Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved.
Snake venom glands synthesize a variety of serine proteinases capable of affecting the haemostatic system. They act on macromolecular substrates of the coagulation, fibrinolytic, and kallikrein-kinin systems, and on platelets to cause an imbalance of the haemostatic system of the prey. In this review we describe their biochemical/biophysical characteristics, biological activities as well as aspects of their evolution and structure-activity relationship.
Serrano
Solange M T
SM
Laboratório Especial de Toxinologia Aplicada-CAT-CEPID, Instituto Butantan, Av. Vital Brasil 1500, 05503-900 São Paulo-SP, Brazil. solangeserrano@butantangov.br
Maroun
Rachid C
RC
D000595:Amino Acid Sequence; D000818:Animals; D001777:Blood Coagulation / Q000502:physiology*; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000378:metabolism; D012910:Snake Venoms / Q000201:enzymology*; D012911:Snakes; D013379:Substrate Specificity / Q000235:genetics
D015842:Serine Proteinase Inhibitors; D012910:Snake Venoms; D012697:Serine Endopeptidases