Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D289A
-
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
-
K232R
-
the mutant protein has lost FBP aldolase activity, whereas the FBP phosphatase activity is 3fold enhanced
Y348F
-
the mutant shows unaltered FBP aldolase activity, but has lost FBP phosphatase activity (less than 5%)
A129S/A165G
-
activity is between 5- to more than 900fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives
D109A
very low catalytic activity
E181A
-
mutant enzyme has wild-type properties
N286A
increased Km, decreased kcat
N286D
increased Km, severely decreased kcat
N35A
-
1.56% activity of the wild-type enzyme
Q59A
-
no significant effect on enzyme function
S61A
-
increased Km for fructose 1,6-bisphosphate
S61T
-
no effect on catalysis
D255A
the mutation results in an enzyme that possesses double specificity, now cleaving D-tagatose 1,6-bisphosphate (albeit with low efficacy) while maintaining activity toward D-fructose 1,6-bisphosphate at a 50fold lower catalytic efficacy compared with that of wild type FBPA
A174D
-
tetramers dissociate into subunits with greatly impaired enzymatic activity, extremely labile mutant, aggregates rapidly
A337V
-
retained tetrameric structure, altered kinetic properties
C239A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
C289A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
C338A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
C72A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
D34S
-
catalytically inactive mutant which still binds to D-fructose 1,6-bisphosphate
E206K
mutant has a KM-value 2fold higher than that of both the Gly346S mutant and the wild-type enzyme, and a turnover-number value 40% less than the wild-type
G346S
mutant enzyme has the same KM-value as the wild-type enzyme, but a 4fold lower turnover-number
Q354E
kinetis resemble that of the wild-type enzyme
R303W
-
retained tetrameric structure, altered kinetic properties
Y363S
-
Y363S has reduced catalytic activity towards D-fructose 1,6-bisphosphate and fructose 1-phosphate
G312A
mutation does not perturb ligand binding in the active site
D34S
-
catalysis-defective mutant enzyme
C-His-rMtFBA
C-terminal histidine-tagged Class II FBA
D276A
about 1% of wild-type activity
E168A
about 30% of wild-type activity
E169A
almost complete loss of activity
G167A
about 3% of wild-type activity
G167A/G166A
about 2% of wild-type activity
C-His-rMtFBA
-
C-terminal histidine-tagged Class II FBA
-
D128V
mutation, mimicking the clinically important D128G mutation in humans
D33N
the mutation drastically reduces the rate of turnover but does not impact substrate binding
D33S
the mutation drastically reduces the rate of turnover but does not impact substrate binding
E189A
almost no loss in catalytic activity
E189Q
only small loss in catalytic activity
H156E
similar kinetics and stability as wild-type enzyme
K229A
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
S271
mutation decreases by 1 order of magnitude the affinity of 1-hydroxy-2-naphthaldehyde 6-phosphate for the aldolase active site but does not modify its ability to catalyze Schiff base formation
D233N
mutant protein is impaired in both aldolase and phosphatase activity
E357Q
mutation abolishes phosphatase activity, no effect on aldolase activity
K232R
mutation abolishes aldolase activity, phosphatase activity is enhanced
Y229F
mutation abolishes aldolase activity, phosphatase activity is slightly reduced
Y358F
mutation abolishes phosphatase activity, no effect on aldolase activity
D233N
-
mutant protein is impaired in both aldolase and phosphatase activity
-
E357Q
-
mutation abolishes phosphatase activity, no effect on aldolase activity
-
K232R
-
mutation abolishes aldolase activity, phosphatase activity is enhanced
-
Y229F
-
mutation abolishes aldolase activity, phosphatase activity is slightly reduced
-
Y358F
-
mutation abolishes phosphatase activity, no effect on aldolase activity
-
Y229F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
Y348F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
Y229F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
-
Y348F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
-
Y146F
catalytically deficient mutant
K156M
-
identical to wild type enzyme
K16M
-
not inhibited by 5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
K239M
-
identical to wild type enzyme
D289A
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
D289A
