alexa Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom.
Microbiology

Microbiology

Journal of Microbial & Biochemical Technology

Author(s): Ponnudurai G, Chung MC, Tan NH

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Abstract The L-amino acid oxidase of Malayan pit viper (Calloselasma rhodostoma) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was 132,000 as determined by Sephadex G-200 gel filtration chromatography and 66,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It is a glycoprotein, has an isoelectric point of 4.4, and contains 2 mol of flavin mononucleotide per mole of enzyme. The N-terminal amino acid sequence of the enzyme was A-D-D-R-N-P-L-A-E-E-F-Q-E-N-N-Y-E-E-F-L. Kinetic studies suggest the presence of a alkyl side-chain binding site in the enzyme and that the binding site comprises at least four hydrophobic subsites. The characteristics of the binding site differ slightly from those of cobra venom L-amino acid oxidases. This article was published in Arch Biochem Biophys and referenced in Journal of Microbial & Biochemical Technology

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