Previous studies indicate that the naphthoate moiety of the azinomycins is polyketide synthase (PKS) derived.  However, when the holo-PKS was expressed, 2-methylbenzoic acid was detected rather than the naphthoate precursor, 5-methylnaphthoic acid.  The detection of 2-methylbenzoic acid (10 ppm error) following the expression of the PKS and aziG thioesterase (TE) domain suggests that a TE domain is required for naphthalene ring formation.  In order to confirm this, the synthesis of 5-methylnaphthoic acid is described here.Cancer cells can utilize glucose carbons more quickly for nucleic acid and lipid syntheses.  Because these processes are dependent on thiamin-based enzymes, the enzymatic breakdown of thiamin via thiaminase I is a viable approach for disrupting cancer cell proliferation.  This study describes the cloning of thiaminase into E. coli.  The cloned vector will ultimately be transfected into liver cancer cells under a cancer specific promoter to further investigate its potential use in targeted cancer therapy.

Synthesis of the azinomycin naphthoate and cloning of thiaminase

245th National Meeting (2013)

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