Identification and Characterization of FabA from the Type II Fatty Acid Synthase of Streptomyces coelicolor

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.

DOI

10.1021/acs.jnatprod.5b00560

Persistent Identifier

http://archives.pdx.edu/ds/psu/18846

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