Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein.
The 2.8-kb sequence of cDNA encoding southeastern diamondback rattlesnake venom L-amino acid oxidase was determined. A translated single open reading frame revealed a 58.7-kDa polypeptide containing a signal sequence and FAD binding motif. The protein similarity search and analysis showed that the snake L-amino acid oxidase possesses the highest degree of homology (37% of identity) with a protein encoded by the mouse B cell interleukin 4-induced Fig1 gene.
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-0606, USA.
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Raibekas
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Massey
D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003435:Crotalid Venoms; D017839:Crotalus; D005420:Flavoproteins / Q000096:biosynthesis / Q000737:chemistry*; D050830:L-Amino Acid Oxidase; D051379:Mice; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D003435:Crotalid Venoms; D005420:Flavoproteins; D021382:Protein Sorting Signals; D000594:Amino Acid Oxidoreductases; C484538:Il4i1 protein, mouse; D050830:L-Amino Acid Oxidase