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

BRENDA support

2.3.2.5: glutaminyl-peptide cyclotransferase

This is an abbreviated version!
For detailed information about glutaminyl-peptide cyclotransferase, go to the full flat file.

Word Map on EC 2.3.2.5

Reaction

L-glutaminyl-peptide
=
5-Oxoprolyl-peptide
 +
NH3

Synonyms

AtQC, cyclotransferase, glutaminyl-transfer ribonucleate, DromeQC, gamma-glutamylamine cyclotransferase, GGACT, glutamine cyclotransferase, glutaminyl cyclase, glutaminyl-peptide cyclotransferase-like protein, glutaminyl-tRNA cyclotransferase, golgi resident enzyme, Golgi resident glutaminyl cyclase, Golgi-resident enzyme, Golgi-resident glutaminyl cyclase, gQC, h-isoQC, h-QC, hQC, isoDromeQC, isoGlutaminyl cyclase, isoQC, PgQC, QC, QCT, Qpct, Qpct1, QPCTL, secretory glutaminyl cyclase, sQC, StQC

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.5 glutaminyl-peptide cyclotransferase

Engineering

Engineering on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase

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
C113A/C136A
mutant of isoform DromeQC lacking a disulfide bond, without influence on the stability of the enzyme
C136A/C158A
mutant of isoform isoDromeQC lacking a disulfide bond, without influence on the stability of the enzyme
C369A
-
improvement of enzyme secretion (expressed in Pichia pastoris)
D248A
D248Q
-
kcat/KM for Gln-2-naphthylamide is 7123fold lower than wild-type value
D305A
D305E
-
kcat/KM for Gln-2-naphthylamide is 21000fold lower than wild-type value
D305L
no activity
D305N
-
kcat/KM for Gln-2-naphthylamide is 772fold lower than wild-type value
E201D
E201L
site-directed mutagenesis, the mutant is inactive, the side chain of L201 has oriented away from the D305 in the mutant structure
E201Q
E225G
site-directed mutagenesis, the mutant shows reduced enzymatic activity compared to wild-type
F146A
the ratio of turnover-number to KM-value for Gln-Gln at pH 8.0 is 1.43fold lower than wild-type ratio
F325A
F325N
the mutant shows a 815fold increase in Ki of PBD150 compared to the wild type enzyme
F325Y
the mutant shows a 381fold increase in Ki of PBD150 compared to the wild type enzyme
H140Q
-
inactive enzyme
H307Q
-
mutant enzyme with increased KM-value
H319L
-
kcat/KM for Gln-2-naphthylamide is 15fold lower than wild-type value
H319Q
-
mutant enzyme with increased KM-value
H330Q
-
inactive enzyme
I303A
the mutation results in a 66.3fold increase in the Ki value of PBD150 compared to the wild type enzyme
I303F
the mutation results in a 6.2fold increase in the Ki value of PBD150 compared to the wild type enzyme
I303N
the mutation results in a 112fold increase in the Ki value of PBD150 compared to the wild type enzyme
I303V
the mutation results in a 1.9fold increase in the Ki value of PBD150 compared to the wild type enzyme
I73N
-
artificial glycosylation site
I73N/C369A
-
further improvement of enzyme secretion (expressed in Pichia pastoris)
K144A
K144M
the mutant shows a 335fold increase in Ki of PBD150 compared to the wild type enzyme
K144R
the mutant shows a 237fold increase in Ki of PBD150 compared to the wild type enzyme
N49A
-
mutant enzyme is not glycosylated, kinetic properties are indistinguishable from unmutated enzyme
Q304L
the ratio of turnover-number to KM-value for Gln-Gln at pH 8.0 is 1.7fold lower than wild-type ratio
R54W
the ratio of turnover-number to KM-value for Gln-Gln at pH 8.0 is 1.4fold lower than wild-type ratio
S160A
-
kcat/KM for Gln-2-naphthylamide is 3fold lower than wild-type value
S160G
S323A
the mutation leads to a significant decrease (0.2fold) in the Ki value of PBD150 compared to the wild type enzyme
S323T
the mutation leads to a significant decrease (0.21fold) in the Ki value of PBD150 compared to the wild type enzyme
S323V
the mutation leads to a strong decrease (0.074fold) in the Ki value of PBD150 compared to the wild type enzyme
W207F
W207L
W207Q
the mutation alters substrate conversion significantly, while the binding constants of inhibitors such as the highly potent PBD150 are minimally affected
W329A
the ratio of turnover-number to KM-value for Gln-Gln at pH 8.0 is 297fold lower than wild-type ratio
W329F
the mutation leads to a significant decrease (0.56fold) in the Ki value of PBD150 compared to the wild type enzyme
W329Y
the mutation does not affect the Ki of PBD150 compared to the wild type enzyme
Y115E/Y117E
Y299A
the mutant shows a 122fold increase in Ki of PBD150 compared to the wild type enzyme
Y299F
the mutant shows a 220fold increase in Ki of PBD150 compared to the wild type enzyme
I74N
-
artificial glycosylation site
Q46E
the mutant’s pH optimum is shifted towards lower pH values, although the activity towards L-glutamine-2-naphtylamine is some 1000fold lower than the wild type
E45A
the mutation leads to a drop in the enzyme activity (1.12% activity compared to the wild type enzyme)
E45Q
the mutation increases the enzyme activity by an order of magnitude (1079.68% activity compared to the wild type enzyme)
E89A
the mutant exhibits 5.46% activity compared to the wild type enzyme
F43A
the mutant exhibits 5.46% activity compared to the wild type enzyme
F87A
the mutant exhibits 3.87% activity compared to the wild type enzyme
W103A
the mutant exhibits 3.05% activity compared to the wild type enzyme
E45A
-
the mutation leads to a drop in the enzyme activity (1.12% activity compared to the wild type enzyme)
-
E45Q
-
the mutation increases the enzyme activity by an order of magnitude (1079.68% activity compared to the wild type enzyme)
-
E89A
-
the mutant exhibits 5.46% activity compared to the wild type enzyme
-
F87A
-
the mutant exhibits 3.87% activity compared to the wild type enzyme
-
W103A
-
the mutant exhibits 3.05% activity compared to the wild type enzyme
-
E48Q
the mutant’s pH optimum is shifted towards higher pH values
additional information