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 2002 |
| Externally published | Yes |
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Keywords
- Dichloro-(2,2′:6′,2″-terpyridine)
- Phospholipase D
- Platinum (II) dihydrate
- Streptomyces
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Organic Chemistry
- Drug Discovery
Cite this
Inhibition of Streptomyces chromofuscus phospholipase D activity by dichloro-(2,2′ : 6′,2″-terpyridine)-platinum (II) dihydrate. / Kubota-Akizawa, Megumi; Negishi, Tomofumi; Mori, Koichi; Hatanaka, Tadashi.
In: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 17, No. 5, 10.2002, p. 329-332.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Inhibition of Streptomyces chromofuscus phospholipase D activity by dichloro-(2,2′
T2 - 6′,2″-terpyridine)-platinum (II) dihydrate
AU - Kubota-Akizawa, Megumi
AU - Negishi, Tomofumi
AU - Mori, Koichi
AU - Hatanaka, Tadashi
PY - 2002/10
Y1 - 2002/10
N2 - 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.
AB - 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.
KW - Dichloro-(2,2′:6′,2″-terpyridine)
KW - Phospholipase D
KW - Platinum (II) dihydrate
KW - Streptomyces
UR - http://www.scopus.com/inward/record.url?scp=0036817728&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036817728&partnerID=8YFLogxK
U2 - 10.1080/1475636021000033252
DO - 10.1080/1475636021000033252
M3 - Article
VL - 17
SP - 329
EP - 332
JO - Journal of Enzyme Inhibition and Medicinal Chemistry
JF - Journal of Enzyme Inhibition and Medicinal Chemistry
SN - 1475-6366
IS - 5
ER -