This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyses the first reaction in the biosynthesis of coelimycin P1. The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains. An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyses the reductive release of the product.
The expected taxonomic range for this enzyme is: Streptomyces coelicolor
This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyses the first reaction in the biosynthesis of coelimycin P1. The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains. An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyses the reductive release of the product.
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
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
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
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