Abstract
Publisher Summary p -Aminobenzoate synthase catalyzes the first specific reaction in the folic acid biosynthetic pathway, that is, the formation of p -aminobenzoate (PABA) from chorismate and glutamine. PABA is also a likely intermediate in the biosynthesis of candicidin by Streptomyces griseus. This chapter describes the assay and some properties of PABA synthase from E. coli and B. subtilis , along with the purification of B. subtilis subunit “G.” B. subtilis PABA synthase subunit G also functions with AS I in the synthesis of anthranilate. In the purification procedure for B. subtilis subunit G, PABA synthase subunit G is isolated in association with anthranilate synthase component I (AS I) and is then further purified as isolated subunit G. For this purification, glutamine-dependent anthranilate synthase is used to assay subunit G in the presence of excess AS I. The purification procedure consists of several steps—preparation of extract, ammonium sulfate precipitation, gel filtration, diethylaminoethyl (DEAE)-sephadex chromatography, and preparative polyacrylamide gel electrophoresis.
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