2.3.1.281: 5-hydroxydodecatetraenal polyketide synthase
This is an abbreviated version!
For detailed information about 5-hydroxydodecatetraenal polyketide synthase, go to the full flat file.
Reaction
6 malonyl-CoA + 5 NADPH + + 6 H+ = + 6 CoA + 5 NADP+ + + 6 CO2 + 4 H2O
Synonyms
cpkAB
ECTree
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General Information
General Information on EC 2.3.1.281 - 5-hydroxydodecatetraenal polyketide synthase
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physiological function
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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
physiological function
the synthase consists of a loading module, five extension modules and a reductase as a terminal domain instead of a typical thioesterase. All acyltransferase domains are specific for a malonyl extender, and have a B-type ketoreductase. A gene disruption mutant does not exhibit any morphological, growth or antibiotic production (actinorhodin and undecyloprodigiosin) differences compared to the wild type, and no difference in antibacterial activity is observed as well as in the UV-Vis absorbance
physiological function
-
the synthase consists of a loading module, five extension modules and a reductase as a terminal domain instead of a typical thioesterase. All acyltransferase domains are specific for a malonyl extender, and have a B-type ketoreductase. A gene disruption mutant does not exhibit any morphological, growth or antibiotic production (actinorhodin and undecyloprodigiosin) differences compared to the wild type, and no difference in antibacterial activity is observed as well as in the UV-Vis absorbance
-
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
-