Arogenate dehydrogenase from Streptomyces phaeochromogenes. Purification and properties.
Arogenate dehydrogenase, the terminal enzyme of tyrosine biosynthesis in Streptomyces phaeochromogenes, was purified to homogeneity by a five-step procedure. The enzyme is a dimer of Mr 57 600 as determined by dodecyl sulfate polyacrylamide gel electrophoresis after cross-linking of the monomers, or of 66 300 as found by gel permeation chromatography, and consists of two identical subunits of Mr 28 100. The pI of the enzyme is 4.45, and the Km values are 0.105mM for arogenate and 0.01 mM for NAD.
D000645:Ammonium Sulfate; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D010088:Oxidoreductases / Q000032:analysis / Q000302:isolation & purification*; D011303:Prephenate Dehydrogenase; D012967:Sodium Dodecyl Sulfate; D013302:Streptomyces / Q000201:enzymology*
D012967:Sodium Dodecyl Sulfate; D010088:Oxidoreductases; D011303:Prephenate Dehydrogenase; C027017:cyclohexadienyl dehydrogenase; D000645:Ammonium Sulfate