Information on EC 3.4.19.6 - pyroglutamyl-peptidase II

Word Map on EC 3.4.19.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.19.6
-
RECOMMENDED NAME
GeneOntology No.
pyroglutamyl-peptidase II
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of the N-terminal pyroglutamyl group from pGlu-/-His-Xaa tripeptides and pGlu-/-His-Xaa-Gly tetrapeptides
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
60063-88-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3-Me-His2)thyrotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
acid-thyroliberin + H2O
?
show the reaction diagram
-
-
-
-
?
L-5-oxoprolyl 2-naphthylamide + H2O
2-naphthylamine + 5-oxoproline
show the reaction diagram
luliberin N-terminal tripeptide + H2O
?
show the reaction diagram
-
pyroglutamyl-His-Trp
-
-
?
pyroglutamyl-7-amido-4-methylcoumarin + H2O
pyroglutamate + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Asn(N-benzyl)-ProNH2 + H2O
L-pyroglutamate + Asn(N-benzyl)-ProNH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Asn(N-methyl)-ProNH2 + H2O
L-pyroglutamate + Asn(N-methyl)-ProNH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His-Gly + H2O
pyroglutamate + His-Gly
show the reaction diagram
-
slight
-
-
?
pyroglutamyl-His-Pro-7-amido-4-methylcoumarin + H2O
pyroglutamate + His-Pro-7-amido-4-methylcoumarin
show the reaction diagram
pyroglutamyl-His-Pro-NH2 + H2O
pyroglutamate + His-Pro-NH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His-Pro-OH + H2O
pyroglutamate + His-Pro-OH
show the reaction diagram
-
-
-
-
?
pyroglutamyl-His-tripeptidyl naphthylamides + H2O
pyroglutamate + His-tripeptidyl naphthylamides
show the reaction diagram
-
-
-
-
?
pyroglutamyl-histidyl-prolyl-7-amido-4-methylcoumarin + H2O
pyroglutamic acid + histidyl-prolyl-7-amido-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Phe-Pro-NH2 + H2O
pyroglutamate + Phe-Pro-NH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Phe-Pro-OH + H2O
pyroglutamate + Phe-Pro-OH
show the reaction diagram
-
-
-
-
?
pyroglutamyl-thienylalanyl-Pro-NH2 + H2O
pyroglutamate + thienylalanyl-Pro-NH2
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Tyr-Pro-OH + H2O
pyroglutamate + Tyr-Pro-OH
show the reaction diagram
-
-
-
-
?
thyroliberin + H2O
?
show the reaction diagram
thyroliberin + H2O
pyroglutamic acid + His-Pro-NH2
show the reaction diagram
thyrotropin releasing hormone + H2O
?
show the reaction diagram
thyrotropin releasing hormone-beta-naphthylamine + H2O
?
show the reaction diagram
-
substrate activity assay
-
-
?
thyrotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
thyrotropin-releasing hormone-beta-naphthylamide + H2O
?
show the reaction diagram
-
essential role of Glu408 within the exopeptidase motif for aminopeptidase activity. Ser269 and Lys463 are implicated in the generation of omegapeptidase specificity. Lys463 creates a putative salt bridge with Glu408
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
thyroliberin + H2O
?
