Primary structure of the snake venom L-amino acid ...[Biochem Biophys Res Commun. 1998]

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1: Biochem Biophys Res Commun. 1998 Jul 30;248(3):476-8. Links

Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein.

Raibekas AA, Massey V.

Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-0606, USA.

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.

PMID: 9703950 [PubMed - indexed for MEDLINE]

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Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from Western diamondback rattlesnake venom. [J Biol Chem. 1997]
Characterization of the human homolog of the IL-4 induced gene-1 (Fig1). [Biochim Biophys Acta. 2002]
ReviewSnake venom L-amino acid oxidases. [Toxicon. 2002]
ReviewBiochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme. [Toxicon. 1996]

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Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein.

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