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Information on EC 3.4.19.3 - pyroglutamyl-peptidase I and Organism(s) Thermococcus litoralis and UniProt Accession O07883

for references in articles please use BRENDA:EC3.4.19.3
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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:
Thermococcus litoralis
UNIPROT: O07883 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermococcus litoralis
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
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
pyrrolidone carboxyl peptidase
-
5-oxoprolyl-peptidase
-
-
-
-
aminopeptidase, pyroglutamate
-
-
-
-
L-pyrrolidonecarboxylate peptidase
-
-
-
-
pyroglutamate aminopeptidase
-
-
-
-
pyroglutamidase
-
-
-
-
pyroglutamyl aminopeptidase
-
-
-
-
pyrrolidone carboxyl peptidase
-
-
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
ethyl L-pyroglutamate + H2O
L-pyroglutamate + ethanol
show the reaction diagram
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-pyroglutamyl-beta-naphthylamide + H2O
L-pyroglutamate + beta-naphthylamine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
-
enhances activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
pH 7.5, temperature not specified in the publication
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 80
50°C: about 50% of maximal activity
50 - 80
-
50°C: about 50% of maximal activity, 80°C: about 40% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24747
4 * 24747, calculated from sequence
80000 - 108000
gel filtration
24472
-
4 * 24472, denaturing PAGE
96000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 24747, calculated from sequence
tetramer
-
4 * 24472, denaturing PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
half-life: approximately 1 h
70
-
half-life: 1 h
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
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)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli under the control of an inducible tac promoter
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Singleton, M.; Isupov, M.; Littlechild, J.
Crystallization and preliminary X-ray diffraction studies of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis
Acta Crystallogr. Sect. D
55
702-703
1999
Thermococcus litoralis
Manually annotated by BRENDA team
Singleton, M.; Isupov, M.; Littlechild, J.
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis
Structure Fold. Des.
15
237-244
1999
Thermococcus litoralis
Manually annotated by BRENDA team
Singleton, M.R.; Littlechild, J.A.
Pyrrolidone carboxylpeptidase from Thermococcus litoralis
Methods Enzymol.
330
394-403
2001
Thermococcus litoralis
Manually annotated by BRENDA team
Singleton, M.R.; Taylor, S.J.; Parrat, J.S.; Littlechild, J.A.
Cloning, expression, and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralis
Extremophiles
4
297-303
2000
Thermococcus litoralis (O07883), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (O07883)
Manually annotated by BRENDA team