A pH- and Co(2+)-dependent dipeptidase from Escherichia coli.
The pH dependency of a Co(2+)-dependent dipeptidase from Escherichia coli AJ005, a peptidase-deficient mutant strain K12, was examined with purified dipeptidase, which was about 106-fold in specific activity. The peptidase had a very sharp optimal pH at 7.5. It is suggested that the peptidase plays an important role in the process of cell division and growth.
Department of Biochemical Sciences, Frick Chemical Laboratory, Princeton University, New Jersey 08540.
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D003035:Cobalt / Q000378:metabolism*; D004150:Dipeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration
D003035:Cobalt; D004150:Dipeptidases; C038937:dipeptidase