Abstract
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 language | English |
|---|---|
| Pages (from-to) | 329-332 |
| Number of pages | 4 |
| Journal | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Volume | 17 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - Oct 1 2002 |
| Externally published | Yes |
Keywords
- Dichloro-(2,2′:6′,2″-terpyridine)
- Phospholipase D
- Platinum (II) dihydrate
- Streptomyces
ASJC Scopus subject areas
- Pharmacology
- Drug Discovery
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Cite this
Kubota-Akizawa, M., Negishi, T., Mori, K., & Hatanaka, T. (2002). Inhibition of Streptomyces chromofuscus phospholipase D activity by dichloro-(2,2′:6′,2″-terpyridine)-platinum (II) dihydrate. Journal of Enzyme Inhibition and Medicinal Chemistry, 17(5), 329-332. https://doi.org/10.1080/1475636021000033252