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.
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Department of Biochemical Sciences, Frick Chemical Laboratory, Princeton University, New Jersey 08540.
D003035:Cobalt / Q000378:metabolism*; D004150:Dipeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration
D003035:Cobalt; D004150:Dipeptidases; C038937:dipeptidase