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

Alkaline phosphomonoesterase, phosphodiesterase, L-amino acid oxidase, hyaluronidase, 5'-nucleotidase, arginine ester hydrolase, phospholipase A2 and proteinase activities were determined in eight snake venoms, including three from sea snake, of families Elapidae and Viperidae from Pakistan. The species includes three sea snakes Hydrophis cyanocinctus, Enhydrina schsitosa, Microcephalophis gracilis gracilis and two land snakes Naja naja naja, Bungarus caeruleus of family Elapidae while three land snakes Vipera russelli russelli, Echis carinatus and Eristocophis macmahoni of family Viperidae. The venoms of family Elapidae are characterized by low levels to traces of proteinase, L-amino acid oxidase and arginine ester hydrolase activities with the exception of Naja naja naja and a moderate to high levels of phospholipase A2 activities. The venoms of family Viperidae, on the other hand, are characterized by the presence of moderate to high levels of 5'-nucleotidase, proteinase, phosphodiesterase and phosphomonoesterase activities.
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PMID:Enzymatic activities of some snake venoms from families Elapidae and Viperidae. 1641 74

The isolation and characterization of individual snake venom components is important for a deeper understanding of the pathophysiology of envenomations, for improving the therapeutic procedures of patients, and it also opens possibilities for the discovery of novel toxins that might be useful as tools for understanding cellular and molecular processes. This review provides a summary of the different toxins that have been isolated and characterized from the venoms of Vipera lebetina (Macrovipera lebetina) subspecies Macrovipera lebetina cernovi, Macrovipera lebetina lebetina, Macrovipera lebetina obtusa, Macrovipera lebetina transmediterranea, Macrovipera lebetina turanica, the snake species causing the majority of human envenomings in Central Asia (Middle East) and North Africa. The venoms of these snakes contain proteins belonging to different families: Zn2+- metalloproteinases, serine proteinases, L-amino acid oxidase, 5'-nucleotidase, phosphodiesterase, phosphomonoesterase, nucleases, hyaluronidase, phospholipase A2, C-type lectin-like protein, disintegrin, DC-fragment, cystein-rich secretory protein, proteinase inhibitors, nerve growth factor (NGF), vascular endothelial growth factor (VEGF), low molecular weight peptides. Their main biochemical properties, toxic and pharmacological actions have been described. In this review we will provide an overview of the proteins and peptides from the venoms of M. lebetina subspecies, their biochemical, pharmacological and structural features and their role in snake venom toxinology. A lot of contributions have been made for better understandings of these venomous snakes, their venom, and their pharmacological effects. Many of these components are also fascinating models for drug design.
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PMID:Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies. 3047 10


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