2.3.1.180: beta-ketoacyl-[acyl-carrier-protein] synthase III
This is an abbreviated version!
For detailed information about beta-ketoacyl-[acyl-carrier-protein] synthase III, go to the full flat file.
Word Map on EC 2.3.1.180
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2.3.1.180
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malonyl-acp
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thiolactomycin
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transacylase
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mycolic
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drug development
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acyl-acps
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claisen
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glaucescens
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isobutyryl-coa
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transacylation
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cuphea
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pharmacology
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malonyl-coa:acp
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bcfas
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synthesis
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biofuel production
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medicine
- 2.3.1.180
- malonyl-acp
- thiolactomycin
-
transacylase
-
mycolic
- drug development
- acyl-acps
-
claisen
- glaucescens
- isobutyryl-coa
-
transacylation
- cuphea
- pharmacology
-
malonyl-coa:acp
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bcfas
- synthesis
- biofuel production
- medicine
Reaction
Synonyms
3-ketoacyl ACP synthase III, 3-ketoacyl acyl carrier protein synthase III, 3-ketoacyl carrier protein synthase III, 3-ketoacyl-(acyl carrier protein) synthase IIIA, 3-ketoacyl-(acyl carrier protein) synthase IIIB, 3-ketoacyl-ACP synthase III, 3-ketoacyl-acyl carrier protein synthase III, 3-ketoacyl-acyl-carrier protein synthase III, 3-oxoacyl-ACP synthase III, 3-oxoacyl-acyl carrier protein synthase III, 3-oxoacyl-[acyl-carrier-protein] synthase III, 3-oxoacyl:ACP synthase III, AbyA1, acetoacetyl-ACP synthase, acetyl-CoA:ACP transacylase, acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase, ACO synthase III, ACP synthase III, AknE2, AlnI, AsuC3, AsuC4, AviN, BenQ, beta-ketoacyl (acyl carrier protein) synthase III, beta-ketoacyl acyl carrier protein synthase III, beta-ketoacyl acyl-carrier protein synthase III, beta-ketoacyl-(ACP) synthase III, beta-ketoacyl-(acyl-carrier-protein) synthase III, beta-ketoacyl-ACP III, beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP synthase III, beta-ketoacyl-ACP synthase III-like protein, beta-ketoacyl-ACP-synthase III, beta-ketoacyl-acyl carrier protein (ACP) synthase III, beta-ketoacyl-acyl carrier protein synthase III, beta-ketoacyl-acyl carrier protein synthase-III, beta-ketoacyl-[acyl-carrier protein (ACP)] synthase III, beta-ketoacyl-[acyl-carrier-protein] synthase III, beta-ketoacyl:acyl carrier protein synthase III, beta-ketoacylacylcarrier protein synthase III, beta-ketobutyryl-ACP synthase, BomK, CalO4, CerJ, ChlB3, ChlB6, CorB, DarB, DpsC, ecFabH, ecKAS III, efFabH, EsmD1, EvrI, FabH, FabH1, FabH2, FabH3, FabHA, FabHB, fatty acid biosynthesis, enzyme H, fatty acid synthase type II condensing enzyme, FdmS, FrenI/FrnI, HedS, hiFabH, initiation ketosynthase, JcKAS III, KAS III, KAS III-like protein, KAS IIIA, KAS IIIB, KAS-III, KAS3a, KAS3b, KASIII, KijB, LstA, LstAB, LstB, mtFabH, MxnB, nmFabH, NphT7, NzsF, paFabH, PpyS, PqsBC, PqsD, PtmR, RedP, RevR, RkD, saFabH, SalQ/Orf12, short-chain condensing enzyme, spFabH, spyFabH, SsfN, TcsB, ThgI, TiaF, Tmn15, [acyl-carrier-protein] synthase III
ECTree
2.3.1.180 beta-ketoacyl-[acyl-carrier-protein] synthase IIIAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.180 - beta-ketoacyl-[acyl-carrier-protein] synthase III
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F56W
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the mutation does not show a drastic change in reactivity towards octanoyl-CoA even though the band of the variant is reduced approximately by 40% compared to the wild type
A294S
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
A295P
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
C111A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
C111S
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site-directed mutagenesis, the mutant enzyme loses all condensing activity, but is still able to bind acetyl-CoA and malonyl-ACP and to decarboxylate the latter to acetyl-ACP
C111S/H261A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
C111S/H261R
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site-directed mutagenesis, the mutant enzyme loses all condensing activity, but is still able to bind acetyl-CoA and malonyl-ACP and to decarboxylate the latter to acetyl-ACP
H261A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
H261R
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
N291D
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
R150A
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
R266A
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
R306A
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site-directed mutagenesis, the mutant enzyme shows highly reduced condensing activity compared to the wild-type enzyme
C112S
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site-directed mutagenesis, the mutant enzyme shows abolished condensation and transacylation activities, but 4fold increased decarboxylation activity compared to the wild-type enzyme
