Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization.
Phenylalanine hydroxylase was purified approximately 3000-fold to apparent homogeneity with a 13% yield and crystalized from L-phenylalanine-induced cells of Chromobacterium violaceum. The enzyme was shown to be composed of a single polypeptide chain with an estimated molecular weight of approximately 32,000. Some of the physical properties of the enzyme include: a Stokes radius of 26.0 A, a sedimentation coefficient of 2.71 S, a diffusion coefficient of 8.20 X 10(-7) CM2/S, a frictional ratio of 1.23, and an isoelectric point of pH 4.5. No detectable iron was found in the purified enzyme. Apparent Km values for L-phenylalanine and 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine were 140 and 54 muM, respectively.
D002384:Catalysis; D002861:Chromobacterium / Q000201:enzymology*; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000032:analysis; D007700:Kinetics; D008970:Molecular Weight; D010649:Phenylalanine / Q000494:pharmacology; D010651:Phenylalanine Hydroxylase / Q000302:isolation & purification* / Q000378:metabolism
D010649:Phenylalanine; D007501:Iron; D010651:Phenylalanine Hydroxylase