compound 3g exhibits similar inhibitory activities to the mutant enzyme (0.0031 mM) as compared to wild-type enzyme
R332A
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
R332A
mutation results in 60fold (0.101 mM) increase of Ki value for compound 3g compared with wild-type enzyme Ca-FBA-II (0.0017 mM)
S62A
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
S62A
mutation results in about 15fold increase of the Ki value of S62A (0.0315 mM) as compared to wild-type enzyme
T290A
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
T290A
mutation results in 130fold (0.230 mM) increase of Ki value for compound 3g as compared with wild-type enzyme Ca-FBA-II (0.0017 mM)
S62A
-
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
-
S62A
-
mutation results in about 15fold increase of the Ki value of S62A (0.0315 mM) as compared to wild-type enzyme
-
T290A
-
the mutant enzyme exhibits higher resistance against inhibitor (2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine compared to the wild type
-
T290A
-
mutation results in 130fold (0.230 mM) increase of Ki value for compound 3g as compared with wild-type enzyme Ca-FBA-II (0.0017 mM)
-
D144A
increased Km
D144A
-
residue is involved in ligating the secondary zinc atom. Mutant exhibits enhancement of enzymatic activity by added nickel
E174A
-
severely crippled catalysis
E174A
-
residue is involved in ligating the secondary zinc atom. Mutant is insensitive to nickel
D83A
inactive
D83A
-
impaired enzyme activity
A149P
no catalytic activity
A149P
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
L256P
melting temperature is 40°C versus 47°C for the wild-type enzyme
L256P
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
N334K
increased Km value
N334K
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
W147R
melting temperature is 40°C versus 47°C for the wild-type enzyme
W147R
-
retained tetrameric structure, altered kinetic properties
E187A
mutation compromises enzyme activity
E187A
the mutation drastically reduces the rate of turnover
E187Q
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
E187Q
mutation compromises enzyme activity
E187Q
the mutation drastically reduces the rate of turnover
K107M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K107M
46fold increase in Ki-value for naphthyl 2,6-bisphosphate, 11.5fold increase in KM-value for D-fructose 1,6-diphosphate. The structure of the enzyme is isomorphous with respect to wild-type enzyme
K107M
the mutation drastically reduces the rate of turnover
K146A
is unable to cleave the C3-C4 bond of the hexose while retaining the ability to form the covalent intermediate, although at a greatly diminished rate
K146A
the mutation drastically reduces the rate of turnover
K146M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K146M
decrease in rate of complex formation between enzyme and inhibitor 1-hydroxy-2-naphthaldehyde 6-phosphate, but no change in ability to form the complex
K146M
mutant with severely compromised catalytic activity
K146M
the mutation drastically reduces the rate of turnover
K229M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K229M
residual background activity
additional information
-
methionine/cysteine-conditional mutant MET3-FBA1/fba1 shows strongly reduced enzyme expression
additional information
-
isolation of thermostable variants of the class II fructose bisphosphate aldolase following four rounds of directed evolution using DNA shuffling of the fda gene. The variants show increased thermostability with no loss of catalytic function at room temperature
additional information
isolation of thermostable variants of the class II fructose bisphosphate aldolase following four rounds of directed evolution using DNA shuffling of the fda gene. The variants show increased thermostability with no loss of catalytic function at room temperature
additional information
-
isolation of thermostable variants of the class II fructose bisphosphate aldolase following four rounds of directed evolution using DNA shuffling of the fda gene. The variants show increased thermostability with no loss of catalytic function at room temperature
additional information
-
chimeric enzymes between two human aldolases A, B, or C with different catalytic properties
additional information
AB_All mutant, isozyme-specific residues from aldolase B swapped into aldolase A and vice versa, decreased Km and kcat compared to aldolase A, similar Km and kcat to aldolase B
additional information
sll1330 deletion mutant
4.1.2.13 fructose-bisphosphate aldolase
results (
results (
top