F87A
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87C
F87C/H244A
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H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87D
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87E
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87G
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87H
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87I
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87I/H244A
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H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87K
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87L
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87M
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87N
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87P
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87Q
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87R
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87S
F87S/N274A
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N274 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87T
F87T/H244A
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H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87V
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87W
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87Y
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
H244A
H244A/N274A
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N274 and H244 play key roles in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
N274A
C122A
site-directed mutagenesis, the mutant shows 0.25% of wild-type enzyme condensation activity, and 2.4% of wild-type malonyl-ACP decarboxylation activity
H258A
site-directed mutagenesis, the mutant shows 0.46% of wild-type enzyme condensation activity, and 0.68% of wild-type malonyl-ACP decarboxylation activity
N289A
site-directed mutagenesis, the mutant shows 0.51% of wild-type enzyme condensation activity, and 2.24% of wild-type malonyl-ACP decarboxylation activity
R161A
site-directed mutagenesis, the mutant shows 69.7% of wild-type enzyme condensation activity, and 8.7% of wild-type malonyl-ACP decarboxylation activity
R46A
site-directed mutagenesis, the mutant shows 7.3% of wild-type enzyme condensation activity, and 0.79% of wild-type malonyl-ACP decarboxylation activity
R46A/R161A
site-directed mutagenesis, the mutant shows 0.31% of wild-type enzyme condensation activity, and 5.1% of wild-type malonyl-ACP decarboxylation activity
T45A
the mutant exhibits slightly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
T45D
the mutant exhibits markedly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
T97F
site-directed mutagenesis, the mutant shows 0.47% of wild-type enzyme condensation activity, and 0.84% of wild-type malonyl-ACP decarboxylation activity
W42A
site-directed mutagenesis, the mutant shows 21.6% of wild-type enzyme condensation activity, and 30.1% of wild-type malonyl-ACP decarboxylation activity
W42A/R161A
site-directed mutagenesis, the mutant shows 0.24% of wild-type enzyme condensation activity, and 9.7% of wild-type malonyl-ACP decarboxylation activity
C122A
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site-directed mutagenesis, the mutant shows 0.25% of wild-type enzyme condensation activity, and 2.4% of wild-type malonyl-ACP decarboxylation activity
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R161A
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site-directed mutagenesis, the mutant shows 69.7% of wild-type enzyme condensation activity, and 8.7% of wild-type malonyl-ACP decarboxylation activity
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R46A
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site-directed mutagenesis, the mutant shows 7.3% of wild-type enzyme condensation activity, and 0.79% of wild-type malonyl-ACP decarboxylation activity
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T45A
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the mutant exhibits slightly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
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T45D
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the mutant exhibits markedly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
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T97F
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site-directed mutagenesis, the mutant shows 0.47% of wild-type enzyme condensation activity, and 0.84% of wild-type malonyl-ACP decarboxylation activity
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W42A
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site-directed mutagenesis, the mutant shows 21.6% of wild-type enzyme condensation activity, and 30.1% of wild-type malonyl-ACP decarboxylation activity
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C122A
-
site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 75% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
C122Q
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site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 500% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
C122S
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site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 100% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
additional information
F87C
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87S
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87T
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87T