show the reaction diagram
thyrotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
detection of a RNA species derived from an alternative processing at the exon 14–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPII–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CoSO4
-
161% enhancement of activity at 0.1 mM and 559% enhancement at 1 mM. 1 mM, 587% reactivation of the enzyme inactivated by EDTA
MnSO4
-
0.1 mM, 56% reactivation of the enzyme inactivated by EDTA
NiSO4
-
1 mM, 185% reactivation of the enzyme inactivated by EDTA
Zn2+
-
-
ZnSO4
-
0.1 mM, 108% reactivation of the enzyme inactivated by EDTA
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-benzodioxol-5-amine
-
-
1,7-phenanthroline
-
10 mM, 67% inhibition
2-Aminobenzyl alcohol
-
-
2-hydroxyaniline
-
-
2-Phenylethylamine
-
-
3,4-dimethoxyaniline
-
-
3,5-dimethoxyaniline
-
-
3-(trifluoromethoxy)aniline
-
-
3-phenyl-1-propylamine
-
-
4,7-phenanthroline
-
10 mM, 56% inhibition
4-(2-aminoethyl)-benzenesulfonylfluoride
-
66% inhibition at 1 mM, 97% inhibition at 10 mM
4-(trifluoromethyl)aniline
-
-
4-amino-N-methylphthalamide
-
-
4-phenylbutylamine
-
-
5,6,7,8-tetrahydro-1-naphthylamine
-
-
5-amino-2-chloropyridine
-
-
5-amino-2-methoxyphenol
-
-
5-aminoindan
-
-
5-chloro-2-methoxyaniline
-
-
5-oxoproline
-
product inhibition at high concentration
6-amino-1,3-dihydroisobenzofuran-1-one
-
-
6-amino-2-mercaptobenzothiazole
-
-
6-amino-3,4-benzocoumarin
-
-
7-amino-4-methylcoumarin
-
-
8-hydroxyquinoline
-
10 mM, 68% inhibition
benzyl alcohol
-
-
benzylamine
-
-
CDTA
-
10 mM, 10% inhibition
Chelating agents
-
-
CuSO4
DTT
-
-
Glp-Asn-Pro-D-Tyr-D-Trp-7-amido-4-methyl-coumarin
-
-
Glp-Asn-Pro-D-Tyr-D-Trp-D-Trp-7-amido-4-methyl-coumarin
-
-
Glp-Asn-Pro-D-Tyr-D-TrpNH2
-
potent inhibitor of TRH-DE. Competetive, fully reversible and not time dependent inhibition
Glp-Asn-Pro-Tyr-Trp-7-amido-4-methyl-coumarin
-
-
Glp-Asn-Pro-Tyr-Trp-Trp-7-amido-4-methyl-coumarin
-
-
Glp-Asn-Pro-Tyr-TrpNH2
-
-
Glp-PSI[P(O)(OH)CH2]-His-Pro-NH2
Hermodice carunculata inhibitor
-
Hermodice carunculata peptidase inhibitor
-
HcPI
-
His-Pro-NH2
-
product inhibition at high concentration
L-pyroglutamyl-Asn-Pro-NH2
-
inhibition is fully reversible
Luliberin
Luteinizing hormone releasing hormone
-
-
m-anisidine
-
-
m-phenethidine
-
-
Metal chelators
-
methyl alcohol
-
-
methylamine
-
-
MgSO4
-
0.1 mM
NEM
-
10 mM, 22% inhibition
neurotensin
-
-
Ni2+
-
-
o-anisidine
-
-
p-anisidine
-
-
p-Glu-Asn-Pro-7-amido-4-methylcoumarin
-
PCMB
-
-
Peptides containing N-terminal pyroglutamyl residues
-
-
-
puromycin
-
1 mM, 17% inhibition
pyroglutamyl-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn(N-benzyl)-ProNH2
-
-
pyroglutamyl-Asn(N-hydroxyl)-ProNH2
-
-
pyroglutamyl-Asn(N-methyl)-ProNH2
-
-
pyroglutamyl-Asn(N-phenyl)-ProNH2
-
-
pyroglutamyl-Asn-Pro-7-amido-4-methyl coumarin
-
-
pyroglutamyl-Asn-Pro-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn-Pro-NH2
-
-
pyroglutamyl-Asn-Pro-Ser-TyrNH2
-
-
pyroglutamyl-Asn-Pro-Trp-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn-Pro-Trp-Trp-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn-Pro-Trp-TyrNH2
-
-
pyroglutamyl-Asn-Pro-TrpNH2
-
-
pyroglutamyl-Asn-Pro-Tyr-Trp-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn-Pro-Tyr-Trp-Trp-7-amido-4-methylcoumarin
-
-
pyroglutamyl-Asn-Pro-Tyr-Trp-TrpNH2
-
-
pyroglutamyl-Asn-Pro-Tyr-TrpNH2
-
-
pyroglutamyl-Asn-Pro-TyrNH2
-
-
pyroglutamyl-Asn-ProNH2
-
-
pyroglutamyl-Gln-Pro-NH2
-
-
pyroglutamyl-Gly-Pro-NH2
-
inhibition is fully reversible
pyroglutamyl-His
-
-
Pyroglutamyl-His-Gly
-
-
pyroglutamyl-His-Gly-NH2
-
-
pyroglutamyl-His-Pro
-
-
pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
-
-
