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Literature summary for 6.2.1.3 extracted from

  • Kang, Y.; Zarzycki-Siek, J.; Walton, C.B.; Norris, M.H.; Hoang, T.T.
    Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa (2010), PLoS ONE, 5, e13557.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene fadD1, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site for fadD1 Pseudomonas aeruginosa
gene fadD2, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site fadD1 Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
additional information construction of fadD1 mutants, phenotype, overview Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HYU3 FadD2; gene FadD2
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Pseudomonas aeruginosa Q9HYU4 FadD1; gene FadD1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids Pseudomonas aeruginosa ?
-
?

Subunits

Subunits Comment Organism
More FadDs contain ATP/AMP signature and FA-binding motifs Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
Acyl-CoA synthetase
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Pseudomonas aeruginosa
FAdD
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Pseudomonas aeruginosa

General Information

General Information Comment Organism
malfunction when compared to the wild-type strain, the fadD2 mutant exhibits decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant shows only increased swarming motility. Growth analysis of the fadD mutants show noticeable deficiencies in utilizing fatty acids and phosphatidylcholine as the sole carbon source, altered swimming and swarming motility of fadD mutants Pseudomonas aeruginosa