title: Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities.
abstract: On the basis of amino acid composition, tryptic fingerprints and the determination of amino acid sequences around the four cysteine residues, it can be concluded that chorismate mutase/prephenate dehydratase from Escherichia coli K12 consists of identical, or closely similar subunits. It follows from this that the mutase and dehydratase activities of the enzyme are probably catalysed on the one subunit.
mesh_terms: D000595:Amino Acid Sequence; D002384:Catalysis; D002827:Chorismic Acid / Q000378:metabolism; D003545:Cysteine / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology; D006836:Hydro-Lyases / Q000032:analysis*; D010455:Peptides / Q000302:isolation & purification; D011302:Prephenate Dehydratase / Q000032:analysis*; D014357:Trypsin
chemical_list: D010455:Peptides; D014357:Trypsin; D006836:Hydro-Lyases; D011302:Prephenate Dehydratase; D002827:Chorismic Acid; D003545:Cysteine