Identification and Characterization of FabA from the Type II Fatty Acid Synthase of Streptomyces coelicolor
This work was supported by a grant from the National Institutes of Health (GM 077147).
Joural of Natrual Products
FabA is proposed to catalyze the dehydration step of chain elongation in fatty acid and undecylprodiginine biosynthesis in Streptomyces coelicolor. Analysis of the S. coelicolor genome has revealed a fabA gene (SCO4636-SCO4637, encoding a heterodimer 3-hydroxyacyl-ACP dehydratase). Herein, we report the identification and characterization of the corresponding gene products. Kinetic analysis has demonstrated that FabA is capable of utilizing various chain lengths of straight- and branched-chain 3-hydroxyacyl-NAC substrates. Additionally, FabA does not discriminate between acyl carrier proteins (ACPs) from primary and secondary metabolism. These data provide the first experimental evidence that FabA has 3-hydroxyacyl-ACP dehydratase activity and processes intermediates for both biosynthetic pathways.
Locate the Document
Singh, R., & Reynolds, K. A. (2016). Identification and Characterization of FabA from the Type II Fatty Acid Synthase of Streptomyces coelicolor. Journal of Natural Products,79(1), 240–3. http://doi.org/10.1021/acs.jnatprod.5b00560