title: Purification and partial amino acid sequence of the cyanogen bromide fragments of muconolactone isomerase from Pseudomonas putida.
abstract: Muconolactone isomerase is shown to be resistant to proteolytic cleavage by trypsin. Cyanogen bromide cleavage at the methionine residues of the polypeptide is at least 95% complete. Six cyanogen bromide fragments are separated on DEAE-cellulose. One fragment is shown by amino acid analysis and carboxyl-terminal analysis to be an incomplete cleavage product. The five remaining fragments represent the entire polypeptide and have been ordered with respect to the entire muconolactone isomerase sequence. Approximately 50% of the polypeptide sequence could be determined from these fragments by the dansyl-Edman technique. The possible evolutionarily homologous origins of muconolactone isomerase and two analogous isomerases, carboxymuconolactone decarboxylase and sigma5-3-ketosteroid isomerase, are discussed.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003488:Cyanogen Bromide; D007535:Isomerases / Q000032:analysis*; D007664:Ketosteroids; D010455:Peptides / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology
chemical_list: D000596:Amino Acids; D007664:Ketosteroids; D010455:Peptides; D007535:Isomerases; D003488:Cyanogen Bromide