Biomaterial Database

[Snake venom metalloproteinases: structure, biosynthesis and function(s)]. 2010

I Limam, and M El Ayeb, and N Marrakchi

Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13, Place Pasteur, 1002 Tunis Belvédère, Tunisia.

The biochemical and the pharmacological characterization of snake venoms revealed an important structural and functional polymorphism of proteins which they contain. Among them, snake venom metalloproteases (SVMPs) constitute approximatively 20 to 60% of the whole venom proteins. During the last decades, a significant progress was performed against structure studies and the biosynthesis of the SVMPs. Indeed, several metalloproteases were isolated and characterized against their structural and pharmacological properties. In this review, we report the most important properties concerning the classification, the structure of the various domains of the SVMPs as well as their biosynthesis and their activities as potential therapeutic agents.

UI	MeSH Term	Description	Entries
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012910	Snake Venoms	Solutions or mixtures of toxic and nontoxic substances elaborated by snake (Ophidia) salivary glands (Duvernoy's gland) for the purpose of killing prey or disabling predators and delivered by grooved or hollow fangs. They usually contain enzymes, toxins, and other factors.	Duvernoy's Gland Secretion,Duvernoy's Secretion,Snake Toxin,Snake Toxins,Snake Venom,Duvernoy Gland Secretion,Duvernoy Secretion,Duvernoys Gland Secretion,Duvernoys Secretion,Secretion, Duvernoy's,Secretion, Duvernoy's Gland,Toxin, Snake,Venom, Snake
D017434	Protein Structure, Tertiary	The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.	Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D045726	Metalloproteases	Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.	Metallopeptidase,Metalloprotease,Metalloproteinase,Metalloproteinases,Metallopeptidases