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V77Q/N153Y/A286K
the mutant, which is not able to form disulfide bonds, exhibits higher activity than the wild type enzyme
C377A
site-directed mutagenesis, almost inactive mutant
C378A
site-directed mutagenesis, almost inactive mutant
C89A
site-directed mutagenesis, almost inactive mutant
C91A
site-directed mutagenesis, almost inactive mutant
F156A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H347A
site-directed mutagenesis, almost inactive mutant
H348A
site-directed mutagenesis, almost inactive mutant
K17A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
K18A
site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
K217A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
M124A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q151A
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
R210A
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
R220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V231A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C377A
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site-directed mutagenesis, almost inactive mutant
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C89A
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site-directed mutagenesis, almost inactive mutant
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C91A
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site-directed mutagenesis, almost inactive mutant
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F156A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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K17A
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site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
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K18A
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site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
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K217A
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site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
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Q151A
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site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
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R210A
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site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
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R220A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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M193T
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naturally occuring mutation leading to enzyme deficiency and to the ketoacidotic episode phenotype, but with differing clinical severity, overview
Q272X
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no residual activity under any condition
C92S
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kcat decreases to 0.2% of that for the recombinant thiolase
C378G
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mutation eliminates the ability of thiolase to catalyze proton abstraction from C2 of acetyl-CoA
C89A
no thiolytic activity towards acetoacetyl-CoA
Q64A
30% lower kcat than that of the wild-type
E252del
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relative protein amount and enzyme activity of 30% and 25% respectively, in comparison to the wild-type at 37°C. 2fold Km-elevation for substrates coenzyme A and acetoacetyl-CoA compared to wild-type values. Vmax is comparable to wild-type value
E252del
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25% of wild-type activity at 37°C, 40% of wild-type activity at 30°C. Mutant is unstable compared to the wild-type protein at 37°C. KM-value for acetoacetyl-CoA is 2fold higher than wild-type value. Km-value for CoA is 1.8fold lower than wild-type value
E252del
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no residual activity under any condition
N158D
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inactive mutant protein
N158D
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no residual activity under any condition
N158S
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inactive mutant protein
N158S
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no residual activity under any condition
N282H
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inactive mutant protein
N282H
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no residual activity under any condition
N353K
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cDNAs yield neither residual T2 protein nor enzyme activity
N353K
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no residual activity under any condition
Q73P
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cDNAs yield neither residual T2 protein nor enzyme activity
Q73P
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no residual activity under any condition
R208Q
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inactive mutant protein
R208Q
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no residual activity under any condition
Y219H
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inactive mutant protein
Y219H
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no residual activity under any condition
additional information
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation
additional information
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation
additional information
-
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation
additional information
the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
additional information
the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
additional information
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the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
additional information
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the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
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additional information
-
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation
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additional information
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naturally occurring mutations analyzed
additional information
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a single-base substitution (c.1124A>G) activates a 5-base upstream cryptic splice donor site within exon 11 in the human mitochondrial acetoacetyl-CoA thiolase gene