RT Journal Article SR Electronic(1) A1 White, Bryan A. A1 Clewell, Don B.YR 1986 T1 Identification and Partial Purification of a Dipeptidyl Aminopeptidase from Streptococcus faecalis JF Microbiology, VO 132 IS 5 SP 1269 OP 1276 DO https://doi.org/10.1099/00221287-132-5-1269 PB Microbiology Society, SN 1465-2080, AB A dipeptidyl aminopeptidase was identified in Streptococcus faecalis JH2SS and was partially purified (approximately 245-fold) by HPLC. Gel filtration chromatography indicated an M r of 140 000. The partially purified enzyme exhibited a requirement for Co2+. The pH optimum for the hydrolysis of l-Val-l-Ala-p-nitroanilide was approximately 9·5. The apparent K m for this substrate was 0·22 mm. The enzyme preferentially hydrolysed X-Ala-Y substrates, but also utilized X-Pro-Y substrates, and therefore is most closely related to the mammalian dipeptidyl aminopeptidase II (EC 3.4.14.-). The enzyme was inhibited by p-chloromercuribenzoate, but not by iodoacetate, N-ethylmaleimide or the serine protease inhibitor phenylmethylsulphonyl fluoride., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-132-5-1269