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A144T/T150S
site-directed mutagenesis
A337S
site-directed mutagenesis, shows activity unaltered to the wild-type enzyme
E169A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
E312V
site-directed mutagenesis
G342D
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
G56S
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
K372R
site-directed mutagenesis, inactive mutant
L122V
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
M1L/M4L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L/M58
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M52L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M4L/M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
N160K
site-directed mutagenesis, inactive mutant
N202S
site-directed mutagenesis
S166N
site-directed mutagenesis
S9R
site-directed mutagenesis, a transit peptide mutant, inactive mutant
T150S
site-directed mutagenesis, inactive mutant
T198A
site-directed mutagenesis, shows activity similar to the wild-type enzyme
V316F
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
V43N
site-directed mutagenesis, a transit peptide mutant, shows activity similar to the wild-type enzyme
E169A
-
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
-
G56S
-
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
-
L122V
-
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
-
M1L/M4L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M52L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M52L/M58
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M58L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M52L/M58L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
S9R
-
site-directed mutagenesis, a transit peptide mutant, inactive mutant
-
T198A
-
site-directed mutagenesis, shows activity similar to the wild-type enzyme
-
DELTA48
a truncated version of soybean ATPS lacking the first 48 amino acids is generated for protein expression and purification, removal of the putative localisation sequence improves the yield of N-terminally His-tagged protein in Escherichia coli
F245A
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
F245L
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
H252N
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
H255A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
H255Q
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
H333Q
site-directed mutagenesis, shows highly increased activity compared to the wild-type enzyme
L258A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
L258V
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
N249A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
N249D
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Q246A
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Q246E
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Q246N
site-directed mutagenesis, shows very highly increased activity compared to the wild-type enzyme
R248K
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
R349K
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
C53A
-
mutation has no effect on activity
C77A
-
mutation has no effect on activity
C84A
-
mutation has no effect on activity
D523A
-
no sulfurylase activity, reduced PAPS kinase activity
G59A
-
significant effect on ATP sulfurylase activity, no effect on adenosine 5'-phosphosulfate kinase activity
G62A
-
mutation has no effect on activity
G64A
-
diminished adenosine 5'-phosphosulfate kinase activity
H425A
-
no sulfurylase activity
H428A
-
no sulfurylase activity
H506A
-
mutant enzyme shows 91% of the sulfurylase activity compared to that of the wild-type enzyme, reduced PAPS kinase activity
K65A
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
K65R
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
R421A
-
no sulfurylase activity
R421K
-
mutant enzyme shows 8% of the sulfurylase activity compared to that of the wild-type enzyme
R468A
-
no sulfurylase activity
R510A
-
mutant enzyme shows 90% of the sulfurylase activity compared to that of the wild-type enzyme
R522A
-
no sulfurylase activity
R522K
-
no sulfurylase activity
T66A
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
del396-573
recombinant ATP sulfurylase lacking the C-terminal allosteric domain is monomeric and noncooperative. Mutant enzyme is less heat stable than wild-type enzyme. Wild-type enzyme behaves cooperative at pH 6.5, truncated enzyme form displays normal hyperbolic behavior
additional information
the plant enzymes only contain ATP sulfurylase domain, unlike the human and yeast enzymes which include an APS kinase domain, located at the N- or C-terminal regions, respectively
additional information
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the plant enzymes only contain ATP sulfurylase domain, unlike the human and yeast enzymes which include an APS kinase domain, located at the N- or C-terminal regions, respectively
additional information
enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
additional information
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enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
additional information
knockdown of PAPSS1 and 2 in HepG2 cells
additional information
-
knockdown of PAPSS1 and 2 in HepG2 cells