Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ecto-5'-nucleotidase (ecto-5'-NUC, EC 3.1.3.5., CD73) is a plasma membrane enzyme, which catalyzes the hydrolytic dephosphorylation of purine nucleotides to the corresponding nucleosides so that they can pass through the plasma membrane. The distribution of ecto-5'-NUC is heterogeneous, but all blood mononuclear cell (BMC) subpopulations investigated until now have had ecto-5'-NUC activity. Purified natural killer (NK) cells were prepared by fluorescence-activated cell sorting of CD16-positive cells (purity 94%). In purified NK cells the ecto-5'-NUC activity was less than 1 U/10(6) as estimated by a radioisotope method. Using a cytochemical assay, the proportion of cells with activity was less than 1%. The most likely explanation is that NK cells have no ecto-5'-NUC activity and that the very small ecto-5'-NUC activity observed in this study was caused by contaminating non-NK cells. NK cells thus constitute the only BMC subset known without ecto-5'-NUC activity.
 ...
PMID:Natural killer cells lack ecto-5'-nucleotidase. 153 54

The activities of five clinically important enzymes of purine metabolism have been determined in lymphocytes from 62 patients with various types of solid tumors. The activity of purine nucleoside phosphorylase was increased in all patient groups studied, i.e. small cell bronchogenic carcinoma (n = 30), carcinoma of the breast (n = 17) and other tumors (n = 15), compared to cells form normal donors. Activities of adenosine deaminase, adenine phosphoribosyltransferase (APRT), hypoxanthine (guanine) phosphoribosyltransferase (HGPRT), and 5'-nucleotidase (5'-NUC) vary little from control values, except for lower levels of APRT in lymphocytes from patients with carcinoma of the breast. In patients with small cell bronchogenic carcinoma, enzyme levels were also determined in granulocytes, where increased APRT activity was found. Following cytostatic treatment of these patients, significant decreases were seen in lymphocytic HGPRT and 5'-NUC activities.
 ...
PMID:Purine metabolizing enzymes in lymphocytes from patients with solid tumors. 632 Jun 1

Snake venom 5'-nucleotidase (5'NUC) plays a very important role in envenomation strategies; however, apart from its modulation of hemostatic functions, its other pharmacological effects are not yet well characterized. Several studies have used specific inhibitors of enzyme toxins as a biochemical or pharmacological tool to characterize or establish its mechanism of action. We report here for the first time vanillin mandelic acid (VMA), an analog of vanillin, to potentially, selectively, and specifically inhibit venom 5'NUC activity among other enzymes present in venoms. VMA is much more potent in inhibiting 5'NUC activity than vanillyl acid (VA). The experimental results obtained are in good agreement with the in silico molecular docking interaction data. Both VA and VMA are competitive inhibitors as evident by the inhibition-relieving effect upon increasing the substrate concentration. VMA also dose-dependently inhibited the anticoagulant effect in Naja naja venom. In this study, we report novel non-nucleoside specific inhibitors of snake venom 5'NUC and experimentally demonstrate their involvement in the anticoagulant activity of N. naja venom. Hence, we hypothesize that VMA can be used as a molecular tool to evaluate the role of 5'NUC in snake envenomation and to develop prototypes and lead compounds with potential therapeutic applications against snake bites.
...
PMID:Vanillin analog--vanillyl mandelic acid, a novel specific inhibitor of snake venom 5'-nucleotidase. 2504 67