Biosynthesis of chloramphenicol in Streptomyces sp. 3022a. Identification of p-amino-L-phenylalanine as a product from the action of arylamine synthetase on chorismic acid.
Products obtained from the action of arylamine synthetase on [G-14C]chorismic acid were fractionated by gel filtration and ion exchange column chromatography to yield a partially purified radioactive component with an arylamine function. From its ultraviolet absorption spectrum and thin-layer chromatographic behaviour the product was considered to be p-aminophenylalanine and the identification was confirmed by co-crystallization with an authentic specimen. Specific deamination of the product with L-amino-acid oxidase indicated that it was the L-epimer. These results strengthen previous evidence that arylamine synthetase is at a branch point in the shikimic acid pathway, specifically diverting intermediates to the synthesis of chloramphenicol.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism; D002474:Cell-Free System; D002701:Chloramphenicol / Q000096:biosynthesis*; D002827:Chorismic Acid / Q000378:metabolism*; D003509:Cyclohexanecarboxylic Acids / Q000378:metabolism*; D003605:D-Amino-Acid Oxidase / Q000378:metabolism; D009097:Multienzyme Complexes / Q000378:metabolism*; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000096:biosynthesis; D013237:Stereoisomerism; D013302:Streptomyces / Q000201:enzymology / Q000378:metabolism*
D003509:Cyclohexanecarboxylic Acids; D009097:Multienzyme Complexes; D010649:Phenylalanine; C019733:arylamine synthetase; D002701:Chloramphenicol; D000594:Amino Acid Oxidoreductases; D003605:D-Amino-Acid Oxidase; D002827:Chorismic Acid