3.4.19.3: pyroglutamyl-peptidase I
This is an abbreviated version!
For detailed information about pyroglutamyl-peptidase I, go to the full flat file.
Word Map on EC 3.4.19.3
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3.4.19.3
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trh
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lymphocyte
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thymocytes
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thyrotropin-releasing
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cd8
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thyrotropin
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trh-degrading
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amyloliquefaciens
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deblocked
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analysis
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thyroliberin
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his-pro
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diketopiperazine
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l-pyroglutamic
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phytolacca
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hermes
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pancreatitis-associated
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adipokinetic
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litoralis
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post-proline
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protein-i
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cyclo
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3.4.21.26
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luliberin
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intrathymic
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medicine
- 3.4.19.3
- trh
- lymphocyte
- thymocytes
-
thyrotropin-releasing
- cd8
- thyrotropin
-
trh-degrading
- amyloliquefaciens
-
deblocked
- analysis
- thyroliberin
- his-pro
-
diketopiperazine
-
l-pyroglutamic
- phytolacca
- hermes
-
pancreatitis-associated
-
adipokinetic
- litoralis
-
post-proline
- protein-i
-
cyclo
-
3.4.21.26
- luliberin
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intrathymic
- medicine
Reaction
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, PGAP, PGP I, PGP-1, PGPEP1, PPI, PYR, PYRase, pyroglutamate aminopeptidase, pyroglutamidase, pyroglutamyl aminopeptidase, pyroglutamyl aminopeptidase I, pyroglutamyl peptidase I, pyroglutamyl peptidase type-1, pyroglutamyl type I aminopeptidase, pyroglutamyl-peptidase 1, pyroglutamylaminopeptidase, pyrrolidone carboxyeptidase, pyrrolidone carboxyl peptidase, pyrrolidone carboxypeptidase type I, pyrrolidone-carboxylate peptidase, pyrrolidonecarboxy peptidase, pyrrolidonecarboxylyl peptidase, pyrrolidonyl arylamidase, pyrrolidonyl peptidase
ECTree
3.4.19.3 pyroglutamyl-peptidase IAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 3.4.19.3 - pyroglutamyl-peptidase I
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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
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room temperature, 40% loss of activity after 15 days, 57% loss of activity after 1 month
24
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50 mM phosphate buffer, pH 7, 10 mM 2-mercaptoethanol, 28% loss of activity after 1 month
30
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pH 7.0, 30 min, about 5% loss of activity of wild-type enzyme and of mutant enzyme S185C
40
47
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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
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pH 7.0, 30 min, complete loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C
89
additional information
40
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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
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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
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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
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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
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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
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alpha6-helix (from Ser188 to Glu205) of PCP-0SH is stably formed in the D1 state
