Heliquinomycin was isolated as a part of a program designed to find inhibitors of DNAhelicase from microbial sources. It was purified from the culture broth of Streptomyces sp. MJ929-SF2by solvent extraction and serial chromatographies of centrifugal partition chromatography, Sephadex LH-20 and Capcell Pak C18 (HPLC). The isolated red powder was analyzed to have the molecular formula of C33H30O17. It inhibited partially purified DNAhelicase from HeLa cell in a noncompetitive manner with the inhibition constant (Ki) of 6.8 mM. Heliquinomycin exhibited biological activity against microorganisms including MRSA,and cultured cell lines. DNAhelicase is essential in the processes of DNA replication, repair, recombination and transcription by unwinding of double-stranded DNAto its reactive single strand form. This is an energy requiring process driven by the hydrolysis of deoxynucleaside S'-triphosphate1*. All knownDNAhelicases have been found to process intrinsic DNA-dependent ATPase activity2~4). DNAhelicase was discovered for the first time in 1976 in E. coli5). Most of the DNAhelicases need SSDNA adjacent to the duplex region to be unwound, with the notable exception of the SV40 T antigen6), E. coli helicase7), and E. coli Rec8) which are also able to

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