Inhibition of Streptomyces chromofuscus phospholipase D activity by dichloro-(2,2′:6′,2″-terpyridine)-platinum (II) dihydrate

Megumi Kubota-Akizawa, Tomofumi Negishi, Koichi Mori, Tadashi Hatanaka

Research output: Contribution to journalArticle

1 Citation (Scopus)


To determine the catalytic site of Streptomyces chromofuscus phospholipase D (PLD), which lacks an HKD motif, we examined the effects of inhibitors on the hydrolytic activity of the PLD by comparing it with cabbage and Streptomyces PLDs, which have two HKD motifs. We showed that dichloro-(2,2′:6′,2″-terpyridine)-platinum (II) dihydrate, a His- and Cys-directed chemical modifier, had inhibitory effects on the activities of all types of PLD examined. On the other hand, N-ethylmaleimide, a thiol-directed modifier had no such effects on PLD activity. These results suggest that the His residue plays an important role in the activity of Streptomyces chromofuscus PLD.

Original languageEnglish
Pages (from-to)329-332
Number of pages4
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Issue number5
Publication statusPublished - Oct 1 2002



  • Dichloro-(2,2′:6′,2″-terpyridine)
  • Phospholipase D
  • Platinum (II) dihydrate
  • Streptomyces

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

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