pyroglutamyl-His-Pro-Gly
-
-
pyroglutamyl-His-Pro-Gly-NH2
-
-
pyroglutamyl-His-Pro-NH2
-
-
pyroglutamyl-His-Trp-Ser-Tyr-Gly
-
-
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu
-
-
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu-Arg
-
-
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly
-
-
pyroglutamyl-homoprolyl-Pro-NH2
-
-
pyroglutamyl-L-alpha-phenylglycyl-Pro-NH2
-
-
pyroglutamyl-Phe-Pro-NH2
-
-
pyroglutamyl-Trp-Pro-NH2
-
-
Thyroliberin analogues
-
LLD-thyroliberin, pyroglutamyl-His-Pro-NHCH3, pyroglutamyl-His-Pro-Gly-NHCH3, pyroglutamyl-Phe-Pro-NH2
-
ZnSO4
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DMSO
-
activity using substrates containing 2% v/v DMSO is 5% higher than that using substrate containing no DSMO
NMDA receptor
-
-
-
thyroid hormone
-
-
-
additional information
-
no requirement for sulfhydryl-reducing agents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
(3-Me-His2)thyrotropin-releasing hormone
-
-
-
0.248
5-oxoprolyl 2-naphthylamide
-
-
0.419
pyroglutamyl-7-amido-4-methylcoumarin
-
37°C
0.00253 - 0.0035
pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
0.035
pyroglutamyl-His-Pro-NH2
-
pH 7.5, 37°C
0.311
pyroglutamyl-His-Pro-OH
-
pH 7.5, 37°C
0.055
pyroglutamyl-Phe-Pro-NH2
-
pH 7.5, 37°C
0.034
pyroglutamyl-thienylalanyl-Pro-NH2
-
pH 7.5, 37°C
0.015
pyroglutamyl-Tyr-Pro-NH2
-
pH 7.5, 37°C
0.027 - 0.056
Thyroliberin
0.025 - 0.035
thyrotropin-releasing hormone
0.00679 - 0.00942
thyrotropin-releasing hormone-beta-naphthylamide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
5-oxoprolyl 2-naphthylamide
Sus scrofa
-
-
38.3
thyrotropin-releasing hormone
Sus scrofa
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00124
1,3-benzodioxol-5-amine
-
-
0.02187
2-Aminobenzyl alcohol
-
-
0.00742
2-hydroxyaniline
-
-
0.00398
2-Phenylethylamine
-
-
0.00318
3,4-dimethoxyaniline
-
-
0.00085
3,5-dimethoxyaniline
-
-
0.00125
3-(trifluoromethoxy)aniline
-
-
0.00498
3-phenyl-1-propylamine
-
-
0.00097
4-(trifluoromethyl)aniline
-
-
0.0089
4-amino-N-methylphthalamide
-
-
0.00345
4-phenylbutylamine
-
-
0.01014
5,6,7,8-tetrahydro-1-naphthylamine
-
-
0.00163
5-amino-2-chloropyridine
-
-
0.00254
5-amino-2-methoxyphenol
-
-
0.00084
5-aminoindan
-
-
0.01085
5-chloro-2-methoxyaniline
-
-
0.00278
6-amino-1,3-dihydroisobenzofuran-1-one
-
-
0.00362
6-amino-2-mercaptobenzothiazole
-
-
0.0019
6-amino-3,4-benzocoumarin
-
-
0.000047
7-amino-4-methylcoumarin
-
-
0.0028
aniline
-
-
0.01529
benzyl alcohol
-
-
0.01281
benzylamine
-
-
0.000096
Glp-Asn-Pro-D-Tyr-D-Trp-7-amido-4-methyl-coumarin
-
-
0.000029
Glp-Asn-Pro-D-Tyr-D-Trp-D-Trp-7-amido-4-methyl-coumarin
-
-
0.000151
Glp-Asn-Pro-D-Tyr-D-TrpNH2
-
-
0.000038
Glp-Asn-Pro-Tyr-Trp-7-amido-4-methyl-coumarin
-
-
0.000001
Glp-Asn-Pro-Tyr-Trp-Trp-7-amido-4-methyl-coumarin
-
-
0.00064
Glp-Asn-Pro-Tyr-TrpNH2
-
-
0.000051
Hermodice carunculata inhibitor
-
37°C
-
0.008
Luteinizing hormone releasing hormone
-
-
0.00127
m-anisidine
-
-
0.00167
m-phenethidine
-
-
0.08416
methyl alcohol
-
-
0.01084
methylamine
-
-
0.01263
o-anisidine
-
-
0.00407
p-anisidine
-
-
0.0996
pyroglutamyl-Asn(N-benzyl)-ProNH2
-
37°C, pH 7.5
0.115
pyroglutamyl-Asn(N-hydroxyl)-ProNH2
-
37°C, pH 7.5
0.103
pyroglutamyl-Asn(N-methyl)-ProNH2
-
37°C, pH 7.5
0.133
pyroglutamyl-Asn(N-phenyl)-ProNH2
-
37°C, pH 7.5
0.00097
pyroglutamyl-Asn-Pro-7-amido-4-methyl coumarin
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
0.000458
pyroglutamyl-Asn-Pro-7-amido-4-methylcoumarin
-
-
0.0175
pyroglutamyl-Asn-Pro-NH2
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
0.00811
pyroglutamyl-Asn-Pro-Ser-TyrNH2
-
-
0.000083
pyroglutamyl-Asn-Pro-Trp-7-amido-4-methylcoumarin
-
-
0.000072
pyroglutamyl-Asn-Pro-Trp-Trp-7-amido-4-methylcoumarin
