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Information on EC 3.4.19.3 - pyroglutamyl-peptidase I
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3.4.19.3 pyroglutamyl-peptidase ISpecify your search results
Word Map
- 3.4.19.3
- trh
- lymphocyte
- thymocytes
-
thyrotropin-releasing
- cd8
- thyrotropin
-
trh-degrading
- amyloliquefaciens
-
deblocked
- analysis
-
pancreatitis-associated
- phytolacca
-
l-pyroglutamic
- hermes
- thyroliberin
-
diketopiperazine
- his-pro
-
intrathymic
-
3.4.21.26
-
post-proline
- litoralis
- luliberin
- medicine
- protein-i
-
cyclo
-
adipokinetic
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
Synonyms
5-oxoprolyl-peptidase, aminopeptidase, pyroglutamate, cysteine-free PCP, EC 3.4.11.8, L-pyrrolidonecarboxylate peptidase, PAP, PAP-I, PAP1, PCP, PCP-0SH, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-oxoprolyl-peptidase
-
-
-
-
aminopeptidase, pyroglutamate
-
-
-
-
EC 3.4.11.8
-
-
formerly
-
L-pyrrolidonecarboxylate peptidase
-
-
-
-
PAP-I
PCP
PYR
pyroglutamate aminopeptidase
pyroglutamidase
-
-
-
-
pyroglutamyl aminopeptidase
pyroglutamyl aminopeptidase I
pyrrolidone carboxyl peptidase
pyrrolidone-carboxylate peptidase
pyrrolidonecarboxy peptidase
-
-
-
-
pyrrolidonecarboxylyl peptidase
-
-
-
-
pyrrolidonyl arylamidase
pyrrolidonyl peptidase
-
-
-
-
PYR
no activity in Staphylococcus aureus ATCC 25923
-
-
-
PYR
no activity in Staphylococcus pseudintermedius LMG 22219T
-
-
-
pyroglutamate aminopeptidase
-
-
-
-
pyroglutamyl aminopeptidase
-
-
-
-
pyrrolidone-carboxylate peptidase
-
-
-
-
pyrrolidonyl arylamidase
no activity in Staphylococcus aureus ATCC 25923
-
-
-
pyrrolidonyl arylamidase
no activity in Staphylococcus pseudintermedius LMG 22219T
-
-
-
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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 SOURCE
PATHWAYS
MetaCyc
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CAS REGISTRY NUMBER
COMMENTARY
9075-21-2
-
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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
no activity in Staphylococcus aureus
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
no activity in Staphylococcus aureus ATCC 25923
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
no activity in Staphylococcus pseudintermedius
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
no activity in Staphylococcus pseudintermedius LMG 22219T
-
-
-
-
?
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
Staphylococcus delphini 49-046
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini 52-006
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini 53-033
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini 56-021
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini 56-039
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini 62-031
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini MI 09-2894
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini MI 09-8445
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini MI 16-1129
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus delphini VPP 12 D
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
Staphylococcus pseudintermedius LMG 22219T
-
-
-
-
?
pyroglutamyl-beta-naphthylamide + H2O
pyroglutamate + beta-naphthylamine
-
-
-
-
?
pyroglutamyl-His-Gly + H2O
pyroglutamate + His-Gly
-
i.e. anorexogenic peptide
-
?
pyroglutamyl-p-nitroanilide + H2O
pyroglutamate + p-nitroaniline
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
-
presence of disulfide-reducing agent such as dithiothreitol required
dithiothreitol
-
rapid increase in activity from 2 to 6 mM, above this concentration plateau effect
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Coinfection
Mucosal T cells recovered from mice after infection with respiratory syncytial virus display a memory/activation phenotype.
Cystitis
Inflammation and nerve injury induce expression of pancreatitis-associated protein-II in primary sensory neurons.
Endotoxemia
Pancreatitis-associated protein-I mRNA expression in mouse pancreas is upregulated by lipopolysaccharide independent of cerulein-pancreatitis.
Hyperalgesia
Nerve Injury-Induced Neuronal PAP-I Maintains Neuropathic Pain by Activating Spinal Microglia.
Hyperthyroidism
Thyroid status regulates particulate but not soluble TRH-degrading pyroglutamate aminopeptidase activity in the rat liver.
Infections
Evaluation of three disk tests for identification of enterococci, leuconostocs, and pediococci.
Infections
Mucosal T cells recovered from mice after infection with respiratory syncytial virus display a memory/activation phenotype.
Influenza, Human
Comparative behavior of membrane protein-antibody complexes on motile fibroblasts: implications for a mechanism of capping.
Insulinoma
Evidence for pyroglutamyl peptidase I and prolyl endopeptidase activities in the rat insulinoma cell line RINm 5F: lack of relationship with TRH metabolism.
Kidney Neoplasms
Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma.
Leukemia
Hepatic gene expression patterns following trauma-hemorrhage: effect of posttreatment with estrogen.
Leukemia
High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate.
Liver Cirrhosis
Serum pyroglutamyl aminopeptidase activity: a promising novel biomarker candidate for liver cirrhosis.
Lymphoma
Regulation of Thy-1 and Pgp-1 glycoproteins in hybrids between T-cell lymphomas and Abelson-leukemia-virus-induced lymphomas.
Lymphoma
T-cell lymphomas emerging as epineoplasms in mice bearing transplanted polyoma virus-induced salivary gland tumors.
Lymphoma, T-Cell
Regulation of Thy-1 and Pgp-1 glycoproteins in hybrids between T-cell lymphomas and Abelson-leukemia-virus-induced lymphomas.
Neoplasms
A ratiometric fluorescent sensor for rapid detection of the pyroglutamate aminopeptidase-1 in mouse tumors.
Neoplasms
Activity of the Bcl-2 family inhibitor ABT-263 in a panel of small cell lung cancer xenograft models.
Neoplasms
Antigenic variation and macrophage infiltration of human bladder tumors xenografted into nude mice.
Neoplasms
Antitumor activity and tumor necrosis factor production of Phytolacca acinosa polysaccharides I in mice.
Neoplasms
Effects of Phytolacca acinosa polysaccharides I combined with interleukin-2 on the cytotoxicity of murine splenocytes against tumor cells.
Neoplasms
Moderate Beer Consumption Modifies Tumoral Growth Parameters and Pyrrolidone Carboxypeptidase Type-I and Type-II Specific Activities in the Hypothalamus-Pituitary-Mammary Gland Axis in an Animal Model of Breast Cancer.
Neuralgia
Erratum: Li et al., 'Nerve Injury-Induced Neuronal PAP-I Maintains Neuropathic Pain by Activating Spinal Microglia'.
Neuralgia
Nerve Injury-Induced Neuronal PAP-I Maintains Neuropathic Pain by Activating Spinal Microglia.
Pancreatitis
Pancreatitis-associated protein-I and pancreatitis-associated protein-III expression in a rat model of kainic acid-induced seizure.
Pancreatitis
Pancreatitis-associated protein-I mRNA expression in mouse pancreas is upregulated by lipopolysaccharide independent of cerulein-pancreatitis.
Pancreatitis
Regulation of mouse pancreatitis-associated protein-I gene expression during caerulein-induced acute pancreatitis.
Peripheral Nerve Injuries
Inflammation and nerve injury induce expression of pancreatitis-associated protein-II in primary sensory neurons.
Peripheral Nerve Injuries
Nerve Injury-Induced Neuronal PAP-I Maintains Neuropathic Pain by Activating Spinal Microglia.
Prostatic Neoplasms
Discovery of 2-chloro-N-(4-methoxyphenyl)-N-methylquinazolin-4-amine (EP128265, MPI-0441138) as a potent inducer of apoptosis with high in vivo activity.
pyroglutamyl-peptidase i deficiency
Nerve Injury-Induced Neuronal PAP-I Maintains Neuropathic Pain by Activating Spinal Microglia.
Seizures
Pancreatitis-associated protein-I and pancreatitis-associated protein-III expression in a rat model of kainic acid-induced seizure.
Sepsis
Pseudomonas pneumonia-mediated sepsis induces expression of pancreatitis-associated protein-I in rat pancreas.
Tonsillitis
Activity of soluble aminopeptidase A and dipeptidyl peptidase IV and membrane-bound aminopeptidase B and pyroglutamyl peptidase I in adenoid hyperplasia, tonsillar hyperplasia and chronic tonsillitis.
Urinary Bladder Neoplasms
Antigenic variation and macrophage infiltration of human bladder tumors xenografted into nude mice.
Vesicular Stomatitis
Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: presence of Thy-1 glycoprotein and absence of H-2, Pgp-1 and T-200 glycoproteins on the envelopes of these virus particles.
Virus Diseases
Intrahepatic alpha beta-TcRintermediate LFA-1high T cells are stimulated during mouse hepatitis viral infection.
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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
0.18
L-pyroglutamyl-beta-naphthylamide
-
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
2.3
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
-
37°C, pH 7.4
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
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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
brenda
-
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
brenda
-
high activity of soluble PGP I during the first days of development, between 20-30 postnatal days activity decreases significantly
brenda
pyroglutamyl-peptidase I is not involved in the aetilohy and pathology of coeliac disease
brenda
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
brenda
-
pyroglutamate aminopeptidase II is predominantly localized in neuronal cells
brenda
-
in the cortex, activity of soluble PGP I and particulate PGP I decreases 5fold and 4fold, respectively, from the embryo to the adult
brenda
orchidectomy increases activity of pyrrolidone carboxypeptidase type I, high dose of testosterone returns activity to control levels
brenda
-
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
brenda
-
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
brenda
no change in pyrrolidone carboxypeptidase type I after orchidectomy, activity increases after administration of testosterone
brenda
-
highest level in particulate sperm fraction. Increased activity in necrozoospermia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
particulate form shows lower activity levels than the soluble form
-
brenda
-
activity is high from embryonic day 22 until postnatal Day 9, and afterwards decreases
brenda
-
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
-
brenda
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
230000
24000
260000
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
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SUBUNIT
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
-
the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5
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
monomer
-
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
tetramer
-
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
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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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PROTEIN VARIANTS
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
-
the mutant enzyme is used in unfolding and refolding experiments to exclude the complexity in reaction due to oxidation of SH groups
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
102
peak temperature on the differential scanning calorimetry is 101.7°C, pH 9,6, cysteine-free mutant enzyme C142S/C188S
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
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
89
peak temperature on the differential scanning calorimetry is 77.6°C, pH 7.3, cysteine-free mutant enzyme C142S/C188S
89
peak temperature on the differential scanning calorimetry is 88.8°C, pH 8,7, cysteine-free mutant enzyme C142S/C188S
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
-
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
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
-
2-mercaptoethanol and EDTA stabilize