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D233A
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catalytic activity is neligible
D233E
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decrease in catalytic efficiency by factor 9
D233N
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catalytic activity is neligible
D236A
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increase in enzyme affinity for substrate
D236E
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kinetics similar to wild-type
D236N
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increase in enzyme affinity for substrate
D392A
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decrease of both kcat and Km value
D392E
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2fold increase in kcat value without affecting Km value
D392N
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2fold increase in kcat value without affecting Km value
H189A
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slight increase of Km value with 6fold decrease in kcat value
H189D
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4fold increase in kcat value without affecting Km value
H189E
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2fold increase in kcat value without affecting Km value
H323A
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kinetics similar to wild-type
H323Q
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kinetics similar to wild-type
H376D
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60% increase in catalytic efficiency
H376N
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twofold increase in catalytic efficiency
R237A
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4fold increase in Km value
R237K
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6fold increase in Km value
R237Q
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3fold increase in Km value
D21A
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D23A
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D256A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
D306A
HD domain mutant with 2',3'-cyclic phosphodiesterase activity
H225A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
H305A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
F235A
the mutant shows near-complete catalytic inactivation
F235L
the mutant shows near-complete catalytic inactivation
P225G
the mutant shows increased activity compared to the wild type enzyme
P296G
the mutant shows slightly increased activity compared to the wild type enzyme
R307Q
the mutant shows reduced activity compared to the wild type enzyme
T232A
the mutant shows near-complete catalytic inactivation
T311A
the mutant shows near-complete catalytic inactivation
Y168A
the mutant shows near-complete catalytic inactivation
Y168S
the mutant shows reduced activity compared to the wild type enzyme
C231A
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CNP1 catalytic fragment mutant, kinetics
C231S
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CNP1 catalytic fragment mutant, kinetics
C236A
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CNP1 catalytic fragment mutant, kinetics
C236S
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CNP1 catalytic fragment mutant, kinetics
C314A
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CNP1 catalytic fragment mutant, kinetics
C314S
-
CNP1 catalytic fragment mutant, kinetics
C397S
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CNP1 catalytic fragment mutant, kinetics
H230A/T232A/H309A/T311A
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catalytically inactive
H230F
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almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H230L
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almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H309F
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almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H309L
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almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
S22A
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CNP2 mutant with reduced phosphate incorporation
S9A
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CNP2 mutant with reduced phosphate incorporation
S9A/S22A
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CNP2 double mutant without phosphate incorporation
H230Q
inactive
H230Q
site-directed mutagenesis, the mutation of the active site residue highly reduces the enzyme activity compared to the wild-type enzyme
H230Q/H309Q
inactive
H230Q/H309Q
site-directed mutagenesis, the mutation of the active site residue completely abolishes enzyme activity compared to the wild-type enzyme
H230S
inactive
H230S
site-directed mutagenesis, the mutation of the active site residue highly reduces enzyme activity compared to the wild-type enzyme
H309Q
inactive
H309Q
site-directed mutagenesis, the mutation of the active site residue highly reduces enzyme activity compared to the wild-type enzyme
H309S
the mutant shows strongly reduced activity compared to the wild type enzyme
H309S
site-directed mutagenesis, the mutation of the active site residue completely abolishes enzyme activity compared to the wild-type enzyme
V321A
the mutant shows reduced activity compared to the wild type enzyme
V321A
site-directed mutagenesis, Val321 stacks against the substrate adenine ring, the mutation does not affect kcat significantly but doubles Km, indicating a functional active site but slightly compromised substrate binding
additional information
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additional information
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CNP1 promoter deletion and replacement mutants, effect on the stimulatory effect of cAMP on CNP1 gene expression
additional information
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enzyme overexpression induces dramatic morphology changes in both glial and nonglial cells, resulting in microtubule and F-actin reorganization and formation of branched processes. Cultured oligodendrocytes from enzyme-deficient mice extend smaller outgrowths with less arborized processes
additional information
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enzyme knockdown by siRNA knockdown of CNPase in BV-2 cells
additional information
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C-terminal deletion of 13 amino acids of CNP1 leads to an abnormal microtubule distribution in the cell
additional information
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CNP1: N-terminal deletion mutants, catalytic fragment corresponding to the last C-terminal 250 amino acids
additional information
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expression of enzyme in yeast can complement growth of strains bearing lethal or temperature-sensitive mutations in the tRNA ligase 3'-end-healing domain
additional information
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CNP-CF is a CNP1 deletion mutant lacking the first 150 amino acids
additional information
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generation of inactive mutants truncated after amino acid 164
additional information
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generation of truncated enzyme mutants: CNP_20-398, CNP_25-398, CNP_20-420, CNP_20-185, and CNP_179-398, analysis of calmodulin binding activity