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Information on EC 3.4.19.3 - pyroglutamyl-peptidase I and Organism(s) Homo sapiens and UniProt Accession Q9NXJ5

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.3 pyroglutamyl-peptidase I
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This record set is specific for:
Homo sapiens
UNIPROT: Q9NXJ5 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro
Synonyms
pgp-1, pap-i, pyroglutamate aminopeptidase, pyroglutamyl aminopeptidase, pyroglutamyl peptidase i, pcp-0sh, pyrase, pyrrolidone carboxyl peptidase, pyrrolidonyl arylamidase, pyroglutamyl aminopeptidase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyroglutamyl aminopeptidase I
-
5-oxoprolyl-peptidase
-
-
-
-
aminopeptidase, pyroglutamate
-
-
-
-
L-pyrrolidonecarboxylate peptidase
-
-
-
-
pyroglutamate aminopeptidase
-
-
-
-
pyroglutamidase
-
-
-
-
pyroglutamyl aminopeptidase
-
-
-
-
pyrrolidone carboxyeptidase
-
-
pyrrolidone-carboxylate peptidase
-
-
-
-
pyrrolidonecarboxy peptidase
-
-
-
-
pyrrolidonecarboxylyl peptidase
-
-
-
-
pyrrolidonyl peptidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-21-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ACE inhibitor + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Trp-
-
?
bombesin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Arg-
-
?
bradykinin potentiator B + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Gly-
-
?
L-pyroglutamyl-p-nitroanilide + H2O
L-pyroglutamate + p-nitroaniline
show the reaction diagram
-
-
-
?
leukopyrokinin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Thr-
-
?
luteinizing hormone releasing hormone + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-His-
-
?
neurotensin + H2O
pyroglutamate + ?
show the reaction diagram
contains the N-terminal dipeptide pyroglutamyl-Leu-
-
?
pyroglutamyl-4-methylcoumaryl-7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
thyrotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
?
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide + H2O
L-2-oxothiazolidine-4-carboxylic acid + ?
show the reaction diagram
-
-
-
-
?
L-2-oxoimidazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxooxazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-oxothiazolidine-4-carboxyl-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-L-Ala + H2O
L-pyroglutamate + L-Ala
show the reaction diagram
-
-
-
-
?
luliberin + H2O
pyroglutamate + His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
pyroglutamate + Leu-Tyr-Glu-Asn-Lys-Pro-Ag-Arg-Pro-Tyr-Ile-Leu
show the reaction diagram
-
-
-
-
?
pyroglutamyl-4-methylcoumarin 7-amide + H2O
pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
thyroliberin + H2O
pyroglutamate + His-Pro-NH2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
maximal activity in absence of divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Pyrrolidone
reversible
Ca2+
1 mM, 20% inhibition
Cu2+
1 mM, 96% inhibition
E64
0.1 mM, 15% inhibition
NEM
reversible
Ni2+
0.1 mM, 98% inhibition
Zn2+
1 mM, 98% inhibition
1,10-phenanthroline
-
-
amastatin
-
-
Arphamenine B
-
-
chymostatin
-
-
EDTA
-
-
Elastinal
-
-
leupeptin
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thio-reducing agent
absolute requirement
-
dithiothreitol
-
absolute requirement for maintenance of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
L-pyroglutamyl-p-nitroanilide
37°C, pH 7.4
0.05
pyroglutamyl-4-methylcoumaryl-7-amide
pH 7.8, 37°C
0.046
thyrotropin-releasing hormone
37°C, pH 7.4
0.5
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
-
37°C, pH 7.4
0.33
L-2-oxoimidazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
0.55
L-2-oxooxazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
0.3
L-2-oxothiazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
0.045
L-pyroglutamyl-L-Ala
-
37°C, pH 7.4
0.08
pyroglutamate-4-methylcoumarin 7-amide
-
-
0.0449
pyroglutamyl-His-Pro-NH2
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
4(R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide
-
37°C, pH 7.4
2.4
L-2-oxoimidazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
6.4
L-2-oxooxazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
2.3
L-2-oxothiazolidine-4-carboxyl-L-Ala
-
37°C, pH 7.4
2.4
L-pyroglutamyl-L-Ala
-
37°C, pH 7.4
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2-Pyrrolidone
pH 7.8, 37°C
0.03
NEM
pH 7.8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.093
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
hydrolysis of pyroglutamyl-4-methylcoumaryl-7-amide
8
-
enzyme from kidney
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
7 - 9.5
-
50% of maximal activity at pH 7 and at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from colon
Manually annotated by BRENDA team
pyroglutamyl-peptidase I is not involved in the aetilohy and pathology of coeliac disease
Manually annotated by BRENDA team
-
highest level in particulate sperm fraction. Increased activity in necrozoospermia
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGPI_HUMAN
209
0
23138
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23188
1 * 23188, calculation from nucleotide sequence
24000
gel filtration
22000
23000
-
enzyme from cerebral cortex
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 23188, calculation from nucleotide sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
4.5 h, stable up to
50
90 min, enzyme is completely stable in crude preparation
60
30 min, activity is almost completely lost
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, retains more than 90% of its activity for 1 month in the presence of a thiol-reducing agent
4°C, pH 7.8, stable for at least 1 week
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed by use of a baculovirus vector in Spodoptera frugiperda
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
application to N-terminal pyroglutamyl unblocking prior to Edman sequential degradation in peptide and protein sequencing
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Awade, A.C.; Cleuziat, P.; Gonzales, T.; Robert-Baudouy, J.
