Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom.
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.
Ponnudurai
G
G
Department of Biochemistry, University of Malaya, Kuala Lumpur.
Chung
M C
MC
Tan
N H
NH
D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D007525:Isoelectric Focusing; D050830:L-Amino Acid Oxidase; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D013379:Substrate Specificity; D014757:Viper Venoms; D017819:Viperidae
D000596:Amino Acids; D010446:Peptide Fragments; D014757:Viper Venoms; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase