Characterization of a novel ADPase in Bothrops jararaca snake venom involved in nucleotide hydrolysis.
Snake venoms hydrolyze several phosphorylated substrates. However, not is clearly understood which enzyme(s) is (are) involved in these process. Here, we propose the existence of an independent ADPase activity. In addition, we studied the reactions mechanism of nucleotide hydrolysis. This system resembles membrane ecto-nucleotidases and acts with a multi enzymatic complex transforming ATP in adenosine without the accumulation of intermediates.
Teixeira-Ferreira
André
A
Laboratório de Química e Função de Proteínas e Peptídeos, Universidade Estadual do Norte Fluminense, Avenida Alberto Lamego 2000, Campos dos Goytacazes, RJ, Brazil.
Alves
Elias Walter
EW
D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001081:Apyrase / Q000378:metabolism*; D017837:Bothrops; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000201:enzymology*; D007700:Kinetics; D053858:Metabolic Networks and Pathways; D009711:Nucleotides / Q000378:metabolism*
D003435:Crotalid Venoms; D009711:Nucleotides; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D001081:Apyrase