Identification and partial purification of a dipeptidyl aminopeptidase from Streptococcus faecalis

B. A. White, D. B. Clewell

Research output: Contribution to journalArticlepeer-review

Abstract

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 140000. 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.

Original languageEnglish (US)
Pages (from-to)1269-1276
Number of pages8
JournalJournal of General Microbiology
Volume132
Issue number5
DOIs
StatePublished - 1986

ASJC Scopus subject areas

  • Microbiology

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