title: Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis.
abstract: Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A(2) . Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitor-enzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.
authors.affiliation: Department of Pharmacy, National University of Singapore, Singapore.
authors.forename: Tse Siang
authors.initials: TS
authors.lastname: Kang
authors.forename: Dessislava
authors.initials: D
authors.lastname: Georgieva
authors.forename: Nikolay
authors.initials: N
authors.lastname: Genov
authors.forename: Mário T
authors.initials: MT
authors.lastname: Murakami
authors.forename: Mau
authors.initials: M
authors.lastname: Sinha
authors.forename: Ramasamy P
authors.initials: RP
authors.lastname: Kumar
authors.forename: Punit
authors.initials: P
authors.lastname: Kaur
authors.forename: Sanjit
authors.initials: S
authors.lastname: Kumar
authors.forename: Sharmistha
authors.initials: S
authors.lastname: Dey
authors.forename: Sujata
authors.initials: S
authors.lastname: Sharma
authors.forename: Alice
authors.initials: A
authors.lastname: Vrielink
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
authors.forename: Soichi
authors.initials: S
authors.lastname: Takeda
authors.forename: Raghuvir K
authors.initials: RK
authors.lastname: Arni
authors.forename: Tej P
authors.initials: TP
authors.lastname: Singh
authors.forename: R Manjunatha
authors.initials: RM
authors.lastname: Kini
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D055162:Biocatalysis; D020134:Catalytic Domain; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D004789:Enzyme Activation; D006801:Humans; D050830:L-Amino Acid Oxidase / Q000737:chemistry / Q000378:metabolism; D045726:Metalloproteases / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D064801:Phospholipase A2 Inhibitors; D054467:Phospholipases A2 / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D012910:Snake Venoms / Q000737:chemistry* / Q000201:enzymology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D002800:Cholinesterase Inhibitors; D064801:Phospholipase A2 Inhibitors; D012910:Snake Venoms; D050830:L-Amino Acid Oxidase; D054467:Phospholipases A2; D000110:Acetylcholinesterase; D045726:Metalloproteases