-
-
0.00591
pyroglutamyl-Asn-Pro-Trp-TyrNH2
-
-
0.00517
pyroglutamyl-Asn-Pro-TrpNH2
-
-
0.000038
pyroglutamyl-Asn-Pro-Tyr-Trp-7-amido-4-methylcoumarin
-
-
0.000001
pyroglutamyl-Asn-Pro-Tyr-Trp-Trp-7-amido-4-methylcoumarin
-
-
0.000734
pyroglutamyl-Asn-Pro-Tyr-Trp-TrpNH2
-
-
0.000639
pyroglutamyl-Asn-Pro-Tyr-TrpNH2
-
-
0.0103
pyroglutamyl-Asn-Pro-TyrNH2
-
-
0.0161
pyroglutamyl-Asn-ProNH2
-
; 37°C, pH 7.5
0.069
pyroglutamyl-Gln-Pro-NH2
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
1.67
Pyroglutamyl-His-Gly
-
37°C
0.582
pyroglutamyl-His-Gly-NH2
-
37°C
0.236
pyroglutamyl-His-Pro
-
37°C
0.0588
pyroglutamyl-His-Pro-Gly
-
37°C
0.0296
pyroglutamyl-His-Pro-Gly-NH2
-
37°C
0.0403
pyroglutamyl-His-Pro-NH2
-
37°C
0.0081
pyroglutamyl-His-Trp-Ser-Tyr-Gly
-
37°C
0.0194
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu
-
37°C
0.0603
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu-Arg
-
37°C
0.0108
pyroglutamyl-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly
-
37°C
0.5
pyroglutamyl-homoprolyl-Pro-NH2
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
0.356
pyroglutamyl-L-alpha-phenylglycyl-Pro-NH2
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
0.0731
pyroglutamyl-Phe-Pro-NH2
-
37°C
0.232
pyroglutamyl-Trp-Pro-NH2
-
pH 7.5, 37°C, hydrolysis of pyroglutamyl-His-Pro-7-amido-4-methylcoumarin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0209
-
-
0.3237
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
-
6.8 - 7.6
-
-
7.5
-
activity assay
additional information
-
broad pH-optimum in the neutral range
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 8.5
-
pH 5.7: about 35% of maximal activity, pH 8.5: about 45% of maximal activity
5.8 - 8.4
-
pH 5.8: about 45% of maximal activity, pH 8.4: about 20% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
activity assay
45
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 56
-
25°C: 16% of maximal activity, 37°C: 70% of maximal activity, 45°C: maximal activity
25 - 55
-
about 70% of activity maximum at 25°C and 55°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
orchidectomy increases activity of pyrrolidone carboxypeptidase type II, testosterone replacement returns it to control levels
Manually annotated by BRENDA team
12 to 14% of cell profiles express pyroglutamyl peptidase II mRNA in the medial septum-diagonal band of Broca, in this region the specific activity of the enzyme is relatively high. Injection of the pyroglutamyl peptidase II inhibitor p-Glu-Asn-Pro-7-amido-4-methylcoumarin into the medial septum enhances the effect of thyrotropin-releasing hormone. The injection of a phosphinic thyrotropin-releasing hormone analog, a higher affinity inhibitor of pyroglutamyl peptidase II, diminishes the duration of ethanol-induced loss of righting reflex by itself
Manually annotated by BRENDA team
-
cervicyl, thoracic and munbar
Manually annotated by BRENDA team
additional information
-
expression of wild-type and mutant enzymes in COS-7 cells and C6 glioma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the physicochemical properties are distinct from the soluble enzyme
-
Manually annotated by BRENDA team
-
the physicochemical properties are distinct from the particulate enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
125000
-
1 * 125000, SDS-PAGE
145000
-
SDS-PAGE
214000
-
gel filtration
230000
250000
-
trypsin-solubilized and purified enzyme
260000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
37°C, 15 min, stable from pH 4.0-8.0
95299
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
24 h, purified enzyme, 60% loss of activity
35 - 40
-
40 min, stable
45
-
1 h, stable
50
-
rapid and irreversible inactivation above
