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Fig. 3 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 3

From: Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Fig. 3

Multiple sequential alignment of snake venom L-amino acid oxidases from the genus Crotalus. Initial N-terminal of bordonein-L [Swiss-Prot: C0HJE7, bottom] and LAAOs from crotalic venoms: C. adamanteus [Swiss-Prot: F8S0Z5, O93364], C. atrox [Swiss-Prot: P56742], C. horridus [Swiss-Prot: T1DJZ4], C. d. cumanensis [Swiss-Prot: K9N7B7 – fragment] and C. d. cascavella [Swiss-Prot: P0C2D2 – fragment]. The highly conserved residues in bordonein-L are highlighted in black. The amino acid residues in red indicate low consensus. Cys residues are shaded in blue. The alignment and figure were generated by the servers MultAlin [52] and ESPript [53], respectively

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