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40 PROCEEDINGS OF INTERNATIONAL SCIENTIFIC CONFERENCE ON APPLIED BIOTECHNOLOGYmake the analogs of herboxidiene with better activity compared to parent compound, a loss of function mutation of herboxidiene PKS was designed. In this study, we examined a novel analog of herboxidiene by engineering the reducing domain module 8 of herboxidiene PKS. It was found that the loss of function mutation of module 8 DH is not enough to avoid the formation of THP ring as herboxidiene was still formed in reduced concentration from the mutant strain. One of three new peaks found during the HPLC chromatogram comparison between module 8 DH mutated strain of S. chromofuscus and wild - type strain were purified and their study based on LC and HR-QTOF mass analysis resulted in the prediction of open ring analogs of herboxidiene. Further studies regarding structural elucidation of a compound produced by 8 DH mutated strain of S. chromofuscusby 2D NMR and completion of other reducing domain loss of function mutation is still in process. Keywords: Herboxidiene, polyketide synthase, dehydratase domains, Streptomyces chromofuscus1. INTRODUCTIONHerboxidiene, also known as GEX1A, is a polyketide named for its structural and biological characteristics, specifically its tetrahydropyran acetic acid moiety and conjugated diene system [1]. Since its identification in 1992, herboxidiene has been effectively utilized as herbicide, anti-cholesterol agent, and anti - tumor compound. Originally reported in 1991 by Monsanto Agricultural Company, herboxidiene was noted as a highly potent and selective herbicide produced by S. chromofuscus A7847, demonstrating effectiveness against various weed species [2, 3].