Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.3.5 (
5'-nucleotidase
)
3,167
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
New
5'-nucleotidase
inhibitors named NF-86I, NF-86II were recently isolated from the seeds of Areca catechu L. NF-86I and NF86II showed inhibitory effects on the growth of Streptococcus mutans MT8148(c) and Streptococcus mutans MT6715(g), respectively. In addition, these inhibitors could inhibit insoluble
glucan
formation from sucrose. NF-86I and NF-86II were found to be polyphenolic substances. Some polyphenols such as tannic acid bind non-specifically to proteins (tannic activity). The
5'-nucleotidase
inhibitors that we isolated did not show any such activity. However, the growth inhibitory activity and the inhibitory effect on water-insoluble
glucan
production were equal to tannic acid. It is therefore considered that these inhibitors bind specifically to the bacterial cell surface. Our findings suggest that the
5'-nucleotidase
inhibitors NF-86I and NF-86II may be useful anti-plaque preventing agents.
...
PMID:The growth inhibition of Streptococcus mutans by 5'-nucleotidase inhibitors from Areca catechu L. 191 9
New
5'-nucleotidase
inhibitors designated as NPF-88BU-IA, NPF-88BU-IB, NPF-88BU-IIA and NPF-88BU-IIB, respectively, were isolated from the seeds and skin of the wine grape "Koshu". They were purified by solvent extraction, dialysis, and reversed-phase high performance liquid chromatography (HPLC). Their physico-chemical properties revealed these compounds to be polyphenolic substances. The average relative molecular masses of the four were estimated by gel permeation chromatography (GPC) analysis to be 7850, 5950, 11900, and 11300, respectively. They strongly inhibited
5'-nucleotidase
activities from snake venom and rat liver membrane, and displayed significant therapeutic activity against Ehrlich ascites carcinoma. They also showed inhibitory effects on the growth of Streptococcus mutans MT8148(c), a primary cariogenic bacterium. Furthermore, these
5'-nucleotidase
inhibitors inhibited the
glucan
formation from sucrose. These results suggest that the
5'-nucleotidase
inhibitors can prevent the cause of caries of tooth.
...
PMID:New polyphenolic 5'-nucleotidase inhibitors isolated from the wine grape "Koshu" and their biological effects. 193 68
The two clinically important classes of antimycotic drugs, the polyenes and azoles, act on the plasma membrane of the cell. The primary modes of action are believed to be through interaction with sterols (polyenes) and alteration in sterol composition of the membrane (azoles). In this report we show that, at growth inhibitory concentrations, the polyenes (nystatin and amphotericin) and azoles (miconazole and ketoconazole) also inhibit plasma membrane enzymes. There was extensive (greater than 75%) inhibition of the Candida albicans plasma membrane enzymes ATPase, glucan synthase, adenyl cyclase and
5'-nucleotidase
, when assayed in situ. The antifungals papulacandin and echinocandin, which inhibit
glucan
synthesis, also inhibited plasma membrane enzymes in situ; glucan synthase (greater than 90%),
5'-nucleotidase
(greater than 80%) and ATPase (70-80%). Purified plasma membrane was prepared from yeast cells of C. albicans by two different techniques: concanavalin A stabilization and coating of spheroplasts with silica microbeads. In the purified plasma membrane vesicles prepared from concanavalin A the adenyl cyclase and phosphodiesterase were extensively (greater than 90%) inhibited by the three different classes of antifungal drugs; variable inhibition was observed with ATPase (70-100%). The 3',5'-cyclic phosphodiesterase of the plasma membrane purified by the microbeads method was almost completely inhibited by all of the antifungals tested and there was partial inhibition of ATPase (20-85%) and adenyl cyclase (30-90%).
...
PMID:The effects of azole and polyene antifungals on the plasma membrane enzymes of Candida albicans. 283 Mar 94