55
-
2 min, partial inactivation
60
-
1 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1% w/v bovine serum albumin greatly 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
-
addition of 20% v/v glyceriol affords no protection of the enzyme stored at 4°C and only moderate protection at -20°C and -80°C
-
after one cycle of freezing at -80°C and thawing, the activity of the purified enzyme preparation containing 0.3, 0.1, 0.03 or 0.01 mg protein/ml decreases by 18%, 36%, 73% and 99%, respectively
-
below a critical protein concentration of 1 mg/ml the enzyme is sensitive to freezing and thawing
-
inclusion of 50% glycerol prevents most of the harmful effect of freezing in imidazole buffer
-
presence of bovine serum albumin, 1%, sucrose, glycerol or trehalose prevents inactivation during freezing and thawing
-
trypsin is the most effective protease, above 0.001 mg/ml, the solubilized enzyme st stable for 14 days at 4°C, approximately 80% of the activity remains after 14 days at -20°C
-
unstable in Tris/HCl buffer, pH 7.3
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, potassium phosphate buffer, pH 7.4, stable for 6 months
-
15°C, 5% loss of activity after 7 days
-
4°C or -20°C, 24 h, decrease of more than 50% of activity of the enzyme solubilized by sodium deoxycholate or Triton X-100, the CHAPS solubilized enzyme is slightly more stable with approximately 90% and 40% of the activity remaining after 72 h at 4°C and -20°C
-
stable at 4°C for more than 2 months or for 24 h at 25°C, in phosphate or diethylmalonate buffer, pH 7.3, irrespective of the protein concentration
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme from brain
-
enzyme from liver
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
detection of a RNA species derived from an alternative processing at the exon 14–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPII–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity
-
full-length enzyme, mutant enzymes and truncated enzyme
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C279S
-
specific activity is 10fold lower than that of the wild-type enzyme
C338S
-
specific activity is 5fold lower than that of the wild-type enzyme
C68S
-
specific enzymatic activities are similar to that of the wild-type enzyme
C823S
-
mutant enzyme is completely inactive
C830S
-
mutant enzyme is completely inactive
C859S
-
mutant enzyme is completely inactive
K463N
-
mutant losses omega-peptidase but displays alanyl-aminopeptidase activity
S269A
-
mutant shows a 40% decrease in activity with thyrotropin-releasing hormone-beta-naphthylamide as substrate
S269E
-
mutant is inactive with thyrotropin-releasing hormone-beta-naphthylamide as substrate
S269Q
-
mutant is inactive with thyrotropin-releasing hormone-beta-naphthylamide as substrate
S269Q/K463N
-
mutant is inactive with thyrotropin-releasing hormone-beta-naphthylamide as substrate
S269Q/K463R
-
mutant is inactive with thyrotropin-releasing hormone-beta-naphthylamide as substrate
additional information
-
detection of a RNA species derived from an alternative processing at the exon 14–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPII–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition
-
animals drinking a 2.5% NaCl solution for 7 d present body weight reduction. Despite their negative energy balance, they avoid food and have increased hypothalamic paraventricular nucleus thyrotropin releasing hormone expression and thyroid-stimulating hormone serum levels. Increased medial basal hypothalamic pyroglutamyl-aminopeptidase II activity in dehydration-induced anorexia rats might counteract their high thyrotropin releasing hormone release