Aromatic amino acid biosynthesis in Alcaligenes eutrophus H 16 III. Properites and regulation of anthranilate synthase.
Properties and regulation of anthranilate synthase from Alcaligenes eutrophus H 16 were investigated. Anthranilate synthase was partially purified from crude extracts by affinity chromatography on tryptophan-substituted Sepharose, and was used for kinetic measurements. During the purification procedure the enzyme was stabilized by 50 mM L-glutamine or during chromatography on DEAE- cellulose and Sephadex G-200 with 30% glucerol, respectively.
D000421:Alcaligenes / Q000201:enzymology*; D000494:Allosteric Regulation; D000877:Anthranilate Phosphoribosyltransferase; D000878:Anthranilate Synthase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009097:Multienzyme Complexes; D013696:Temperature; D014364:Tryptophan / Q000096:biosynthesis / Q000494:pharmacology
D009097:Multienzyme Complexes; D014364:Tryptophan; D000877:Anthranilate Phosphoribosyltransferase; D000878:Anthranilate Synthase