Using a synthetic oligopeptide (d -Phe)4 , a microorganismBacillus cereusDF4-B producing alkaline d -peptidase (ADP) was isolated. The enzymatic properties have been characterized; the enzyme showed d -stereospecific dipeptidyl aminopeptidase and endopeptidase activities. The enzyme was active toward (d -Phe)n, Boc-(d -Phe)n, (d -Phe)nmethyl ester, d -Phe-NH2 , Boc-(d -Phe)nmethyl ester, and Boc-(d -Phe)ntert-butyl ester, but not toward (d -Ala)n(n= 2–4), (d -Val)3 , and (d -Leu)2 .