Purification and characterization of the indole-3-glycerolphosphate synthase/anthranilate synthase complex of Saccharomyces cerevisiae.
The indole-3-glycerolphosphate synthase/anthranilate synthase complex from Saccharomyces cerevisiae was purified to apparent homogeneity. The native complex with Mr approximately equal to 130 000 consists of two different subunits, the TRP2 gene product with Mr = 64 000 and the TRP3 gene product with Mr = 58 000. The larger polypeptide was identified as anthranilate synthase and is active in vitro with ammonia as cosubstrate without need of complex formation. The smaller polypeptide carries both glutamine amidotransferase activity and indole-3-glycerolphosphate synthase activity. Various steady-state kinetic parameters as well as the amino acid composition of the two polypeptides were determined.
D000596:Amino Acids / Q000032:analysis; D000878:Anthranilate Synthase / Q000235:genetics / Q000302:isolation & purification*; D002262:Carboxy-Lyases / Q000302:isolation & purification*; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D007209:Indole-3-Glycerol-Phosphate Synthase / Q000235:genetics / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D000596:Amino Acids; D002262:Carboxy-Lyases; D007209:Indole-3-Glycerol-Phosphate Synthase; D000878:Anthranilate Synthase