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Further Studies of the d-Aspartic Acid-activating Enzyme of Streptococcus faecalis and Its Attachment to the Membrane

From the ¹ From the Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138

The d-aspartic acid-activating enzyme of Streptococcus faecalis is found both in the supernatant solution and bound to the membrane. Under the gentlest conditions of lysis, virtually all of the enzyme is on the membrane fraction. When the enzyme is prepared from the supernatant fraction, it has a higher molecular weight than when it is prepared from the membrane, but it can be disaggregated by treatment with salt. Both preparations can be rebound to saltdepleted membranes under certain conditions. Both preparations also contain d-aspartyltransferase activity which can transfer aspartic acid from ß-d-aspartyl phosphate (the presumed intermediate) either to a uridine nucleotide acceptor or to a lipid intermediate in peptidoglycan synthesis. The transferase and the activating enzyme have not been separated so far.

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