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coexpression of the enzyme in Arabidopsis thaliana plastids with Ser325Thr/Gln481Lys mutated polyhydroxyalkanoate synthase from Pseudomonas sp. 61-3, along with the beta-ketothiolase PhaA and acetoacetyl-CoA reductase PhaB from Ralstonia eutropha for successful production of short-chain-length/medium-chain-length polyhydroxyalkanoates in the transgenic plant plastids, expression of the engineered fabH gene in the plastid leads to an increase in the amount of the SCL monomer, 3-hydroxybutyrate, incorporated into polyhydroxyalkanoates, and contributes to supply of medium-chain-length monomers for polyhydroxyalkanoate production, overview
H244A
-
site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but 6fold increased transacylation activity compared to the wild-type enzyme
H244A
-
H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding, in the mutant stabilization is reduced inhibiting the condensation reaction, leading to an increase in transacylase activity, allowing larger substrates to be subjected to acyl-ACP to acyl-CoA transacylation
N274A
-
site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but about 20% increased transacylation activity compared to the wild-type enzyme
N274A
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N274 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
additional information
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coexpression of the KASIII mutant F87T enzyme from Escherichia coli in Arabidopsis thaliana plastids together with Ser325Thr/Gln481Lys mutated polyhydroxyalkanoate synthase from Pseudomonas sp. 61-3, along with the beta-ketothiolase PhaA and acetoacetyl-CoA reductase PhaB from Ralstonia eutropha for successful production of short-chain-length/medium-chain-length polyhydroxyalkanoates in the transgenic plant plastids, expression of the engineered Escherichia coli fabH gene in the plastid leads to an increase in the amount of the SCL monomer, 3-hydroxybutyrate, incorporated into polyhydroxyalkanoates, and contributes to supply of medium-chain-length monomers for polyhydroxyalkanoate production, overview
additional information
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transfection with Cuphea glaucescens isozymes KAS III-1 and KAS III-2 leads to altered fatty acid levels with accumulation of palmitate
additional information
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analysis of fatty acid composition and acyl-ACP content of transgenic plants expressing the two isozymes of Cuphea glaucescens, the transgenic plants show altered fatty acid levels with accumulation of palmitate
additional information
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construction of an enzyme-deficient null mutant strain in which the gene encoding the enzyme from Salmonella enterica serovar typhimurium is inserted as a single copy or in two copies, removal of one of the two copies reduces enzyme activity, removal of the single copy of the gene leads to cell death revealing that the enzyme is absolutely essential for viability, overview
additional information
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construction of transgenic Brassica napus plants overexpressing the Escherichia coli enzyme in seeds, expression analysis during seed adevelopment
additional information
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construction of an enzyme-deficient null mutant strain CL112 by in-frame deletion of FabH active site region, the mutant strain requires unsaturated, but not saturated, long-chain fatty acids for growth, and retains about 10% of wild-type acetate incorporation and fatty acid synthesis activity leading to synthesis of branched-chain fatty acids, analysis of fatty acid content of the mutant strain, overview
additional information
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construction of an enzyme-deficient null mutant strain CL112 by in-frame deletion of FabH active site region, the mutant strain requires unsaturated, but not saturated, long-chain fatty acids for growth, and retains about 10% of wild-type acetate incorporation and fatty acid synthesis activity leading to synthesis of branched-chain fatty acids, analysis of fatty acid content of the mutant strain, overview
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additional information
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transfections with Cuphea glaucescens isozymes KAS III-1 and KAS III-2 or the spinach enzyme lead to altered fatty acid levels with accumulation of palmitate
additional information
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mutagenic replacement of the chromosomal endogenous enzyme by a plasmid-encoded Escherichia coli enzyme leads to a highly altered fatty acid profile in Streptomyces coelicolor, while plasmid-encoded expression of the Streptomyces glaucescens enzyme alters the fatty acid profile only slightly, overview
additional information
the Synechococcus FabH is used for replacement of its counterpart in the reconstituted Escherichia coli fatty acid synthase system, the resulting complex is strongly limited in FabH activity. The introduction of the Escherichia coli FabH enzyme into the Synechococcus fatty acid synthase system virtually eliminates its dependence on the FabH subunit
additional information
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the Synechococcus FabH is used for replacement of its counterpart in the reconstituted Escherichia coli fatty acid synthase system, the resulting complex is strongly limited in FabH activity. The introduction of the Escherichia coli FabH enzyme into the Synechococcus fatty acid synthase system virtually eliminates its dependence on the FabH subunit
