L-Amino Acid Oxidase from Crotalus adamanteus

L-Amino acid oxidase (LAAO) is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70 kDa. Each molecule of holoenzyme has two flavin adenine dinucleotide (FAD) molecules. LAAO is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. optimum pH is approximately 7.5. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney. In the N-terminal region, it has a βαβ domain with glutamic acid residues. LAAO imparts yellow color to venom.

L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays. The enzyme has been immobilized and used in an enzymatic flow-injection procedure with chemiluminescence detection for on-site determination of L-alanine.

L-Amino Acid Oxidase from Crotalus adamanteus has been used in the quantification of rid protein in imine deaminase activity.

L-Amino acid oxidase (LAAO) from Crotalus adamanteus requires Mg²⁺ for its activation. The N-terminal region is essential for FAD binding. The H₂O₂ generated by LAAO based oxidation reactions lead to prevention of platelet aggregation and induces edema and apoptosis. LAAO activity is inhibited by ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF).

Dissolves in water at 1 mg/mL concentration to form a clear solution.