15. In later stages there are not significant changes of synaptosomal activity
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus amyloliquefaciens;
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O58321
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);
O07883
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C);
Q5SJW4
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Xenorhabdus bovienii (strain SS-2004);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
O73944
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
22936
-
x * 22936, ionspray triple quadrupole mass spectrometry, carboxymethylated enzyme
22940
-
ionspray triple quadrupole mass spectrometry, carboxymethylated enzyme
23000
24000
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
41000
45643
-
x * 45643, ionspray triple quadrupole mass spectrometry, native enzyme
85000
230000
260000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
?
-
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
?
-
x * 22936, ionspray triple quadrupole mass spectrometry, carboxymethylated enzyme; x * 45643, ionspray triple quadrupole mass spectrometry, native enzyme
dimer
-
2 * 22441, calculation from nucleotide sequence; 2 * 23000, SDS-PAGE
dimer
-
the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5
dimer
-
the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5
monomer
-
the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5
monomer
-
the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5
tetramer
-
the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5
tetramer
-
the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5
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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
-
crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
7 - 8
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
7 - 8
-
30°C, stable in presence of 5 mM EDTA and 2-mercaptoethanol
95290
7 - 8
-
30°C, 30 min, stable in presence of 5 mM each of EDTA and 2-mercaptoethanol
95283
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
40
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
50
59
-
peak temperature on the differential scanning calorimetry is 59.3°C, pH 2.15, cysteine-free mutant enzyme C142S/C188S
60
70
75
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
40
-
pH 7.0, 30 min, about 30% loss of activity of wild-type enzyme, about 5% loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C
50
-
pH 7.0, 30 min, about 95% loss of activity of wild-type enzyme, about 10% loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C
75
-
pH 7.0, 30 min, about 65% loss of activity of mutant enzyme S185C and about 80% loss of activity of mutant enzyme C68S/S185C
additional information
-
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
additional information
-
the thermal stability of the mutant enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V, C142S/C188S/E192D and C142S/C188S/E192Q 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 enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V and C142S/C188S/E192Q is higher than that of the cysteine-free mutant C142S/C188S. The thermal stability of mutant enzyme C142S/C188S/E192D at pH 8.7 and 9.6 is less than that of cysteine-free mutant enzyme C142S/C188S
additional information
-
alpha6-helix (from Ser188 to Glu205) of PCP-0SH is stably formed in the D1 state
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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
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
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
acetonitrile
at 50% (v/v) concentrations more than 50% of the initial activity is retained
acetonitrile
-
at 50% (v/v) concentrations more than 50% of the initial activity is retained
-
Ethanol
the enzyme retains stability at concentrations up to 90% (v/v)
Ethanol
-
the enzyme retains stability at concentrations up to 90% (v/v)
-
isopropanol
at 50% (v/v) concentrations more than 50% of the initial activity is retained
isopropanol
-
at 50% (v/v) concentrations more than 50% of the initial activity is retained
-
Methanol
the enzyme retains stability at concentrations up to 75% (v/v)
Methanol
-
the enzyme retains stability at concentrations up to 75% (v/v)
-
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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, retains more than 90% of its activity for 1 month in the presence of a thiol-reducing agent
-
4°C, 50 mM phosphate buffer, pH 7, 10 mM 2-mercaptoethanol, 13% loss of activity after 1 month
-
4°C, pH 7, in presence of 5 mM EDTA and 5 mM 2-mercaptoethanol, less than 50% loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of mutant enzmyes F10Y, F10A, F13Y, F13A, F142Y and F142A
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli under the control of an inducible tac promoter
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
-
PGAP expressed from a pET3a-series vector in Escherichia coli BL21(DE) cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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
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/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
C142S/C188S
-
small thermodynamic stability of the mutant enzyme C142S/C188S at low pH. The mutant enzyme is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5. The heat-denaturation of the mutant enzyme is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics
C142S/C188S
-
the mutant enzyme is used in unfolding and refolding experiments to exclude the complexity in reaction due to oxidation of SH groups
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
analysis
-
pyroglutamyl aminopeptidase is an auxiliary enzyme in a spectrometric assay for glutaminyl cyclase activity. It is a fast, continuous, and reliable determination of glutaminyl cyclase activity, even in the presence of ammonium ions, during the course of protein purification and enzymatic analysis
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
analysis
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application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
medicine
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the natural oligosaccharide gum from Hakea gibbosa is an 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
medicine
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profiles of macrophage and renal PAP activities may be considered into the elaboration of new potential strategies for preventing nephrotoxicity during cyclosporin treatment
medicine
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overexpression of active PPI in Leishmania major impairs differentiation from the procyclic promastigote to the infective metacyclic promastigote. PPI does not protect against the natural antimicrobial peptide gomesin
medicine
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diabetes mellitus affects the levels of hippocampal and hypothalamic PAP-I activities, which may change the metabolic control of its susceptible physiological peptide substrates in the brain
medicine
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examination of Peptoclostridium difficile isolates from children with hematological malignancies, diarrhoea and from healthy neonates. All strains from children with hematological malignancies react with the substrate for L-pyrrolidone arylamidase
medicine
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healthy post-menopausal women show higher values of pyroglutamyl-peptidase I activity than pre-menopausal women. No differences are found in serum pyroglutamyl-peptidase activity between pre- and post-menopausal women with breast cancer. Only post-menopausal women with breast cancer show lower values of pyroglutamyl-peptidase activity than control women
medicine
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analysis of enzymic activity in serum of controls and patients diagnosed with pancreatitis, hepatitis, and liver cirrhosis. Pyroglutamyl-aminopeptidase activity decreases selectively in liver cirrhosis compared with all the rest of groups
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