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C163A
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synthase I, site-directed mutagenesis, active site mutant, no activity, but decarboxylates malonyl-[acyl-carrier-protein]
C163S
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synthase I, site-directed mutagenesis, active site mutant, increased activity, decarboxylates malonyl-[acyl-carrier-protein]
D306A
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synthase I, site-directed mutagenesis, active site mutant, increased activity
E309A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298E
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site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.08.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H298Q
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site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H333A
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synthase I, site-directed mutagenesis, active site mutant, increased activity
K151Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
K328E
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328F
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site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328H
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site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328I
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328R
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient, crystal structure determination with the free mutant enzyme, comparison to the wild-type enzyme structure
K63Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R62Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R66Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
C171Q
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mimics the acyl enzyme intermediate
D66N
the non-active site mutation alters the structural stability of the mutant protein structures
F413L
the non-active site mutation alters the structural stability of the mutant protein structures
G269S
the non-active site mutation alters the structural stability of the mutant protein structures
G312S
the non-active site mutation alters the structural stability of the mutant protein structures
R161A
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69.6% of wild-type activity
R46A
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7.3% of wild-type activity
R46A/R161A
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0.3% of wild-type activity
T97F
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no enzymic activity
W42A
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21.5% of wild-type activity
W42A/R161A
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0.2% of wild-type activity
D66N
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the non-active site mutation alters the structural stability of the mutant protein structures
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F413L
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the non-active site mutation alters the structural stability of the mutant protein structures
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G269S
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the non-active site mutation alters the structural stability of the mutant protein structures
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G312S
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the non-active site mutation alters the structural stability of the mutant protein structures
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C161Q
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site-directed mutagenesis, active site Cys mutant, no condensation activity, but 377fold increased decarboxylation activity
C122A
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site-directed mutagenesis, 75% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
C122Q
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site-directed mutagenesis, 500% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
C122S
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site-directed mutagenesis, enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type
A193M
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site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 2.55fold, 12fold reduced catalytic activity
I108F
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site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 1.75fold, 38fold reduced catalytic activity towards octanoyl-[acyl-carrier-protein] compared to the activity towards hexanoy-[acyl-carrier-protein]
K328A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
K328A
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site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
additional information
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transformation of Brassica napus via Agrobacterium tumefaciens infection with binary vector overexpressing Escherichia coli fabH gene, targeted expression in cytoplasm and plastids is seed specific, modified fatty acid profile of seed oil
additional information
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transformation of Brassica napus via Agrobacterium tumefaciens infection with binary vector overexpressing Escherichia coli fabH gene, targeted expression in cytoplasm and plastids is seed specific, modified fatty acid profile of seed oil
additional information
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introduction of temperature-sensitive mutation in fabB into strain K27 by phage P1-mediated transduction using closely linked Tn10 insertion as selectable marker. A fabB mutant strain accumulates less cis-5-dodecenoic acid than the parental wild-type strain. The wild-type strain also accumulates 2.7fold more cis-7-tetradecenoate than the fabB(Ts) strain. The combination of null mutations in fadD and fabA or fabB is synthetically lethal even in the presence of oleic acid supplementation. A temperature-sensitive mutation is used rather than null mutations because a strain having fabB null mutation has an obligate requirement for an unsaturated fatty acid and FabD is required for uptake of the supplement
additional information
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in-frame deletion of enzyme active site region, mutant strain retains about 10% enzymic activity and fails to grow in the absence of supplementation with exogenous long-chain fatty acids. Mutant requires only long-chain unsaturated fatty acids, no saturated fatty acids
additional information
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construction of a mutant hybrid gene OskasI from of subssp. indica and japonica, that results in a short root phenotype
additional information
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triple and quadruple mutants of fatty acid synthase complex including mutation sites in the beta-ketoacyl-[acyl-carrier-protein] synthase. e.g. H293A, H331A, K326A,S581A, kinetics, overview
additional information
construction of FAS or ELO enzyme-deficient mutant strains by RNA interference or gene disruption, ACP depletion by RNAi or gene knockout reduces lipoic acid levels and drastically decreases protein lipoylation
additional information
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construction of FAS or ELO enzyme-deficient mutant strains by RNA interference or gene disruption, ACP depletion by RNAi or gene knockout reduces lipoic acid levels and drastically decreases protein lipoylation