Tetralysine endopeptidase activity in a cell-free extract of Escherichia coli AJ005.
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.
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Department of Biochemical Science, Frick Chemical Laboratory, Princeton University, New Jersey 08540.
D010450:Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D008239:Lysine / Q000378:metabolism; D013379:Substrate Specificity
D010450:Endopeptidases; C068307:tetralysine endopeptidase; D008239:Lysine