Information on EC 2.3.1.207 - beta-ketodecanoyl-[acyl-carrier-protein] synthase

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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

EC NUMBER
COMMENTARY hide
2.3.1.207
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RECOMMENDED NAME
GeneOntology No.
beta-ketodecanoyl-[acyl-carrier-protein] synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid salvage
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)
This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via beta-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for beta-oxidation degradation intermediates into de novo fatty acid biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fabY, i.e. orf PA3286
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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FabY belongs to the KASIII domain containing enzymes
malfunction
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the fabY deletion strain grows slowly in comparison to the fabHEc exchange control without C10 supplementation
metabolism
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the KASIII domain-containing enzyme FabY from open reading frame PA3286 shunts fatty acid degradation intermediates from the beta-oxidation pathway by condensing octanoyl-CoA with malonyl-ACP to make beta-keto-decanoyl-ACP, a key building block common to saturated fatty acids, unsaturated fatty acids, and lipopolysaccharides
physiological function
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FabY, a beta-ketoacyl synthase KASI/II domain-containing enzyme that condenses acetyl-CoA with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis, FAS, primer beta-acetoacetyl-ACP. FabY is an enzyme required for FAS initiation in the absence of exogenous fatty acids
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
show the reaction diagram
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PA3286 specifically shunts C8-CoA in vivo
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PA3286 protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of orf PA3286 in Escherichia coli strain BL21(DE3) as His-tagged protein, expression of PA3286 gene in Escherichia coli strain BW25113
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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gene fabY is replaced with fabH (pTMT123) or deleted (pTMT124) in Pseudomonas aeruginosa strain PAO1. The fabY deletion strain grows slowly in comparison to the fabHEc exchange control without C10 supplementation, synthetic lethal analysis for fabY with KASIII domain fabH orthologues and fatty acid rescue, overview. The fabY deletion is synthetic lethal when introduced into the KASIII domain knockout strain TMT16. Synthetic lethal relationship between PA3286 and fabY indicates shared acetyl-CoA:malonyl-ACP condensing activity. PA3286 cross complements fabH and confers a fatty acid shunt in Escherichia coli