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Literature summary for 2.3.1.281 extracted from

  • Awodi, U.; Ronan, J.; Masschelein, J.; De Los Santos, E.; Challis, G.
    Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis (2016), Chem. Sci., 8, 411-415 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.281

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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Streptomyces coelicolor M145
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6 malonyl-CoA + 5 NADPH + NADH + 6 H+
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 Streptomyces coelicolor (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
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 ?
6 malonyl-CoA + 5 NADPH + NADH + 6 H+
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 Streptomyces coelicolor M145 (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
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 ?
additional information the isolated subunit CpkC reduces octanoyl-CoA to octanal and further to 1-octanol in presence of NADH Streptomyces coelicolor ?
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 ?
additional information the isolated subunit CpkC reduces octanoyl-CoA to octanal and further to 1-octanol in presence of NADH Streptomyces coelicolor M145 ?
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 ?

General Information

General Information Comment Organism
physiological function the C-terminal thioester reductase domain of the PKS and an omega-transaminase are responsible for release of the polyketide chain as an aldehyde and its subsequent reductive amination Streptomyces coelicolor