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Q47L
the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme
T173S
the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme
Q47L
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the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme
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T173S
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the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme
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A154T
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similar thermal stability as wild-type enzyme
A154T/E233K
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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
E233K
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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
F87T
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coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources
D42A
the mutant shows 36% activity with acetoacetyl-CoA and NADH, 20% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 26% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K152A
the mutant shows 109% activity with acetoacetyl-CoA and NADH, no activity with acetoacetyl-CoA and NADPH, 123% activity with 9,10-phenanthrene and NAD+, and 2.2% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K169E
the mutant shows 95% activity with acetoacetyl-CoA and NADH, 5.5% activity with acetoacetyl-CoA and NADPH, 76% activity with 9,10-phenanthrene and NAD+, and 6% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K173A
the mutant shows 0.3% activity with acetoacetyl-CoA and NADH, 2.4% activity with acetoacetyl-CoA and NADPH, 6% activity with 9,10-phenanthrene and NAD+, and 22% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/K169E
the mutant shows 156% activity with acetoacetyl-CoA and NADH, 4.3% activity with acetoacetyl-CoA and NADPH, 84% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/R168E/K169E
the mutant shows 72% activity with acetoacetyl-CoA and NADH, 0.5% activity with acetoacetyl-CoA and NADPH, 40% activity with 9,10-phenanthrene and NAD+, and no activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R168E
the mutant shows 106% activity with acetoacetyl-CoA and NADH, 6.3% activity with acetoacetyl-CoA and NADPH, 38% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R34A
the mutant shows 102% activity with acetoacetyl-CoA and NADH, 100% activity with acetoacetyl-CoA and NADPH, 40.44% activity with 9,10-phenanthrene and NAD+, and 2.1% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Y169A
the mutant shows 3% activity with acetoacetyl-CoA and NADH, 2% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 15% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
S140A
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mutant shows no enzymatic activity. S140A mutant does not bind to NADPH
S140T
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mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding
R187A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 3fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187A/R230A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 4fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E/R230E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 80fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187K
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no decreased affinity binding to acyl-carrier protein with respect to wild-type
R230A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R230E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 41fold decreased affinity binding to acyl-carrier protein with respect to wild-type
S36A
the mutant shows reduced activity compared to the wild type enzyme
S40A
the mutant shows reduced activity compared to the wild type enzyme
E233K
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
M125I/S233T
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
G141A
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the mutant shows less than 5% of wild type activity
G92A
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the mutant shows less than 60% of wild type activity
G92D
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the mutant shows less than 5% of wild type activity
Q152A
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the mutant shows less than 10% of wild type activity
Y155F
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the mutant shows less than 3% of wild type activity
additional information
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insertional mutants in KCR1 and KCR2
additional information
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter. In plants with altered reductase activity, total seed yield is reduced in all cases. In less severely affected plant lines, seeds have a normal appearance and composition but the yield of seeds is reduced by approximately 50%. In more severely affected lines, reductions in both seed fatty acid content and the number of seeds produced per plant are evident, resulting in a 90% reduction in fatty acid synthesized per plant. Phenotypes are independent of the promoter used. In severely affected lines, a large proportion of seeds show precocious germination, and these have a reduced oleate content and increased levels of polyunsaturated 18-carbon fatty acids, compared with normal seeds of the same line
additional information
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transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter. In plants with altered reductase activity, total seed yield is reduced in all cases. In less severely affected plant lines, seeds have a normal appearance and composition but the yield of seeds is reduced by approximately 50%. In more severely affected lines, reductions in both seed fatty acid content and the number of seeds produced per plant are evident, resulting in a 90% reduction in fatty acid synthesized per plant. Phenotypes are independent of the promoter used. In severely affected lines, a large proportion of seeds show precocious germination, and these have a reduced oleate content and increased levels of polyunsaturated 18-carbon fatty acids, compared with normal seeds of the same line
additional information
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glutathione-S-transferase fusion protein without transit peptide, expressed in Escherichia coli
additional information
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mutant cells lacking the homologous mitochondrial FASII enzyme 3-oxoacyl-ACP reductase Oar1p
additional information
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oar1-DELTA mutants, lack 3-oxoacyl-ACP reductase acitivity, expression of FabG4 gene of Mycobacterium tuberculosis