Asano Yasuhisa
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Toyama, Japan.
Methods Mol Biol. 2012;794:397-406. doi: 10.1007/978-1-61779-331-8_27.
Using a synthetic oligopeptide (D-Phe)(4), a microorganism Bacillus cereus DF4-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)(n) methyl ester, D-Phe-NH(2), Boc-(D-Phe)(n) methyl ester, and Boc-(D-Phe)(n) tert-butyl ester, but not toward (D-Ala)(n) (n = 2-4), (D-Val)(3), and (D-Leu)(2).
