Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.3 pyroglutamyl-peptidase I

Engineering

Engineering on EC 3.4.19.3 - pyroglutamyl-peptidase I

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
C210A
-
no detectable activity
E101Q
-
ca. 2% activity of the native enzyme
E107Q
-
ca. 50% activity of the native enzyme
H234S
-
no detectable activity
C144A
-
inactive enzyme
D89A
-
no activity
D89N
-
35% of activity of the 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
H166S
-
inactive 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
complete loss of the activity
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