Pyrrolidone carboxyl peptidase (Pcp): An enzyme that removes pyroglutamic acid (pGlu) from pGlu peptides and pGlu-proteins
Proteins Struct. Funct. Genet.
20
34-51
1994
Bos taurus, Cavia porcellus, Enterobacter cloacae, Enterococcus faecium, Homo sapiens, Oryctolagus cuniculus, Pseudomonas fluorescens, Rattus norvegicus, Streptococcus pyogenes, Sus scrofa
Manually annotated by BRENDA team
Mantle, D.; Lauffart, B.; Gibson, A.
Purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human skeletal muscle
Clin. Chim. Acta
197
35-46
1991
Homo sapiens
Manually annotated by BRENDA team
Yamada, M.; Mori, M.
Thyrotropin-releasing hormone-degrading enzyme in human serum is classified as type II of pyroglutamyl aminopeptidase: influence of thyroid status
Proc. Soc. Exp. Biol. Med.
194
346-351
1990
Homo sapiens
Manually annotated by BRENDA team
Dando, P.M.; Fortunato, M.; Strand, G.B.; Smith, T.S.; Barrett, A.J.
Pyroglutamyl-peptidase I: cloning, sequencing, and characterisation of the recombinant human enzyme
Protein Expr. Purif.
28
111-119
2003
Homo sapiens (Q9NXJ5), Homo sapiens
Manually annotated by BRENDA team
Larrinaga, G.; Callado, L.F.; Agirregoitia, N.; Varona, A.; Gil, J.
Subcellular distribution of membrane-bound aminopeptidases in the human and rat brain
Neurosci. Lett.
383
136-140
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Abe, K.; Saito, F.; Yamada, M.; Tokui, T.
Pyroglutamyl aminopeptidase I, as a drug metabolizing enzyme, recognizes xenobiotic substrates containing L-2-oxothiazolidine-4-carboxylic acid
Biol. Pharm. Bull.
27
113-116
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Abe, K.; Fukuda, K.; Tokui, T.
Marginal involvement of pyroglutamyl aminopeptidase I in metabolism of thyrotropin-releasing hormone in rat brain
Biol. Pharm. Bull.
27
1197-1201
2004
Homo sapiens (Q9NXJ5), Homo sapiens, Mus musculus (Q9ESW8), Mus musculus, Rattus norvegicus (Q76IC5)
Manually annotated by BRENDA team
Monsuur, A.J.; Stepniak, D.; Diosdado, B.; Wapenaar, M.C.; Mearin, M.L.; Koning, F.; Wijmenga, C.
Genetic and functional analysis of pyroglutamyl-peptidase I in coeliac disease
Eur. J. Gastroenterol. Hepatol.
18
637-644
2006
Homo sapiens (Q9NXJ5)
Manually annotated by BRENDA team
Valdivia, A.; Irazusta, J.; Fernandez, D.; Mugica, J.; Ochoa, C.; Casis, L.
Pyroglutamyl peptidase I and prolyl endopeptidase in human semen: increased activity in necrozoospermia
Regul. Pept.
122
79-84
2004
Homo sapiens
Manually annotated by BRENDA team
Carrera-Gonzalez, M. del P.; Ramirez-Exposito, M.J.; Duenas, B.; Martinez-Ferrol, J.; Mayas, M.D.; Martinez-Martos, J.M.
Putative relationship between hormonal status and serum pyrrolidone carboxypeptidase activity in pre- and post-menopausal women with breast cancer
Breast
21
751-754
2012
Homo sapiens
Manually annotated by BRENDA team
Megias, M.J.; Alba-Araguez, F.; Luna, J.D.; Vives, F.; Ramirez-Sanchez, M.
Serum pyroglutamyl aminopeptidase activity: apromising novel biomarker candidate for liver cirrhosis
Endocr. Regul.
49
20-24
2015
Homo sapiens
Manually annotated by BRENDA team