Isolation of a bifunctional domain from the pentafunctional arom enzyme complex of Neurospora crassa.
Limited proteolysis of the arom enzyme complex of Neurospora crassa by trypsin or subtilisin yielded a stable fragment of Mr 68000. This fragment, which was purified by two-dimensional polyacrylamide-gel electrophoresis, was shown by activity staining to contain the shikimate dehydrogenase active site, and by substrate labelling with 3-dehydroquinate and NaB3H4 to contain the 3-dehydroquinase active site. The fragment thus constitutes a bifunctional domain containing the two enzymic activities that are known, from genetic evidence, to be located adjacently at the C-terminal end of the pentafunctional arom polypeptide.
D000429:Alcohol Oxidoreductases; D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006836:Hydro-Lyases / Q000302:isolation & purification; D008024:Ligands; D008190:Lyases; D008956:Models, Chemical; D009097:Multienzyme Complexes / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D010455:Peptides / Q000032:analysis; D017853:Phosphotransferases (Alcohol Group Acceptor); D013381:Subtilisins; D014166:Transferases; D014357:Trypsin
D008024:Ligands; D009097:Multienzyme Complexes; D010455:Peptides; C019728:arom enzyme; D000429:Alcohol Oxidoreductases; D014166:Transferases; D017853:Phosphotransferases (Alcohol Group Acceptor); D013381:Subtilisins; D014357:Trypsin; D008190:Lyases; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase