title: Tetralysine endopeptidase activity in a cell-free extract of Escherichia coli AJ005.
abstract: The activity of tetralysine endopeptidase was examined with cell-free extracts of Escherichia coli AJ005. The peptidase activity of cell-free extracts increased as the concentration became higher, and reached its maximum at about 30 mg protein/ml. The peptidase activity was stable and maintained most of its activity throughout a 5 h period of observation during incubation at 35 degrees C.
authors: Department of Biochemical Science, Frick Chemical Laboratory, Princeton University, New Jersey 08540.
authors: A
authors: A
authors: Ota
mesh_terms: D010450:Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D008239:Lysine / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D010450:Endopeptidases; C068307:tetralysine endopeptidase; D008239:Lysine