Coronado, Mônika Aparecida [UNESP]da Silva Olivier, Danilo [UNESP]Eberle, Raphael Josef [UNESP]do Amaral, Marcos SerrouArni, Raghuvir Krishnaswamy [UNESP]2018-12-112018-12-112018-10-01Toxicon, v. 153, p. 106-113.1879-31500041-0101http://hdl.handle.net/11449/176812Phospholipase-B-like (SVPLB-like) enzymes are present in relatively small amounts in a number of venoms, however, their biological function and mechanisms of action are un-clear. A three-dimensional model of the SVPLB-like enzyme from Crotalus adamanteus was generated by homology modeling based on the crystal structures of bovine Ntn-hydrolyases and the modeled protein possesses conserved domains characteristic of Ntn-hydrolases. Molecular dynamics simulations indicate that activation by autocatalytic cleavage results in the removal of 25 amino acids which increases accessibility to the active site. SVPLB-like enzymes possess a highly reactive cysteine and are hence amidases that to belong to the N-terminal nucleophile (Ntn) hydrolase family. The Ntn-hydrolases (N-terminal nucleophile) form a superfamily of diverse enzymes that are activated autocatalytically; wherein the N-terminal catalytic nucleophile is implicated in the cleavage of the amide bond.106-113engCrotalus adamanteusMolecular dynamicsMolecular modelingNtn-hydrolaseSnake venom phospholipase BResenha10.1016/j.toxicon.2018.08.014Acesso aberto2-s2.0-850529676922-s2.0-85052967692.pdf91625089789458870000-0003-2460-1145