Identification and Characterization of FabA from the Type II Fatty Acid Synthase of Streptomyces coelicolor
Sponsor
This work was supported by a grant from the National Institutes of Health (GM 077147).
Published In
Joural of Natrual Products
Document Type
Citation
Publication Date
1-5-2016
Abstract
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.
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DOI
10.1021/acs.jnatprod.5b00560
Persistent Identifier
http://archives.pdx.edu/ds/psu/18846
Citation Details
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