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Literature summary for 2.3.1.207 extracted from

  • Yuan, Y.; Leeds, J.; Meredith, T.
    Pseudomonas aeruginosa directly shunts beta-oxidation degradation intermediates into de novo fatty acid biosynthesis (2012), J. Bacteriol., 194, 5185-5196.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.207

Cloned(Commentary)

Cloned (Comment) Organism
expression of orf PA3286 in Escherichia coli strain BL21(DE3) as His-tagged protein, expression of PA3286 gene in Escherichia coli strain BW25113 Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
additional information 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 Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
octanoyl-CoA + malonyl-[acyl-carrier protein] Pseudomonas aeruginosa PA3286 specifically shunts C8-CoA in vivo 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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 fabY, i.e. orf PA3286
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged PA3286 protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
octanoyl-CoA + malonyl-[acyl-carrier protein]
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 Pseudomonas aeruginosa 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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 ?
octanoyl-CoA + malonyl-[acyl-carrier protein] PA3286 specifically shunts C8-CoA in vivo Pseudomonas aeruginosa 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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 ?

Synonyms

Synonyms Comment Organism
beta-ketoacyl synthase
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 Pseudomonas aeruginosa
FabY
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 Pseudomonas aeruginosa
PA3286 protein
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 Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution FabY belongs to the KASIII domain containing enzymes Pseudomonas aeruginosa
malfunction the fabY deletion strain grows slowly in comparison to the fabHEc exchange control without C10 supplementation Pseudomonas aeruginosa
metabolism 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 Pseudomonas aeruginosa
physiological function 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 Pseudomonas aeruginosa